ID CK5P3_HUMAN Reviewed; 506 AA. AC Q96JB5; B7Z6N4; D3DTU1; D3DTU2; F5H3I5; Q53FA2; Q9H3F8; Q9H8G0; Q9HBR9; DT 16-JUN-2003, integrated into UniProtKB/Swiss-Prot. DT 16-JUN-2003, sequence version 2. DT 28-JAN-2026, entry version 196. DE RecName: Full=CDK5 regulatory subunit-associated protein 3 {ECO:0000305}; DE AltName: Full=CDK5 activator-binding protein C53 {ECO:0000305|PubMed:10721722}; DE AltName: Full=LXXLL/leucine-zipper-containing ARF-binding protein {ECO:0000303|PubMed:20164180}; DE AltName: Full=Protein HSF-27 {ECO:0000312|EMBL:AAK69655.1}; GN Name=CDK5RAP3 {ECO:0000303|PubMed:30635284, GN ECO:0000312|HGNC:HGNC:18673}; GN Synonyms=IC53 {ECO:0000303|PubMed:20164180}, LZAP GN {ECO:0000303|PubMed:20164180}; ORFNames=MSTP016, OK/SW-cl.114, PP1553; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), AND TISSUE SPECIFICITY. RC TISSUE=Aorta; RX PubMed=12054757; DOI=10.1016/s0006-291x(02)00446-1; RA Chen J., Liu B., Liu Y.Q., Han Y., Yu H., Zhang Y., Lu L., Zhen Y., RA Hui R.T.; RT "A novel gene IC53 stimulates ECV304 cell proliferation and is upregulated RT in failing heart."; RL Biochem. Biophys. Res. Commun. 294:161-166(2002). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), INTERACTION WITH CDK5R1, AND TISSUE RP SPECIFICITY. RC TISSUE=Placenta; RX PubMed=12737517; DOI=10.1038/sj.cr.7290153; RA Xie Y.H., He X.H., Tang Y.T., Li J.J., Pan Z.M., Qin W.X., Wan da F., RA Gu J.R.; RT "Cloning and characterization of human IC53-2, a novel CDK5 activator RT binding protein."; RL Cell Res. 13:83-91(2003). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). RC TISSUE=Kidney; RA Favier A.-L., Harsi C., Chrobozcek J.; RT "Protein interacting with the receptor binding domain of enteric adenovirus RT serotype 41 fiber protein."; RL Submitted (JAN-2001) to the EMBL/GenBank/DDBJ databases. RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Colon adenocarcinoma; RA Shichijo S., Itoh K.; RT "Identification of immuno-peptidmics that are recognized by tumor-reactive RT CTL generated from TIL of colon cancer patients."; RL Submitted (MAY-2001) to the EMBL/GenBank/DDBJ databases. RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 4). RC TISSUE=Placenta, and Rectum; RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., RA Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Synovial cell; RA Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.; RL Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases. RN [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., RA Hunkapiller M.W., Myers E.W., Venter J.C.; RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases. RN [8] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16625196; DOI=10.1038/nature04689; RA Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R., RA Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A., RA Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J., RA Chang J.L., Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J., RA DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S., RA Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E., RA Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K., RA LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J., RA Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A., RA Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K., RA Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D., RA Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A., RA Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.; RT "DNA sequence of human chromosome 17 and analysis of rearrangement in the RT human lineage."; RL Nature 440:1045-1049(2006). RN [9] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Brain; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA project: RT the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [10] RP TISSUE SPECIFICITY. RX PubMed=10721722; DOI=10.1016/s0378-1119(99)00499-0; RA Ching Y.-P., Qi Z., Wang J.H.; RT "Cloning of three novel neuronal Cdk5 activator binding proteins."; RL Gene 242:285-294(2000). RN [11] RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH CCNB1. RX PubMed=15790566; DOI=10.1074/jbc.m413431200; RA Jiang H., Luo S., Li H.; RT "Cdk5 activator-binding protein C53 regulates apoptosis induced by RT genotoxic stress via modulating the G2/M DNA damage checkpoint."; RL J. Biol. Chem. 280:20651-20659(2005). RN [12] RP FUNCTION, INTERACTION WITH CDKN2A/ARF AND MDM2, AND SUBCELLULAR LOCATION. RX PubMed=16173922; DOI=10.1042/bj20050960; RA Wang J., He X., Luo Y., Yarbrough W.G.; RT "A novel ARF-binding protein (LZAP) alters ARF regulation of HDM2."; RL Biochem. J. 393:489-501(2006). RN [13] RP FUNCTION, AND INTERACTION WITH RELA. RX PubMed=17785205; DOI=10.1016/j.ccr.2007.07.002; RA Wang J., An H., Mayo M.W., Baldwin A.S., Yarbrough W.G.; RT "LZAP, a putative tumor suppressor, selectively inhibits NF-kappaB."; RL Cancer Cell 12:239-251(2007). RN [14] RP FUNCTION, INTERACTION WITH CHEK1, REGION, AND SUBCELLULAR LOCATION. RX PubMed=19223857; DOI=10.1038/cr.2009.14; RA Jiang H., Wu J., He C., Yang W., Li H.; RT "Tumor suppressor protein C53 antagonizes checkpoint kinases to promote RT cyclin-dependent kinase 1 activation."; RL Cell Res. 19:458-468(2009). RN [15] RP INTERACTION WITH UFL1. RX PubMed=20164180; DOI=10.1074/jbc.m109.065920; RA Kwon J., Cho H.J., Han S.H., No J.G., Kwon J.Y., Kim H.; RT "A novel LZAP-binding protein, NLBP, inhibits cell invasion."; RL J. Biol. Chem. 285:12232-12240(2010). RN [16] RP FUNCTION, INTERACTION WITH DDRGK1 AND UFL1, REGION, AND UBIQUITINATION. RX PubMed=20228063; DOI=10.1074/jbc.m110.110619; RA Wu J., Lei G., Mei M., Tang Y., Li H.; RT "A novel C53/LZAP-interacting protein regulates stability of C53/LZAP and RT DDRGK domain-containing Protein 1 (DDRGK1) and modulates NF-kappaB RT signaling."; RL J. Biol. Chem. 285:15126-15136(2010). RN [17] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21269460; DOI=10.1186/1752-0509-5-17; RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., RA Bennett K.L., Superti-Furga G., Colinge J.; RT "Initial characterization of the human central proteome."; RL BMC Syst. Biol. 5:17-17(2011). RN [18] RP FUNCTION, AND INTERACTION WITH MAPK14. RX PubMed=21283629; DOI=10.1371/journal.pone.0016427; RA An H., Lu X., Liu D., Yarbrough W.G.; RT "LZAP inhibits p38 MAPK (p38) phosphorylation and activity by facilitating RT p38 association with the wild-type p53 induced phosphatase 1 (WIP1)."; RL PLoS ONE 6:E16427-E16427(2011). RN [19] RP INTERACTION WITH TUBG1. RX PubMed=21465471; DOI=10.1002/jcp.22772; RA Horejsi B., Vinopal S., Sladkova V., Draberova E., Sulimenko V., RA Sulimenko T., Vosecka V., Philimonenko A., Hozak P., Katsetos C.D., RA Draber P.; RT "Nuclear gamma-tubulin associates with nucleoli and interacts with tumor RT suppressor protein C53."; RL J. Cell. Physiol. 227:367-382(2012). RN [20] RP FUNCTION (MICROBIAL INFECTION), AND INTERACTION WITH HEPATITIS B VIRUS RP LARGE ENVELOPE PROTEIN. RX PubMed=21971960; DOI=10.3892/or.2011.1489; RA Lei Y., Liu H., Yang Y., Wang X., Ren N., Li B., Liu S., Cheng J., Fu X., RA Zhang J.; RT "Interaction of LHBs with C53 promotes hepatocyte mitotic entry: A novel RT mechanism for HBV-induced hepatocellular carcinoma."; RL Oncol. Rep. 27:151-159(2012). RN [21] RP FUNCTION. RX PubMed=23152784; DOI=10.1371/journal.pone.0048587; RA Zhang Y., Zhang M., Wu J., Lei G., Li H.; RT "Transcriptional regulation of the Ufm1 conjugation system in response to RT disturbance of the endoplasmic reticulum homeostasis and inhibition of RT vesicle trafficking."; RL PLoS ONE 7:E48587-E48587(2012). RN [22] RP FUNCTION, CLEAVAGE BY CASPASES, MUTAGENESIS OF ASP-268; ASP-282 AND RP ASP-311, AND SUBCELLULAR LOCATION. RX PubMed=23478299; DOI=10.1038/cr.2013.36; RA Wu J., Jiang H., Luo S., Zhang M., Zhang Y., Sun F., Huang S., Li H.; RT "Caspase-mediated cleavage of C53/LZAP protein causes abnormal microtubule RT bundling and rupture of the nuclear envelope."; RL Cell Res. 23:691-704(2013). RN [23] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014; RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., RA Ye M., Zou H.; RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver RT phosphoproteome."; RL J. Proteomics 96:253-262(2014). RN [24] RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-450, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=25772364; DOI=10.1016/j.celrep.2015.02.033; RA Hendriks I.A., Treffers L.W., Verlaan-de Vries M., Olsen J.V., RA Vertegaal A.C.; RT "SUMO-2 orchestrates chromatin modifiers in response to DNA damage."; RL Cell Rep. 10:1778-1791(2015). RN [25] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=25944712; DOI=10.1002/pmic.201400617; RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D., RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.; RT "N-terminome analysis of the human mitochondrial proteome."; RL Proteomics 15:2519-2524(2015). RN [26] RP FUNCTION. RX PubMed=30635284; DOI=10.1242/dev.169235; RA Yang R., Wang H., Kang B., Chen B., Shi Y., Yang S., Sun L., Liu Y., RA Xiao W., Zhang T., Yang J., Zhang Y., Zhu M., Xu P., Chang Y., Jia Y., RA Huang Y.; RT "CDK5RAP3, a UFL1 substrate adaptor, is crucial for liver development."; RL Development 146:0-0(2019). RN [27] RP FUNCTION, IDENTIFICATION IN THE UREL COMPLEX, INTERACTION WITH GABARAP AND RP GABARAPL1, AND DOMAIN. RX PubMed=32851973; DOI=10.7554/elife.58396; RA Stephani M., Picchianti L., Gajic A., Beveridge R., Skarwan E., RA Sanchez de Medina Hernandez V., Mohseni A., Clavel M., Zeng Y., Naumann C., RA Matuszkiewicz M., Turco E., Loefke C., Li B., Duernberger G., RA Schutzbier M., Chen H.T., Abdrakhmanov A., Savova A., Chia K.S., Djamei A., RA Schaffner I., Abel S., Jiang L., Mechtler K., Ikeda F., Martens S., RA Clausen T., Dagdas Y.; RT "A cross-kingdom conserved ER-phagy receptor maintains endoplasmic RT reticulum homeostasis during stress."; RL Elife 9:0-0(2020). RN [28] RP FUNCTION, AND IDENTIFICATION IN THE UREL COMPLEX. RX PubMed=36121123; DOI=10.15252/embj.2022111015; RA Peter J.J., Magnussen H.M., DaRosa P.A., Millrine D., Matthews S.P., RA Lamoliatte F., Sundaramoorthy R., Kopito R.R., Kulathu Y.; RT "A non-canonical scaffold-type E3 ligase complex mediates protein RT UFMylation."; RL EMBO J. 41:e111015-e111015(2022). RN [29] RP FUNCTION, SUBCELLULAR LOCATION, IDENTIFICATION IN THE UREL COMPLEX, RP INTERACTION WITH MAP1LC3A; MAP1LC3B; GABARAP; GABARAPL1 AND GABARAPL2, AND RP MUTAGENESIS OF TRP-269; TRP-294 AND TRP-312. RX PubMed=36543799; DOI=10.1038/s41467-022-35501-0; RA Ishimura R., El-Gowily A.H., Noshiro D., Komatsu-Hirota S., Ono Y., RA Shindo M., Hatta T., Abe M., Uemura T., Lee-Okada H.C., Mohamed T.M., RA Yokomizo T., Ueno T., Sakimura K., Natsume T., Sorimachi H., Inada T., RA Waguri S., Noda N.N., Komatsu M.; RT "The UFM1 system regulates ER-phagy through the ufmylation of CYB5R3."; RL Nat. Commun. 13:7857-7857(2022). RN [30] RP INTERACTION WITH GABARAP, DOMAIN, AND MUTAGENESIS OF TRP-269; TRP-294 AND RP TRP-312. RX PubMed=36762703; DOI=10.15252/embj.2022112053; RA Picchianti L., Sanchez de Medina Hernandez V., Zhan N., Irwin N.A., RA Groh R., Stephani M., Hornegger H., Beveridge R., Sawa-Makarska J., RA Lendl T., Grujic N., Naumann C., Martens S., Richards T.A., Clausen T., RA Ramundo S., Karagoez G.E., Dagdas Y.; RT "Shuffled ATG8 interacting motifs form an ancestral bridge between RT UFMylation and autophagy."; RL EMBO J. 42:e112053-e112053(2023). RN [31] RP FUNCTION, IDENTIFICATION IN THE UREL COMPLEX, AND MUTAGENESIS OF GLU-217; RP ASP-355; GLU-359; GLU-373 AND ARG-432. RX PubMed=37595036; DOI=10.1126/sciadv.adh3635; RA Ishimura R., Ito S., Mao G., Komatsu-Hirota S., Inada T., Noda N.N., RA Komatsu M.; RT "Mechanistic insights into the roles of the UFM1 E3 ligase complex in RT ufmylation and ribosome-associated protein quality control."; RL Sci. Adv. 9:eadh3635-eadh3635(2023). RN [32] {ECO:0007744|PDB:8QFC} RP STRUCTURE BY ELECTRON MICROSCOPY (3.2 ANGSTROMS) IN COMPLEX WITH UFL1 AND RP RPL10A, FUNCTION, SUBCELLULAR LOCATION, IDENTIFICATION IN THE UREL COMPLEX, RP AND DOMAIN. RX PubMed=38383789; DOI=10.1038/s41586-024-07093-w; RA Makhlouf L., Peter J.J., Magnussen H.M., Thakur R., Millrine D., RA Minshull T.C., Harrison G., Varghese J., Lamoliatte F., Foglizzo M., RA Macartney T., Calabrese A.N., Zeqiraj E., Kulathu Y.; RT "The UFM1 E3 ligase recognizes and releases 60S ribosomes from ER RT translocons."; RL Nature 627:437-444(2024). RN [33] {ECO:0007744|PDB:8OHD, ECO:0007744|PDB:8OJ0, ECO:0007744|PDB:8OJ5} RP STRUCTURE BY ELECTRON MICROSCOPY (2.9 ANGSTROMS) OF THE UREL COMPLEX IN RP COMPLEX WITH THE 60S RIBOSOME, FUNCTION, SUBCELLULAR LOCATION, AND RP IDENTIFICATION IN THE UREL COMPLEX. RX PubMed=38383785; DOI=10.1038/s41586-024-07073-0; RA DaRosa P.A., Penchev I., Gumbin S.C., Scavone F., Wachalska M., Paulo J.A., RA Ordureau A., Peter J.J., Kulathu Y., Harper J.W., Becker T., Beckmann R., RA Kopito R.R.; RT "UFM1 E3 ligase promotes recycling of 60S ribosomal subunits from the ER."; RL Nature 627:445-452(2024). CC -!- FUNCTION: Substrate adapter of E3 ligase complexes mediating CC ufmylation, the covalent attachment of the ubiquitin-like modifier UFM1 CC to substrate proteins, and which is involved in various processes, such CC as ribosome recycling and reticulophagy (also called ER-phagy) CC (PubMed:23152784, PubMed:30635284, PubMed:32851973, PubMed:36121123, CC PubMed:36543799, PubMed:37595036, PubMed:38383785, PubMed:38383789). As CC part of the UREL complex, plays a key role in ribosome recycling by CC promoting mono-ufmylation of RPL26/uL24 subunit of the 60S ribosome CC (PubMed:38383785, PubMed:38383789). Ufmylation of RPL26/uL24 occurs on CC free 60S ribosomes following ribosome dissociation: it weakens the CC junction between post-termination 60S subunits and SEC61 translocons, CC promoting release and recycling of the large ribosomal subunit from the CC endoplasmic reticulum membrane (PubMed:38383785, PubMed:38383789). CC Ufmylation of RPL26/uL24 and subsequent 60S ribosome recycling either CC take place after normal termination of translation or after ribosome CC stalling during cotranslational translocation at the endoplasmic CC reticulum (PubMed:32851973, PubMed:37595036, PubMed:38383785, CC PubMed:38383789). Within the UREL complex, CDK5RAP3 acts as a substrate CC adapter that constrains UFL1 ligase activity to mono-ufmylate CC RPL26/uL24 at 'Lys-134' (PubMed:36121123, PubMed:38383785, CC PubMed:38383789). The UREL complex is also involved in reticulophagy in CC response to endoplasmic reticulum stress by promoting ufmylation of CC proteins such as CYB5R3, thereby promoting lysosomal degradation of CC ufmylated proteins (PubMed:36543799). Also acts as a regulator of CC transcription: negatively regulates NF-kappa-B-mediated gene CC transcription through the control of RELA phosphorylation CC (PubMed:17785205, PubMed:20228063). Also regulates mitotic G2/M CC transition checkpoint and mitotic G2 DNA damage checkpoint CC (PubMed:15790566, PubMed:19223857). Through its interaction with CC CDKN2A/ARF and MDM2 may induce MDM2-dependent p53/TP53 ubiquitination, CC stabilization and activation in the nucleus, thereby promoting G1 cell CC cycle arrest and inhibition of cell proliferation (PubMed:16173922). CC May also play a role in the rupture of the nuclear envelope during CC apoptosis (PubMed:23478299). May regulate MAPK14 activity by regulating CC its dephosphorylation by PPM1D/WIP1 (PubMed:21283629). Required for CC liver development (By similarity). {ECO:0000250|UniProtKB:Q99LM2, CC ECO:0000269|PubMed:15790566, ECO:0000269|PubMed:16173922, CC ECO:0000269|PubMed:17785205, ECO:0000269|PubMed:19223857, CC ECO:0000269|PubMed:20228063, ECO:0000269|PubMed:21283629, CC ECO:0000269|PubMed:23152784, ECO:0000269|PubMed:23478299, CC ECO:0000269|PubMed:30635284, ECO:0000269|PubMed:32851973, CC ECO:0000269|PubMed:36121123, ECO:0000269|PubMed:36543799, CC ECO:0000269|PubMed:37595036, ECO:0000269|PubMed:38383785, CC ECO:0000269|PubMed:38383789}. CC -!- FUNCTION: (Microbial infection) May be negatively regulated by CC hepatitis B virus large envelope protein mutant pre-s2 to promote CC mitotic entry. {ECO:0000269|PubMed:21971960}. CC -!- SUBUNIT: Substrate adapter component of the UFM1 ribosome E3 ligase CC (UREL) complex, composed of UFL1, DDRGK1 and CDK5RAP3 (PubMed:20164180, CC PubMed:20228063, PubMed:32851973, PubMed:36121123, PubMed:36543799, CC PubMed:37595036, PubMed:38383785, PubMed:38383789). Interaction with CC UFL1 anchors CDK5RAP3 in the cytoplasm, preventing its translocation to CC the nucleus which allows expression of the CCND1 cyclin and progression CC of cells through the G1/S transition (By similarity). Interacts with CC ATG8 family proteins MAP1LC3A, MAP1LC3B, GABARAP, GABARAPL1 and CC GABARAPL2 (PubMed:32851973, PubMed:36543799, PubMed:36762703). CC Interacts with CDK5R1; competes with CDK5RAP1 and CDK5RAP2 CC (PubMed:12737517). Interacts with RELA (PubMed:17785205). Interacts CC with CHEK1; may negatively regulate CHEK1 and thereby stimulate entry CC into mitosis (PubMed:19223857). Interacts with CDKN2A/ARF and MDM2; CC forms a ternary complex involved in regulation of p53/TP53 CC (PubMed:16173922). Interacts with MAPK14 (PubMed:21283629). Interacts CC with CCNB1 (PubMed:15790566). Interacts with TUBG1; may regulate CC CDK5RAP3 in mitotic G2/M transition checkpoint (PubMed:21465471). CC {ECO:0000250|UniProtKB:Q9JLH7, ECO:0000269|PubMed:12737517, CC ECO:0000269|PubMed:15790566, ECO:0000269|PubMed:16173922, CC ECO:0000269|PubMed:17785205, ECO:0000269|PubMed:19223857, CC ECO:0000269|PubMed:20164180, ECO:0000269|PubMed:20228063, CC ECO:0000269|PubMed:21283629, ECO:0000269|PubMed:21465471, CC ECO:0000269|PubMed:32851973, ECO:0000269|PubMed:36121123, CC ECO:0000269|PubMed:36543799, ECO:0000269|PubMed:36762703, CC ECO:0000269|PubMed:37595036, ECO:0000269|PubMed:38383785, CC ECO:0000269|PubMed:38383789}. CC -!- SUBUNIT: (Microbial infection) Interacts with hepatitis B virus large CC envelope protein mutant pre-s2; promotes mitotic entry. CC {ECO:0000269|PubMed:21971960}. CC -!- INTERACTION: CC Q96JB5; Q96HY6: DDRGK1; NbExp=6; IntAct=EBI-718818, EBI-1054024; CC Q96JB5; O75344: FKBP6; NbExp=12; IntAct=EBI-718818, EBI-744771; CC Q96JB5; Q04206: RELA; NbExp=4; IntAct=EBI-718818, EBI-73886; CC Q96JB5; Q9Y5M8: SRPRB; NbExp=3; IntAct=EBI-718818, EBI-355393; CC Q96JB5; Q9UJ04: TSPYL4; NbExp=6; IntAct=EBI-718818, EBI-308511; CC Q96JB5; Q9Y3C8: UFC1; NbExp=8; IntAct=EBI-718818, EBI-1045733; CC Q96JB5; O94874: UFL1; NbExp=13; IntAct=EBI-718818, EBI-1048088; CC Q96JB5; P61960: UFM1; NbExp=4; IntAct=EBI-718818, EBI-1045061; CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane CC {ECO:0000269|PubMed:36543799, ECO:0000269|PubMed:38383785, CC ECO:0000269|PubMed:38383789}. Cytoplasm {ECO:0000269|PubMed:15790566, CC ECO:0000269|PubMed:16173922, ECO:0000269|PubMed:19223857}. Nucleus CC {ECO:0000269|PubMed:16173922}. Cytoplasm, cytoskeleton, microtubule CC organizing center, centrosome {ECO:0000269|PubMed:19223857}. Cytoplasm, CC cytoskeleton {ECO:0000269|PubMed:23478299}. Note=Tethered to the CC endoplasmic reticulum membrane as part of the UFM1 ribosome E3 ligase CC (UREL) complex (PubMed:38383785, PubMed:38383789). Colocalizes and CC associates with microtubules (PubMed:23478299). CC {ECO:0000269|PubMed:23478299, ECO:0000269|PubMed:38383785, CC ECO:0000269|PubMed:38383789}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=4; CC Name=1; CC IsoId=Q96JB5-1; Sequence=Displayed; CC Name=2; Synonyms=IC53; CC IsoId=Q96JB5-2; Sequence=VSP_007566, VSP_007567; CC Name=3; Synonyms=IC53-2; CC IsoId=Q96JB5-3; Sequence=VSP_007568; CC Name=4; CC IsoId=Q96JB5-4; Sequence=VSP_055646; CC -!- TISSUE SPECIFICITY: Ubiquitously expressed (PubMed:10721722, CC PubMed:12054757). Expressed in heart, brain, placenta, lung, liver, CC skeletal muscle, kidney and pancreas. Isoform 3 is expressed in kidney, CC liver, skeletal muscle and placenta (PubMed:12737517). CC {ECO:0000269|PubMed:10721722, ECO:0000269|PubMed:12054757, CC ECO:0000269|PubMed:12737517}. CC -!- DOMAIN: The shuffled ATG8-binding motifs mediate interaction with both CC ATG8 family protein and UFM1. {ECO:0000269|PubMed:32851973, CC ECO:0000269|PubMed:36762703}. CC -!- DOMAIN: The RPL10a-binding domain (RBD) anchors the UREL complex onto CC the ribosome via association with RPL10a/ul1. CC {ECO:0000269|PubMed:38383789}. CC -!- PTM: May be phosphorylated by CDK5. {ECO:0000250|UniProtKB:Q9JLH7}. CC -!- PTM: Ubiquitinated. Probably triggers proteasomal degradation and is CC negatively regulated by UFL1. {ECO:0000269|PubMed:20228063}. CC -!- PTM: May be ufmylated. {ECO:0000250|UniProtKB:Q99LM2}. CC -!- PTM: Cleaved by caspases early during apoptosis, the resulting peptides CC may play a role in rupture of the nuclear envelope. CC {ECO:0000269|PubMed:23478299}. CC -!- MISCELLANEOUS: [Isoform 2]: Due to an intron retention. {ECO:0000305}. CC -!- MISCELLANEOUS: [Isoform 3]: Due to intron retention. {ECO:0000305}. CC -!- SIMILARITY: Belongs to the CDK5RAP3 family. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=AAK69655.1; Type=Frameshift; Evidence={ECO:0000305}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AF110322; AAG39277.1; -; mRNA. DR EMBL; AF217982; AAG17225.1; -; mRNA. DR EMBL; AF343090; AAK69655.1; ALT_FRAME; mRNA. DR EMBL; AB062433; BAB93496.1; -; mRNA. DR EMBL; AK023722; BAB14657.1; -; mRNA. DR EMBL; AK300643; BAH13320.1; -; mRNA. DR EMBL; AK223387; BAD97107.1; -; mRNA. DR EMBL; AC018521; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471109; EAW94772.1; -; Genomic_DNA. DR EMBL; CH471109; EAW94774.1; -; Genomic_DNA. DR EMBL; CH471109; EAW94775.1; -; Genomic_DNA. DR EMBL; CH471109; EAW94778.1; -; Genomic_DNA. DR EMBL; BC009957; AAH09957.1; -; mRNA. DR EMBL; BC072435; AAH72435.1; -; mRNA. DR CCDS; CCDS42356.1; -. [Q96JB5-1] DR CCDS; CCDS62232.1; -. [Q96JB5-4] DR PIR; JC7863; JC7863. DR RefSeq; NP_001265126.1; NM_001278197.2. [Q96JB5-4] DR RefSeq; NP_001265127.1; NM_001278198.1. DR RefSeq; NP_001265145.1; NM_001278216.2. [Q96JB5-3] DR RefSeq; NP_001265146.1; NM_001278217.2. [Q96JB5-2] DR RefSeq; NP_788276.1; NM_176096.3. [Q96JB5-1] DR RefSeq; XP_011523599.1; XM_011525297.1. [Q96JB5-4] DR RefSeq; XP_054173383.1; XM_054317408.1. [Q96JB5-4] DR PDB; 8OHD; EM; 3.10 A; B=1-506. DR PDB; 8OJ0; EM; 3.30 A; B=1-506. DR PDB; 8OJ5; EM; 2.90 A; B=1-506. DR PDB; 8QFC; EM; 3.20 A; C=1-506. DR PDB; 9GY4; EM; 3.00 A; B=1-506. DR PDBsum; 8OHD; -. DR PDBsum; 8OJ0; -. DR PDBsum; 8OJ5; -. DR PDBsum; 8QFC; -. DR PDBsum; 9GY4; -. DR AlphaFoldDB; Q96JB5; -. DR EMDB; EMD-16880; -. DR EMDB; EMD-16902; -. DR EMDB; EMD-16905; -. DR EMDB; EMD-18381; -. DR EMDB; EMD-51681; -. DR SMR; Q96JB5; -. DR BioGRID; 123213; 192. DR ComplexPortal; CPX-8304; UFM1 ribosome E3 ligase complex. DR FunCoup; Q96JB5; 2347. DR IntAct; Q96JB5; 112. DR MINT; Q96JB5; -. DR STRING; 9606.ENSP00000438886; -. DR iPTMnet; Q96JB5; -. DR PhosphoSitePlus; Q96JB5; -. DR SwissPalm; Q96JB5; -. DR BioMuta; CDK5RAP3; -. DR DMDM; 32129444; -. DR jPOST; Q96JB5; -. DR MassIVE; Q96JB5; -. DR PaxDb; 9606-ENSP00000438886; -. DR PeptideAtlas; Q96JB5; -. DR ProteomicsDB; 26284; -. DR ProteomicsDB; 76930; -. [Q96JB5-1] DR ProteomicsDB; 76931; -. [Q96JB5-2] DR ProteomicsDB; 76932; -. [Q96JB5-3] DR Pumba; Q96JB5; -. DR Antibodypedia; 8591; 235 antibodies from 32 providers. DR DNASU; 80279; -. DR Ensembl; ENST00000338399.9; ENSP00000344683.4; ENSG00000108465.16. [Q96JB5-1] DR Ensembl; ENST00000536708.6; ENSP00000438886.2; ENSG00000108465.16. [Q96JB5-4] DR GeneID; 80279; -. DR KEGG; hsa:80279; -. DR MANE-Select; ENST00000338399.9; ENSP00000344683.4; NM_176096.3; NP_788276.1. DR UCSC; uc002imr.5; human. [Q96JB5-1] DR AGR; HGNC:18673; -. DR ClinPGx; PA38633; -. DR CTD; 80279; -. DR DisGeNET; 80279; -. DR GeneCards; CDK5RAP3; -. DR HGNC; HGNC:18673; CDK5RAP3. DR HPA; ENSG00000108465; Low tissue specificity. DR MIM; 608202; gene. DR OpenTargets; ENSG00000108465; -. DR VEuPathDB; HostDB:ENSG00000108465; -. DR eggNOG; KOG2607; Eukaryota. DR GeneTree; ENSGT00390000000713; -. DR HOGENOM; CLU_025645_1_0_1; -. DR InParanoid; Q96JB5; -. DR OMA; CRLYEKN; -. DR OrthoDB; 340432at2759; -. DR PAN-GO; Q96JB5; 2 GO annotations based on evolutionary models. DR PhylomeDB; Q96JB5; -. DR PathwayCommons; Q96JB5; -. DR SignaLink; Q96JB5; -. DR Agora; ENSG00000108465; -. DR BioGRID-ORCS; 80279; 61 hits in 1170 CRISPR screens. DR CD-CODE; 8C2F96ED; Centrosome. DR CD-CODE; FB4E32DD; Presynaptic clusters and postsynaptic densities. DR ChiTaRS; CDK5RAP3; human. DR GeneWiki; CDK5RAP3; -. DR GenomeRNAi; 80279; -. DR Pharos; Q96JB5; Tbio. DR PRO; PR:Q96JB5; -. DR Proteomes; UP000005640; Chromosome 17. DR RNAct; Q96JB5; protein. DR Bgee; ENSG00000108465; Expressed in pituitary gland and 93 other cell types or tissues. DR ExpressionAtlas; Q96JB5; baseline and differential. DR GO; GO:0005813; C:centrosome; IDA:UniProtKB. DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB. DR GO; GO:0005829; C:cytosol; IDA:HPA. DR GO; GO:0012505; C:endomembrane system; IBA:GO_Central. DR GO; GO:0005789; C:endoplasmic reticulum membrane; IDA:UniProtKB. DR GO; GO:0016020; C:membrane; HDA:UniProtKB. DR GO; GO:0005730; C:nucleolus; IDA:HPA. DR GO; GO:0005634; C:nucleus; IDA:UniProtKB. DR GO; GO:0032991; C:protein-containing complex; IDA:MGI. DR GO; GO:0030332; F:cyclin binding; IPI:UniProtKB. DR GO; GO:0097371; F:MDM2/MDM4 family protein binding; IPI:UniProtKB. DR GO; GO:0051019; F:mitogen-activated protein kinase binding; IPI:UniProtKB. DR GO; GO:0051059; F:NF-kappaB binding; IPI:UniProtKB. DR GO; GO:0019901; F:protein kinase binding; IPI:UniProtKB. DR GO; GO:1990756; F:ubiquitin-like ligase-substrate adaptor activity; IDA:UniProtKB. DR GO; GO:0044389; F:ubiquitin-like protein ligase binding; IDA:MGI. DR GO; GO:0030262; P:apoptotic nuclear changes; IMP:UniProtKB. DR GO; GO:0007420; P:brain development; NAS:UniProtKB. DR GO; GO:0008283; P:cell population proliferation; IDA:UniProtKB. DR GO; GO:0060318; P:definitive erythrocyte differentiation; ISS:UniProtKB. DR GO; GO:0030968; P:endoplasmic reticulum unfolded protein response; IMP:UniProtKB. DR GO; GO:0001889; P:liver development; ISS:UniProtKB. DR GO; GO:0007095; P:mitotic G2 DNA damage checkpoint signaling; IMP:UniProtKB. DR GO; GO:0044818; P:mitotic G2/M transition checkpoint; IMP:UniProtKB. DR GO; GO:0043407; P:negative regulation of MAP kinase activity; IMP:UniProtKB. DR GO; GO:0032088; P:negative regulation of NF-kappaB transcription factor activity; IMP:UniProtKB. DR GO; GO:0042177; P:negative regulation of protein catabolic process; IDA:UniProtKB. DR GO; GO:0044387; P:negative regulation of protein kinase activity by regulation of protein phosphorylation; IMP:UniProtKB. DR GO; GO:0001933; P:negative regulation of protein phosphorylation; IMP:UniProtKB. DR GO; GO:0071901; P:negative regulation of protein serine/threonine kinase activity; IMP:UniProtKB. DR GO; GO:1900182; P:positive regulation of protein localization to nucleus; IDA:UniProtKB. DR GO; GO:0031398; P:positive regulation of protein ubiquitination; IDA:UniProtKB. DR GO; GO:0140501; P:positive regulation of reticulophagy; IDA:UniProtKB. DR GO; GO:1901798; P:positive regulation of signal transduction by p53 class mediator; IDA:UniProtKB. DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IEA:Ensembl. DR GO; GO:0071569; P:protein ufmylation; IDA:UniProtKB. DR GO; GO:0000079; P:regulation of cyclin-dependent protein serine/threonine kinase activity; ISS:UniProtKB. DR GO; GO:0007346; P:regulation of mitotic cell cycle; IBA:GO_Central. DR GO; GO:0045664; P:regulation of neuron differentiation; NAS:UniProtKB. DR GO; GO:0010921; P:regulation of phosphatase activity; IMP:UniProtKB. DR GO; GO:0072344; P:rescue of stalled ribosome; IDA:UniProtKB. DR GO; GO:0034976; P:response to endoplasmic reticulum stress; ISS:UniProtKB. DR GO; GO:0032790; P:ribosome disassembly; IDA:UniProtKB. DR InterPro; IPR008491; CDK5RAP3. DR PANTHER; PTHR14894; CDK5 REGULATORY SUBUNIT-ASSOCIATED PROTEIN 3; 1. DR PANTHER; PTHR14894:SF0; CDK5 REGULATORY SUBUNIT-ASSOCIATED PROTEIN 3; 1. DR Pfam; PF05600; CDK5RAP3; 1. PE 1: Evidence at protein level; KW 3D-structure; Alternative splicing; Cytoplasm; Cytoskeleton; KW Endoplasmic reticulum; Host-virus interaction; Isopeptide bond; Membrane; KW Nucleus; Phosphoprotein; Proteomics identification; Reference proteome; KW Ubl conjugation; Ubl conjugation pathway. FT CHAIN 1..506 FT /note="CDK5 regulatory subunit-associated protein 3" FT /id="PRO_0000220516" FT REGION 269..506 FT /note="Required for interaction with UFL1 and mediates FT interaction with CHEK1" FT /evidence="ECO:0000269|PubMed:19223857, FT ECO:0000269|PubMed:20228063" FT REGION 355..370 FT /note="RPL10a-binding domain (RBD)" FT /evidence="ECO:0000269|PubMed:38383789" FT MOTIF 267..270 FT /note="Shuffled ATG8-binding motif 1" FT /evidence="ECO:0000269|PubMed:32851973, FT ECO:0000269|PubMed:36762703" FT MOTIF 292..295 FT /note="Shuffled ATG8-binding motif 2" FT /evidence="ECO:0000269|PubMed:32851973, FT ECO:0000269|PubMed:36762703" FT MOTIF 310..313 FT /note="Shuffled ATG8-binding motif 3" FT /evidence="ECO:0000269|PubMed:32851973, FT ECO:0000269|PubMed:36762703" FT CROSSLNK 450 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:25772364" FT VAR_SEQ 1..225 FT /note="Missing (in isoform 3)" FT /evidence="ECO:0000303|PubMed:12737517" FT /id="VSP_007568" FT VAR_SEQ 1..87 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:12054757" FT /id="VSP_007566" FT VAR_SEQ 1..2 FT /note="ME -> MRRQSMTSATRDLHTALDGKATQGGKK (in isoform 4)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_055646" FT VAR_SEQ 88..111 FT /note="RYSSQRMKDWQEIIALYEKDNTYL -> MCVHPGACLPHVGVSWAEFPGHFS FT (in isoform 2)" FT /evidence="ECO:0000303|PubMed:12054757" FT /id="VSP_007567" FT VARIANT 324 FT /note="L -> V (in dbSNP:rs35054799)" FT /id="VAR_048688" FT MUTAGEN 217 FT /note="E->A: Abolished interaction with UFL1; when FT associated with A-355, A-359, A-373 and A-432." FT /evidence="ECO:0000269|PubMed:37595036" FT MUTAGEN 268 FT /note="D->E: Alters cleavage by CASP3 in vitro. Prevents FT apoptosis-induced cleavage in vivo; when associated with FT E-282 and E-311." FT /evidence="ECO:0000269|PubMed:23478299" FT MUTAGEN 269 FT /note="W->A: Abolished interaction with ATG8 family FT proteins; when associated with A-294 and A-312." FT /evidence="ECO:0000269|PubMed:36543799, FT ECO:0000269|PubMed:36762703" FT MUTAGEN 282 FT /note="D->E: Alters cleavage by CASP3 in vitro. Prevents FT apoptosis-induced cleavage in vivo; when associated with FT E-268 and E-311." FT /evidence="ECO:0000269|PubMed:23478299" FT MUTAGEN 294 FT /note="W->A: Abolished interaction with ATG8 family FT proteins; when associated with A-269 and A-312." FT /evidence="ECO:0000269|PubMed:36543799, FT ECO:0000269|PubMed:36762703" FT MUTAGEN 311 FT /note="D->E: Alters cleavage by CASP3 in vitro. Prevents FT apoptosis-induced cleavage in vivo; when associated with FT E-268 and E-282." FT /evidence="ECO:0000269|PubMed:23478299" FT MUTAGEN 312 FT /note="W->A: Abolished interaction with ATG8 family FT proteins; when associated with A-269 and A-294." FT /evidence="ECO:0000269|PubMed:36543799, FT ECO:0000269|PubMed:36762703" FT MUTAGEN 355 FT /note="D->A: Abolished interaction with UFL1; when FT associated with A-355, A-359, A-373 and A-432." FT /evidence="ECO:0000269|PubMed:37595036" FT MUTAGEN 359 FT /note="E->A: Abolished interaction with UFL1; when FT associated with A-217, A-355, A-373 and A-432." FT /evidence="ECO:0000269|PubMed:37595036" FT MUTAGEN 373 FT /note="E->A: Abolished interaction with UFL1; when FT associated with A-217, A-355, A-359 and A-432." FT /evidence="ECO:0000269|PubMed:37595036" FT MUTAGEN 432 FT /note="R->A: Abolished interaction with UFL1; when FT associated with A-217, A-355, A-359 and A-373." FT /evidence="ECO:0000269|PubMed:37595036" FT CONFLICT 98 FT /note="Q -> R (in Ref. 5; BAH13320)" FT /evidence="ECO:0000305" FT CONFLICT 113 FT /note="E -> V (in Ref. 6; BAD97107)" FT /evidence="ECO:0000305" FT CONFLICT 406 FT /note="E -> K (in Ref. 3; AAK69655)" FT /evidence="ECO:0000305" FT CONFLICT 443 FT /note="Q -> E (in Ref. 6; BAD97107)" FT /evidence="ECO:0000305" FT CONFLICT 479 FT /note="T -> A (in Ref. 5; BAH13320)" FT /evidence="ECO:0000305" FT STRAND 9..12 FT /evidence="ECO:0007829|PDB:8QFC" FT HELIX 13..15 FT /evidence="ECO:0007829|PDB:8QFC" FT HELIX 16..22 FT /evidence="ECO:0007829|PDB:8QFC" FT HELIX 30..46 FT /evidence="ECO:0007829|PDB:8QFC" FT HELIX 65..78 FT /evidence="ECO:0007829|PDB:8QFC" FT HELIX 92..105 FT /evidence="ECO:0007829|PDB:8QFC" FT HELIX 106..108 FT /evidence="ECO:0007829|PDB:8QFC" FT HELIX 109..124 FT /evidence="ECO:0007829|PDB:8QFC" FT HELIX 126..167 FT /evidence="ECO:0007829|PDB:8QFC" FT HELIX 175..184 FT /evidence="ECO:0007829|PDB:8QFC" FT HELIX 189..198 FT /evidence="ECO:0007829|PDB:8QFC" FT HELIX 202..215 FT /evidence="ECO:0007829|PDB:8QFC" FT HELIX 225..232 FT /evidence="ECO:0007829|PDB:8QFC" FT HELIX 238..242 FT /evidence="ECO:0007829|PDB:8QFC" FT TURN 343..345 FT /evidence="ECO:0007829|PDB:8QFC" FT HELIX 347..372 FT /evidence="ECO:0007829|PDB:8QFC" FT HELIX 377..382 FT /evidence="ECO:0007829|PDB:8QFC" FT TURN 388..390 FT /evidence="ECO:0007829|PDB:8QFC" FT HELIX 395..417 FT /evidence="ECO:0007829|PDB:8QFC" FT HELIX 420..424 FT /evidence="ECO:0007829|PDB:8QFC" FT HELIX 428..468 FT /evidence="ECO:0007829|PDB:8QFC" FT HELIX 470..493 FT /evidence="ECO:0007829|PDB:8QFC" FT TURN 494..496 FT /evidence="ECO:0007829|PDB:8QFC" FT STRAND 499..502 FT /evidence="ECO:0007829|PDB:8QFC" SQ SEQUENCE 506 AA; 56921 MW; A21E59A79E1F87E0 CRC64; MEDHQHVPID IQTSKLLDWL VDRRHCSLKW QSLVLTIREK INAAIQDMPE SEEIAQLLSG SYIHYFHCLR ILDLLKGTEA STKNIFGRYS SQRMKDWQEI IALYEKDNTY LVELSSLLVR NVNYEIPSLK KQIAKCQQLQ QEYSRKEEEC QAGAAEMREQ FYHSCKQYGI TGENVRGELL ALVKDLPSQL AEIGAAAQQS LGEAIDVYQA SVGFVCESPT EQVLPMLRFV QKRGNSTVYE WRTGTEPSVV ERPHLEELPE QVAEDAIDWG DFGVEAVSEG TDSGISAEAA GIDWGIFPES DSKDPGGDGI DWGDDAVALQ ITVLEAGTQA PEGVARGPDA LTLLEYTETR NQFLDELMEL EIFLAQRAVE LSEEADVLSV SQFQLAPAIL QGQTKEKMVT MVSVLEDLIG KLTSLQLQHL FMILASPRYV DRVTEFLQQK LKQSQLLALK KELMVQKQQE ALEEQAALEP KLDLLLEKTK ELQKLIEADI SKRYSGRPVN LMGTSL //