ID TPPC8_HUMAN Reviewed; 1435 AA. AC Q9Y2L5; A0JP15; B3KME5; Q9H0L2; DT 16-APR-2002, integrated into UniProtKB/Swiss-Prot. DT 18-MAY-2010, sequence version 2. DT 28-JAN-2026, entry version 186. DE RecName: Full=Trafficking protein particle complex subunit 8; DE AltName: Full=Protein TRS85 homolog; GN Name=TRAPPC8; Synonyms=KIAA1012; 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 [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANTS SER-137 RP AND ALA-1146. RC TISSUE=Brain; RX PubMed=10231032; DOI=10.1093/dnares/6.1.63; RA Nagase T., Ishikawa K., Suyama M., Kikuno R., Hirosawa M., Miyajima N., RA Tanaka A., Kotani H., Nomura N., Ohara O.; RT "Prediction of the coding sequences of unidentified human genes. XIII. The RT complete sequences of 100 new cDNA clones from brain which code for large RT proteins in vitro."; RL DNA Res. 6:63-70(1999). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND VARIANT SER-137. RC TISSUE=Testis; RX PubMed=11230166; DOI=10.1101/gr.gr1547r; RA Wiemann S., Weil B., Wellenreuther R., Gassenhuber J., Glassl S., RA Ansorge W., Boecher M., Bloecker H., Bauersachs S., Blum H., Lauber J., RA Duesterhoeft A., Beyer A., Koehrer K., Strack N., Mewes H.-W., RA Ottenwaelder B., Obermaier B., Tampe J., Heubner D., Wambutt R., Korn B., RA Klein M., Poustka A.; RT "Towards a catalog of human genes and proteins: sequencing and analysis of RT 500 novel complete protein coding human cDNAs."; RL Genome Res. 11:422-435(2001). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16177791; DOI=10.1038/nature03983; RA Nusbaum C., Zody M.C., Borowsky M.L., Kamal M., Kodira C.D., Taylor T.D., RA Whittaker C.A., Chang J.L., Cuomo C.A., Dewar K., FitzGerald M.G., Yang X., RA Abouelleil A., Allen N.R., Anderson S., Bloom T., Bugalter B., Butler J., RA Cook A., DeCaprio D., Engels R., Garber M., Gnirke A., Hafez N., Hall J.L., RA Norman C.H., Itoh T., Jaffe D.B., Kuroki Y., Lehoczky J., Lui A., RA Macdonald P., Mauceli E., Mikkelsen T.S., Naylor J.W., Nicol R., Nguyen C., RA Noguchi H., O'Leary S.B., Piqani B., Smith C.L., Talamas J.A., Topham K., RA Totoki Y., Toyoda A., Wain H.M., Young S.K., Zeng Q., Zimmer A.R., RA Fujiyama A., Hattori M., Birren B.W., Sakaki Y., Lander E.S.; RT "DNA sequence and analysis of human chromosome 18."; RL Nature 437:551-555(2005). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 54-1435 (ISOFORM 1). 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 [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 427-1435 (ISOFORM 1). RC TISSUE=Teratocarcinoma; 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 IDENTIFICATION IN TRAPP COMPLEX. RX PubMed=11805826; DOI=10.1038/415141a; RA Gavin A.-C., Boesche M., Krause R., Grandi P., Marzioch M., Bauer A., RA Schultz J., Rick J.M., Michon A.-M., Cruciat C.-M., Remor M., Hoefert C., RA Schelder M., Brajenovic M., Ruffner H., Merino A., Klein K., Hudak M., RA Dickson D., Rudi T., Gnau V., Bauch A., Bastuck S., Huhse B., Leutwein C., RA Heurtier M.-A., Copley R.R., Edelmann A., Querfurth E., Rybin V., RA Drewes G., Raida M., Bouwmeester T., Bork P., Seraphin B., Kuster B., RA Neubauer G., Superti-Furga G.; RT "Functional organization of the yeast proteome by systematic analysis of RT protein complexes."; RL Nature 415:141-147(2002). RN [7] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=18669648; DOI=10.1073/pnas.0805139105; RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., RA Elledge S.J., Gygi S.P.; RT "A quantitative atlas of mitotic phosphorylation."; RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008). RN [8] 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 [9] RP FUNCTION, AND IDENTIFICATION IN TRAPP COMPLEX. RX PubMed=21525244; DOI=10.1091/mbc.e10-11-0873; RA Scrivens P.J., Noueihed B., Shahrzad N., Hul S., Brunet S., Sacher M.; RT "C4orf41 and TTC-15 are mammalian TRAPP components with a role at an early RT stage in ER-to-Golgi trafficking."; RL Mol. Biol. Cell 22:2083-2093(2011). RN [10] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-273, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21406692; DOI=10.1126/scisignal.2001570; RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.; RT "System-wide temporal characterization of the proteome and phosphoproteome RT of human embryonic stem cell differentiation."; RL Sci. Signal. 4:RS3-RS3(2011). RN [11] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-279 AND SER-309, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Erythroleukemia; RX PubMed=23186163; DOI=10.1021/pr300630k; RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., RA Mohammed S.; RT "Toward a comprehensive characterization of a human cancer cell RT phosphoproteome."; RL J. Proteome Res. 12:260-271(2013). RN [12] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-273, AND IDENTIFICATION BY RP 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 [13] RP FUNCTION, INTERACTION WITH TBC1D14, AND SUBCELLULAR LOCATION. RX PubMed=26711178; DOI=10.15252/embj.201592695; RA Lamb C.A., Nuehlen S., Judith D., Frith D., Snijders A.P., Behrends C., RA Tooze S.A.; RT "TBC1D14 regulates autophagy via the TRAPP complex and ATG9 traffic."; RL EMBO J. 35:281-301(2016). RN [14] RP FUNCTION, INTERACTION WITH TMEM131, AND MUTAGENESIS OF 1035-TRP--ASP-1040. RX PubMed=32095531; DOI=10.1126/sciadv.aay7667; RA Zhang Z., Bai M., Barbosa G.O., Chen A., Wei Y., Luo S., Wang X., Wang B., RA Tsukui T., Li H., Sheppard D., Kornberg T.B., Ma D.K.; RT "Broadly conserved roles of TMEM131 family proteins in intracellular RT collagen assembly and secretory cargo trafficking."; RL Sci. Adv. 6:eaay7667-eaay7667(2020). RN [15] RP VARIANT [LARGE SCALE ANALYSIS] GLN-537. RX PubMed=16959974; DOI=10.1126/science.1133427; RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., RA Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V., RA Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H., RA Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W., RA Velculescu V.E.; RT "The consensus coding sequences of human breast and colorectal cancers."; RL Science 314:268-274(2006). CC -!- FUNCTION: Plays a role in endoplasmic reticulum to Golgi apparatus CC trafficking at a very early stage (PubMed:21525244). Maintains together CC with TBC1D14 the cycling pool of ATG9 required for initiation of CC autophagy (PubMed:26711178). Involved in collagen secretion CC (PubMed:32095531). {ECO:0000269|PubMed:21525244, CC ECO:0000269|PubMed:26711178, ECO:0000269|PubMed:32095531}. CC -!- SUBUNIT: Component of the multisubunit TRAPP (transport protein CC particle) complex, which includes TRAPPC2, TRAPPC2L, TRAPPC3, TRAPPC3L, CC TRAPPC4, TRAPPC5, TRAPPC8, TRAPPC9, TRAPPC10, TRAPPC11 and TRAPPC12 CC (PubMed:11805826, PubMed:21525244). Interacts with TBC1D14 CC (PubMed:26711178). Interacts (via C-terminus) with TMEM131 (via C- CC terminus); the interaction is direct and is involved in collagen CC secretion (PubMed:32095531). {ECO:0000269|PubMed:11805826, CC ECO:0000269|PubMed:21525244, ECO:0000269|PubMed:26711178, CC ECO:0000269|PubMed:32095531}. CC -!- SUBCELLULAR LOCATION: Golgi apparatus, cis-Golgi network {ECO:0000250}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=Q9Y2L5-1; Sequence=Displayed; CC Name=2; CC IsoId=Q9Y2L5-2; Sequence=VSP_014454, VSP_004000; CC -!- MISCELLANEOUS: [Isoform 2]: May be produced at very low levels due to a CC premature stop codon in the mRNA, leading to nonsense-mediated mRNA CC decay. {ECO:0000305}. CC -!- SIMILARITY: Belongs to the TRS85 family. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=AAI27110.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305}; CC Sequence=AAI27111.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305}; CC Sequence=BAA76856.2; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305}; CC Sequence=BAG50957.1; Type=Erroneous initiation; Note=Truncated N-terminus.; 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; AB023229; BAA76856.2; ALT_INIT; mRNA. DR EMBL; AL136749; CAB66683.2; -; mRNA. DR EMBL; AC009831; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC022960; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC127109; AAI27110.1; ALT_INIT; mRNA. DR EMBL; BC127110; AAI27111.1; ALT_INIT; mRNA. DR EMBL; AK001662; BAG50957.1; ALT_INIT; mRNA. DR CCDS; CCDS11901.1; -. [Q9Y2L5-1] DR AlphaFoldDB; Q9Y2L5; -. DR SMR; Q9Y2L5; -. DR BioGRID; 116545; 86. DR ComplexPortal; CPX-4750; TRAPP III complex, TRAPPC2 variant. DR ComplexPortal; CPX-6903; TRAPP III complex, TRAPPC2B variant. DR CORUM; Q9Y2L5; -. DR DIP; DIP-48280N; -. DR FunCoup; Q9Y2L5; 2669. DR MINT; Q9Y2L5; -. DR STRING; 9606.ENSP00000283351; -. DR GlyConnect; 1829; 3 N-Linked glycans (1 site). DR GlyCosmos; Q9Y2L5; 1 site, 4 glycans. DR GlyGen; Q9Y2L5; 2 sites, 4 N-linked glycans (1 site), 1 O-linked glycan (1 site). DR iPTMnet; Q9Y2L5; -. DR PhosphoSitePlus; Q9Y2L5; -. DR SwissPalm; Q9Y2L5; -. DR BioMuta; TRAPPC8; -. DR DMDM; 296452850; -. DR jPOST; Q9Y2L5; -. DR MassIVE; Q9Y2L5; -. DR PaxDb; 9606-ENSP00000283351; -. DR PeptideAtlas; Q9Y2L5; -. DR ProteomicsDB; 85834; -. [Q9Y2L5-1] DR ProteomicsDB; 85835; -. [Q9Y2L5-2] DR Pumba; Q9Y2L5; -. DR Antibodypedia; 48760; 11 antibodies from 8 providers. DR DNASU; 22878; -. DR Ensembl; ENST00000283351.10; ENSP00000283351.4; ENSG00000153339.16. [Q9Y2L5-1] DR GeneID; 22878; -. DR KEGG; hsa:22878; -. DR MANE-Select; ENST00000283351.10; ENSP00000283351.4; NM_014939.5; NP_055754.3. DR UCSC; uc002kxc.5; human. [Q9Y2L5-1] DR AGR; HGNC:29169; -. DR ClinPGx; PA165429149; -. DR CTD; 22878; -. DR DisGeNET; 22878; -. DR GeneCards; TRAPPC8; -. DR HGNC; HGNC:29169; TRAPPC8. DR HPA; ENSG00000153339; Low tissue specificity. DR MIM; 614136; gene. DR OpenTargets; ENSG00000153339; -. DR VEuPathDB; HostDB:ENSG00000153339; -. DR eggNOG; KOG1938; Eukaryota. DR GeneTree; ENSGT00390000000568; -. DR HOGENOM; CLU_004823_2_0_1; -. DR InParanoid; Q9Y2L5; -. DR OMA; GHTISMW; -. DR OrthoDB; 203724at2759; -. DR PAN-GO; Q9Y2L5; 5 GO annotations based on evolutionary models. DR PhylomeDB; Q9Y2L5; -. DR PathwayCommons; Q9Y2L5; -. DR Reactome; R-HSA-8876198; RAB GEFs exchange GTP for GDP on RABs. DR SignaLink; Q9Y2L5; -. DR Agora; ENSG00000153339; -. DR BioGRID-ORCS; 22878; 808 hits in 1167 CRISPR screens. DR ChiTaRS; TRAPPC8; human. DR GeneWiki; KIAA1012; -. DR GenomeRNAi; 22878; -. DR Pharos; Q9Y2L5; Tdark. DR PRO; PR:Q9Y2L5; -. DR Proteomes; UP000005640; Chromosome 18. DR RNAct; Q9Y2L5; protein. DR Bgee; ENSG00000153339; Expressed in hair follicle and 211 other cell types or tissues. DR ExpressionAtlas; Q9Y2L5; baseline and differential. DR GO; GO:0005737; C:cytoplasm; NAS:ComplexPortal. DR GO; GO:0005829; C:cytosol; TAS:Reactome. DR GO; GO:0030008; C:TRAPP complex; IDA:UniProtKB. DR GO; GO:1990072; C:TRAPPIII protein complex; IBA:GO_Central. DR GO; GO:0032964; P:collagen biosynthetic process; IMP:UniProtKB. DR GO; GO:0048208; P:COPII vesicle coating; NAS:ComplexPortal. DR GO; GO:0006888; P:endoplasmic reticulum to Golgi vesicle-mediated transport; NAS:ComplexPortal. DR GO; GO:0007030; P:Golgi organization; IMP:UniProtKB. DR GO; GO:0099022; P:vesicle tethering; NAS:ComplexPortal. DR InterPro; IPR058541; Ig_TPPC8_1st. DR InterPro; IPR058538; Ig_TPPC8_2nd. DR InterPro; IPR058540; Ig_TPPC8_3rd. DR InterPro; IPR057651; Ig_TPPC8_C. DR InterPro; IPR011990; TPR-like_helical_dom_sf. DR InterPro; IPR024420; TRAPP_III_complex_Trs85. DR PANTHER; PTHR12975:SF6; TRAFFICKING PROTEIN PARTICLE COMPLEX SUBUNIT 8; 1. DR PANTHER; PTHR12975; TRANSPORT PROTEIN TRAPP; 1. DR Pfam; PF24545; Ig_TPPC8_1st; 1. DR Pfam; PF24544; Ig_TPPC8_2nd; 1. DR Pfam; PF24546; Ig_TPPC8_3rd; 1. DR Pfam; PF24542; Ig_TPPC8_C; 1. DR Pfam; PF12739; TRAPPC-Trs85; 1. DR SUPFAM; SSF48452; TPR-like; 1. PE 1: Evidence at protein level; KW Alternative splicing; ER-Golgi transport; Golgi apparatus; Phosphoprotein; KW Proteomics identification; Reference proteome; Transport. FT CHAIN 1..1435 FT /note="Trafficking protein particle complex subunit 8" FT /id="PRO_0000065641" FT REGION 301..321 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 302..312 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 273 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21406692, FT ECO:0007744|PubMed:24275569" FT MOD_RES 279 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 309 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT VAR_SEQ 916..926 FT /note="VFFIHFPTGLL -> TLALAQEVNQR (in isoform 2)" FT /evidence="ECO:0000303|PubMed:11230166" FT /id="VSP_014454" FT VAR_SEQ 927..1002 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:11230166" FT /id="VSP_004000" FT VARIANT 74 FT /note="N -> S (in dbSNP:rs34292533)" FT /id="VAR_057814" FT VARIANT 137 FT /note="L -> S (in dbSNP:rs6506948)" FT /evidence="ECO:0000269|PubMed:10231032, FT ECO:0000269|PubMed:11230166" FT /id="VAR_060250" FT VARIANT 517 FT /note="S -> G (in dbSNP:rs17857486)" FT /id="VAR_060251" FT VARIANT 537 FT /note="R -> Q (in a breast cancer sample; somatic mutation; FT dbSNP:rs754569032)" FT /evidence="ECO:0000269|PubMed:16959974" FT /id="VAR_036270" FT VARIANT 708 FT /note="Q -> E (in dbSNP:rs16962530)" FT /id="VAR_057815" FT VARIANT 954 FT /note="R -> H (in dbSNP:rs2170562)" FT /id="VAR_060252" FT VARIANT 1146 FT /note="T -> A (in dbSNP:rs3737374)" FT /evidence="ECO:0000269|PubMed:10231032" FT /id="VAR_060253" FT VARIANT 1189 FT /note="I -> V (in dbSNP:rs36034613)" FT /id="VAR_057816" FT VARIANT 1298 FT /note="S -> P (in dbSNP:rs633500)" FT /id="VAR_060254" FT MUTAGEN 1035..1040 FT /note="WLRGPD->ALAGPA: Attenuates interaction with FT TMEM131." FT /evidence="ECO:0000269|PubMed:32095531" FT CONFLICT 251 FT /note="K -> E (in Ref. 2; CAB66683)" FT /evidence="ECO:0000305" FT CONFLICT 631 FT /note="E -> G (in Ref. 5; BAG50957)" FT /evidence="ECO:0000305" FT CONFLICT 1060 FT /note="P -> T (in Ref. 5; BAG50957)" FT /evidence="ECO:0000305" SQ SEQUENCE 1435 AA; 160997 MW; A6D60A7C9E65F46D CRC64; MAQCVQSVQE LIPDSFVPCV AALCSDEAER LTRLNHLSFA ELLKPFSRLT SEVHMRDPNN QLHVIKNLKI AVSNIVTQPP QPGAIRKLLN DVVSGSQPAE GLVANVITAG DYDLNISATT PWFESYRETF LQSMPALDHE FLNHYLACML VASSSEAEPV EQFSKLSQEQ HRIQHNSDYS YPKWFIPNTL KYYVLLHDVS AGDEQRAESI YEEMKQKYGT QGCYLLKINS RTSNRASDEQ IPDPWSQYLQ KNSIQNQESY EDGPCTITSN KNSDNNLLSL DGLDNEVKDG LPNNFRAHPL QLEQSSDPSN SIDGPDHLRS ASSLHETKKG NTGIIHGACL TLTDHDRIRQ FIQEFTFRGL LPHIEKTIRQ LNDQLISRKG LSRSLFSATK KWFSGSKVPE KSINDLKNTS GLLYPPEAPE LQIRKMADLC FLVQHYDLAY SCYHTAKKDF LNDQAMLYAA GALEMAAVSA FLQPGAPRPY PAHYMDTAIQ TYRDICKNMV LAERCVLLSA ELLKSQSKYS EAAALLIRLT SEDSDLRSAL LLEQAAHCFI NMKSPMVRKY AFHMILAGHR FSKAGQKKHA LRCYCQAMQV YKGKGWSLAE DHINFTIGRQ SYTLRQLDNA VSAFRHILIN ESKQSAAQQG AFLREYLYVY KNVSQLSPDG PLPQLPLPYI NSSATRVFFG HDRRPADGEK QAATHVSLDQ EYDSESSQQW RELEEQVVSV VNKGVIPSNF HPTQYCLNSY SDNSRFPLAV VEEPITVEVA FRNPLKVLLL LTDLSLLWKF HPKDFSGKDN EEVKQLVTSE PEMIGAEVIS EFLINGEESK VARLKLFPHH IGELHILGVV YNLGTIQGSM TVDGIGALPG CHTGKYSLSM SVRGKQDLEI QGPRLNNTKE EKTSVKYGPD RRLDPIITEE MPLLEVFFIH FPTGLLCGEI RKAYVEFVNV SKCPLTGLKV VSKRPEFFTF GGNTAVLTPL SPSASENCSA YKTVVTDATS VCTALISSAS SVDFGIGTGS QPEVIPVPLP DTVLLPGASV QLPMWLRGPD EEGVHEINFL FYYESVKKQP KIRHRILRHT AIICTSRSLN VRATVCRSNS LENEEGRGGN MLVFVDVENT NTSEAGVKEF HIVQVSSSSK HWKLQKSVNL SENKDTKLAS REKGKFCFKA IRCEKEEAAT QSSEKYTFAD IIFGNEQIIS SASPCADFFY RSLSSELKKP QAHLPVHTEK QSTEDAVRLI QKCSEVDLNI VILWKAYVVE DSKQLILEGQ HHVILRTIGK EAFSYPQKQE PPEMELLKFF RPENITVSSR PSVEQLSSLI KTSLHYPESF NHPFHQKSLC LVPVTLLLSN CSKADVDVIV DLRHKTTSPE ALEIHGSFTW LGQTQYKLQL KSQEIHSLQL KACFVHTGVY NLGTPRVFAK LSDQVTVFET SQQNSMPALI IISNV //