ID TRIM5_HUMAN Reviewed; 493 AA. AC Q9C035; A6NGQ1; A8WFA8; D3DQS8; D3DQS9; G3GJY1; Q2MLV4; Q2MLV8; Q2MLV9; AC Q2MLW1; Q2MLW3; Q2MLW4; Q2MLW6; Q2MLW7; Q2MLX1; Q2MLX2; Q2MLX3; Q2MLX5; AC Q2MLY3; Q2MLY4; Q2V6Q6; Q6GX26; Q8WU46; Q96SR5; Q9C031; Q9C032; Q9C033; AC Q9C034; DT 28-NOV-2003, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-2001, sequence version 1. DT 10-JUN-2026, entry version 218. DE RecName: Full=Tripartite motif-containing protein 5; DE EC=2.3.2.27; DE AltName: Full=RING finger protein 88; DE AltName: Full=RING-type E3 ubiquitin transferase TRIM5 {ECO:0000305}; GN Name=TRIM5; Synonyms=RNF88; 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] (ISOFORMS ALPHA; BETA; GAMMA; DELTA AND RP EPSILON), AND VARIANT GLN-136. RX PubMed=11331580; DOI=10.1093/emboj/20.9.2140; RA Reymond A., Meroni G., Fantozzi A., Merla G., Cairo S., Luzi L., RA Riganelli D., Zanaria E., Messali S., Cainarca S., Guffanti A., Minucci S., RA Pelicci P.G., Ballabio A.; RT "The tripartite motif family identifies cell compartments."; RL EMBO J. 20:2140-2151(2001). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM ALPHA). RX PubMed=15249690; DOI=10.1073/pnas.0402876101; RA Yap M.W., Nisole S., Lynch C., Stoye J.P.; RT "Trim5alpha protein restricts both HIV-1 and murine leukemia virus."; RL Proc. Natl. Acad. Sci. U.S.A. 101:10786-10791(2004). RN [3] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM ALPHA), AND VARIANTS TYR-43 AND RP ASP-249. RX PubMed=16401428; DOI=10.1016/j.cub.2005.11.045; RA Sawyer S.L., Wu L.I., Akey J.M., Emerman M., Malik H.S.; RT "High-frequency persistence of an impaired allele of the retroviral defense RT gene TRIM5alpha in humans."; RL Curr. Biol. 16:95-100(2006). RN [4] RP NUCLEOTIDE SEQUENCE [MRNA], VARIANT GLN-136, FUNCTION, AUTOUBIQUITINATION, RP UBIQUITINATION BY TRIM21, AND MUTAGENESIS OF CYS-15. RC TISSUE=Brain; RX PubMed=18312418; DOI=10.1111/j.1742-4658.2008.06313.x; RA Yamauchi K., Wada K., Tanji K., Tanaka M., Kamitani T.; RT "Ubiquitination of E3 ubiquitin ligase TRIM5 alpha and its potential RT role."; RL FEBS J. 275:1540-1555(2008). RN [5] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM EPSILON), ALTERNATIVE SPLICING, AND RP FUNCTION. RX PubMed=21632761; DOI=10.1128/jvi.00648-11; RA Battivelli E., Migraine J., Lecossier D., Matsuoka S., Perez-Bercoff D., RA Saragosti S., Clavel F., Hance A.J.; RT "Modulation of TRIM5alpha activity in human cells by alternatively spliced RT TRIM5 isoforms."; RL J. Virol. 85:7828-7835(2011). RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM ALPHA), AND VARIANT RP GLN-136. 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 [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16554811; DOI=10.1038/nature04632; RA Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K., RA Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F., Bloom T., RA Bruford E., Chang J.L., Cuomo C.A., Eichler E., FitzGerald M.G., RA Jaffe D.B., LaButti K., Nicol R., Park H.-S., Seaman C., Sougnez C., RA Yang X., Zimmer A.R., Zody M.C., Birren B.W., Nusbaum C., Fujiyama A., RA Hattori M., Rogers J., Lander E.S., Sakaki Y.; RT "Human chromosome 11 DNA sequence and analysis including novel gene RT identification."; RL Nature 440:497-500(2006). RN [8] 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 [9] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS SER-31; TYR-43; TYR-58; RP GLU-110; PHE-112; GLN-136; ASP-249; TYR-419; SER-467 AND LEU-479. RG NIEHS SNPs program; RL Submitted (NOV-2007) to the EMBL/GenBank/DDBJ databases. RN [10] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM GAMMA). RC TISSUE=Rhabdomyosarcoma; 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 [11] RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH BTBD1 AND BTBD2. RX PubMed=12878161; DOI=10.1016/s0014-4827(03)00187-3; RA Xu L., Yang L., Moitra P.K., Hashimoto K., Rallabhandi P., Kaul S., RA Meroni G., Jensen J.P., Weissman A.M., D'Arpa P.; RT "BTBD1 and BTBD2 colocalize to cytoplasmic bodies with the RBCC/tripartite RT motif protein, TRIM5delta."; RL Exp. Cell Res. 288:84-93(2003). RN [12] RP FUNCTION (ISOFORM ALPHA). RX PubMed=16474118; DOI=10.1128/jvi.80.5.2100-2105.2006; RA Passerini L.D., Keckesova Z., Towers G.J.; RT "Retroviral restriction factors Fv1 and TRIM5alpha act independently and RT can compete for incoming virus before reverse transcription."; RL J. Virol. 80:2100-2105(2006). RN [13] RP MUTAGENESIS OF ARG-332. RX PubMed=16809279; DOI=10.1128/jvi.00270-06; RA Li Y., Li X., Stremlau M., Lee M., Sodroski J.; RT "Removal of arginine 332 allows human TRIM5alpha to bind human RT immunodeficiency virus capsids and to restrict infection."; RL J. Virol. 80:6738-6744(2006). RN [14] RP FUNCTION (ISOFORM ALPHA). RX PubMed=16643975; DOI=10.1016/j.virol.2006.03.015; RA Stremlau M., Song B., Javanbakht H., Perron M., Sodroski J.; RT "Cyclophilin A: an auxiliary but not necessary cofactor for TRIM5alpha RT restriction of HIV-1."; RL Virology 351:112-120(2006). RN [15] RP REVIEW. RX PubMed=16956947; DOI=10.1128/jvi.01519-06; RA Luban J.; RT "Cyclophilin A, TRIM5, and resistance to human immunodeficiency virus type RT 1 infection."; RL J. Virol. 81:1054-1061(2007). RN [16] RP FUNCTION, SUBUNIT, AND INTERACTION WITH TRIM6 AND TRIM34. RX PubMed=17156811; DOI=10.1016/j.virol.2006.10.035; RA Li X., Gold B., O'hUigin C., Diaz-Griffero F., Song B., Si Z., Li Y., RA Yuan W., Stremlau M., Mische C., Javanbakht H., Scally M., Winkler C., RA Dean M., Sodroski J.; RT "Unique features of TRIM5alpha among closely related human TRIM family RT members."; RL Virology 360:419-433(2007). RN [17] RP INTERACTION WITH HSPA1A/B. RX PubMed=20053985; DOI=10.1074/jbc.m109.040618; RA Hwang C.Y., Holl J., Rajan D., Lee Y., Kim S., Um M., Kwon K.S., Song B.; RT "Hsp70 interacts with the retroviral restriction factor TRIM5alpha and RT assists the folding of TRIM5alpha."; RL J. Biol. Chem. 285:7827-7837(2010). RN [18] RP INTERACTION WITH SQSTM1, AND SUBCELLULAR LOCATION. RX PubMed=20357094; DOI=10.1128/jvi.02412-09; RA O'Connor C., Pertel T., Gray S., Robia S.L., Bakowska J.C., Luban J., RA Campbell E.M.; RT "p62/sequestosome-1 associates with and sustains the expression of RT retroviral restriction factor TRIM5alpha."; RL J. Virol. 84:5997-6006(2010). RN [19] RP REVIEW, AND PROTEASOMAL DEGRADATION. RX PubMed=21247355; DOI=10.1089/aid.2010.0367; RA Sastri J., Campbell E.M.; RT "Recent insights into the mechanism and consequences of TRIM5alpha RT retroviral restriction."; RL AIDS Res. Hum. Retroviruses 27:231-238(2011). RN [20] RP REVIEW. RX PubMed=21575904; DOI=10.1016/j.chom.2011.05.003; RA Tareen S.U., Emerman M.; RT "Trim5 TAKes on pattern recognition."; RL Cell Host Microbe 9:349-350(2011). RN [21] RP INTERACTION WITH TRIM6 AND TRIM34. RX PubMed=21680743; DOI=10.1074/jbc.m111.260406; RA Li X., Yeung D.F., Fiegen A.M., Sodroski J.; RT "Determinants of the higher order association of the restriction factor RT TRIM5alpha and other tripartite motif (TRIM) proteins."; RL J. Biol. Chem. 286:27959-27970(2011). RN [22] RP REVIEW. RX PubMed=21512569; DOI=10.1038/472305a; RA Aiken C., Joyce S.; RT "Immunology: TRIM5 does double duty."; RL Nature 472:305-306(2011). RN [23] RP FUNCTION, AND INTERACTION WITH MAP3K7/TAK1; TAB2 AND TAB3. RX PubMed=21512573; DOI=10.1038/nature09976; RA Pertel T., Hausmann S., Morger D., Zueger S., Guerra J., Lascano J., RA Reinhard C., Santoni F.A., Uchil P.D., Chatel L., Bisiaux A., Albert M.L., RA Strambio-De-Castillia C., Mothes W., Pizzato M., Gruetter M.G., Luban J.; RT "TRIM5 is an innate immune sensor for the retrovirus capsid lattice."; RL Nature 472:361-365(2011). RN [24] RP REVIEW. RX PubMed=21572451; DOI=10.1038/nrmicro2582; RA Jermy A.; RT "Antiviral immunity: TRIM5 moonlights as a pattern recognition receptor."; RL Nat. Rev. Microbiol. 9:398-398(2011). RN [25] RP INTERACTION WITH PSMC2. RX PubMed=22078707; DOI=10.1186/1742-4690-8-93; RA Lukic Z., Hausmann S., Sebastian S., Rucci J., Sastri J., Robia S.L., RA Luban J., Campbell E.M.; RT "TRIM5alpha associates with proteasomal subunits in cells while in complex RT with HIV-1 virions."; RL Retrovirology 8:93-93(2011). RN [26] RP FUNCTION. RX PubMed=21035162; DOI=10.1016/j.virol.2010.09.018; RA Tareen S.U., Emerman M.; RT "Human Trim5alpha has additional activities that are uncoupled from RT retroviral capsid recognition."; RL Virology 409:113-120(2011). RN [27] RP REVIEW. RX PubMed=21866272; DOI=10.3390/v3071204; RA de Silva S., Wu L.; RT "TRIM5 acts as more than a retroviral restriction factor."; RL Viruses 3:1204-1209(2011). RN [28] RP REVIEW. RX PubMed=22482711; DOI=10.1016/j.coviro.2012.02.003; RA Gruetter M.G., Luban J.; RT "TRIM5 structure, HIV-1 capsid recognition, and innate immune signaling."; RL Curr. Opin. Virol. 2:142-150(2012). RN [29] RP REVIEW, AND FUNCTION. RX PubMed=22291694; DOI=10.3389/fmicb.2012.00013; RA Nakayama E.E., Shioda T.; RT "TRIM5alpha and species tropism of HIV/SIV."; RL Front. Microbiol. 3:13-13(2012). RN [30] RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY RP [LARGE SCALE ANALYSIS]. RX PubMed=22223895; DOI=10.1074/mcp.m111.015131; RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., RA Giglione C.; RT "Comparative large-scale characterisation of plant vs. mammal proteins RT reveals similar and idiosyncratic N-alpha acetylation features."; RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012). RN [31] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-86, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma, and 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 [32] RP FUNCTION, INTERACTION WITH ULK1; SQSTM1; GABARAP; GABARAPL1; GABARAPL2; RP MAP1LC3A; MAP1LC3C AND BECN1, AND SUBCELLULAR LOCATION. RX PubMed=25127057; DOI=10.1016/j.devcel.2014.06.013; RA Mandell M.A., Jain A., Arko-Mensah J., Chauhan S., Kimura T., Dinkins C., RA Silvestri G., Munch J., Kirchhoff F., Simonsen A., Wei Y., Levine B., RA Johansen T., Deretic V.; RT "TRIM proteins regulate autophagy and can target autophagic substrates by RT direct recognition."; RL Dev. Cell 30:394-409(2014). RN [33] 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 [34] RP STRUCTURE BY NMR OF 1-78. RX PubMed=21734049; DOI=10.1128/jvi.00497-11; RA Lienlaf M., Hayashi F., Di Nunzio F., Tochio N., Kigawa T., Yokoyama S., RA Diaz-Griffero F.; RT "Contribution of E3-ubiquitin ligase activity to HIV-1 restriction by RT TRIM5alpha(rh): structure of the RING domain of TRIM5alpha."; RL J. Virol. 85:8725-8737(2011). RN [35] RP STRUCTURE BY NMR OF 86-129. RG RIKEN structural genomics initiative (RSGI); RT "Solution structure of the b-box domain from tripartite motif-containing RT protein 5."; RL Submitted (FEB-2009) to the PDB data bank. CC -!- FUNCTION: Capsid-specific restriction factor that prevents infection CC from non-host-adapted retroviruses. Blocks viral replication early in CC the life cycle, after viral entry but before reverse transcription. In CC addition to acting as a capsid-specific restriction factor, also acts CC as a pattern recognition receptor that activates innate immune CC signaling in response to the retroviral capsid lattice. Binding to the CC viral capsid triggers its E3 ubiquitin ligase activity, and in concert CC with the heterodimeric ubiquitin conjugating enzyme complex UBE2V1- CC UBE2N (also known as UBC13-UEV1A complex) generates 'Lys-63'-linked CC polyubiquitin chains, which in turn are catalysts in the CC autophosphorylation of the MAP3K7/TAK1 complex (includes TAK1, TAB2, CC and TAB3). Activation of the MAP3K7/TAK1 complex by autophosphorylation CC results in the induction and expression of NF-kappa-B and MAPK- CC responsive inflammatory genes, thereby leading to an innate immune CC response in the infected cell. Restricts infection by N-tropic murine CC leukemia virus (N-MLV), equine infectious anemia virus (EIAV), simian CC immunodeficiency virus of macaques (SIVmac), feline immunodeficiency CC virus (FIV), and bovine immunodeficiency virus (BIV) (PubMed:17156811). CC Plays a role in regulating autophagy through activation of autophagy CC regulator BECN1 by causing its dissociation from its inhibitors BCL2 CC and TAB2 (PubMed:25127057). Also plays a role in autophagy by acting as CC a selective autophagy receptor which recognizes and targets HIV-1 CC capsid protein p24 for autophagic destruction (PubMed:25127057). CC {ECO:0000269|PubMed:12878161, ECO:0000269|PubMed:17156811, CC ECO:0000269|PubMed:18312418, ECO:0000269|PubMed:21035162, CC ECO:0000269|PubMed:21512573, ECO:0000269|PubMed:21632761, CC ECO:0000269|PubMed:22291694, ECO:0000269|PubMed:25127057}. CC -!- CATALYTIC ACTIVITY: CC Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + CC [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L- CC cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.; CC EC=2.3.2.27; CC -!- PATHWAY: Protein modification; protein ubiquitination. CC -!- SUBUNIT: Can form homodimers and homotrimers. In addition to lower- CC order dimerization, also exhibits a higher-order multimerization and CC both low- and high-order multimerizations are essential for its CC restriction activity. Isoform Delta interacts with BTBD1 and BTBD2. CC Interacts with PSMC4, PSMC5, PSMD7 and HSPA8/HSC70 (By similarity). CC Interacts (via B30.2/SPRY domain) with HSPA1A/B. Interacts with PSMC2, CC MAP3K7/TAK1, TAB2 and TAB3 (PubMed:21512573, PubMed:22078707). CC Interacts with SQSTM1 (PubMed:20357094, PubMed:25127057). Interacts CC with TRIM6 and TRIM34 (PubMed:17156811, PubMed:21680743). Interacts CC with ULK1 (phosphorylated form), GABARAP, GABARAPL1, GABARAPL2, CC MAP1LC3A, MAP1LC3C and BECN1 (PubMed:25127057). {ECO:0000250, CC ECO:0000269|PubMed:12878161, ECO:0000269|PubMed:17156811, CC ECO:0000269|PubMed:20053985, ECO:0000269|PubMed:20357094, CC ECO:0000269|PubMed:21512573, ECO:0000269|PubMed:21680743, CC ECO:0000269|PubMed:22078707, ECO:0000269|PubMed:25127057}. CC -!- INTERACTION: CC Q9C035; P13569: CFTR; NbExp=3; IntAct=EBI-924214, EBI-349854; CC Q9C035; O95863: SNAI1; NbExp=3; IntAct=EBI-924214, EBI-1045459; CC Q9C035; Q13049: TRIM32; NbExp=2; IntAct=EBI-924214, EBI-742790; CC Q9C035; Q9C035: TRIM5; NbExp=3; IntAct=EBI-924214, EBI-924214; CC Q9C035-1; Q2Y080; Xeno; NbExp=3; IntAct=EBI-924230, EBI-924086; CC Q9C035-3; Q08426: EHHADH; NbExp=3; IntAct=EBI-12840050, EBI-2339219; CC Q9C035-3; P13473-2: LAMP2; NbExp=3; IntAct=EBI-12840050, EBI-21591415; CC Q9C035-3; Q5T2T1: MPP7; NbExp=3; IntAct=EBI-12840050, EBI-2514004; CC Q9C035-3; Q8N3F0: MTURN; NbExp=3; IntAct=EBI-12840050, EBI-11980301; CC Q9C035-3; Q96HA8: NTAQ1; NbExp=3; IntAct=EBI-12840050, EBI-741158; CC Q9C035-3; O43765: SGTA; NbExp=3; IntAct=EBI-12840050, EBI-347996; CC Q9C035-3; Q9Y371: SH3GLB1; NbExp=3; IntAct=EBI-12840050, EBI-2623095; CC Q9C035-3; Q3SY00: TSGA10IP; NbExp=3; IntAct=EBI-12840050, EBI-10241197; CC Q9C035-3; P57075-2: UBASH3A; NbExp=3; IntAct=EBI-12840050, EBI-7353612; CC Q9C035-3; P61086: UBE2K; NbExp=6; IntAct=EBI-12840050, EBI-473850; CC Q9C035-3; P07947: YES1; NbExp=3; IntAct=EBI-12840050, EBI-515331; CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:25127057}. Nucleus CC {ECO:0000250|UniProtKB:Q0PF16}. Note=Predominantly localizes in CC cytoplasmic bodies (PubMed:12878161, PubMed:20357094). Localization may CC be influenced by the coexpression of other TRIM proteins, hence partial CC nuclear localization is observed in the presence of TRIM22 or TRIM27 CC (By similarity). In cytoplasmic bodies, colocalizes with proteasomal CC subunits and SQSTM1 (By similarity). {ECO:0000250|UniProtKB:Q0PF16, CC ECO:0000269|PubMed:12878161, ECO:0000269|PubMed:20357094, CC ECO:0000269|PubMed:25127057}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=6; CC Name=Alpha; CC IsoId=Q9C035-1; Sequence=Displayed; CC Name=Beta; CC IsoId=Q9C035-2; Sequence=VSP_009010, VSP_009011; CC Name=Gamma; CC IsoId=Q9C035-3; Sequence=VSP_009012, VSP_009013; CC Name=Delta; CC IsoId=Q9C035-4; Sequence=VSP_009014, VSP_009015; CC Name=Epsilon; Synonyms=Kappa; CC IsoId=Q9C035-5; Sequence=VSP_009016, VSP_009017; CC Name=Iota; CC IsoId=Q9C035-6; Sequence=VSP_044095, VSP_044096; CC -!- DOMAIN: The B box-type zinc finger domain and the coiled-coil domain CC contribute to the higher and low order multimerization respectively CC which is essential for restriction activity (PubMed:22482711). The CC coiled coil domain is important for higher order multimerization by CC promoting the initial dimerization (By similarity). CC {ECO:0000250|UniProtKB:Q0PF16, ECO:0000269|PubMed:22482711}. CC -!- DOMAIN: The B30.2/SPRY domain acts as a capsid recognition domain. CC Polymorphisms in this domain explain the observed species-specific CC differences among orthologs (PubMed:22482711). CC {ECO:0000269|PubMed:22482711}. CC -!- DOMAIN: The RING-type zinc finger domain confers E3 ubiquitin ligase CC activity and is essential for retrovirus restriction activity, CC autoubiquitination and higher-order multimerization. CC {ECO:0000269|PubMed:22482711}. CC -!- PTM: Degraded in a proteasome-independent fashion in the absence of CC viral infection but in a proteasome-dependent fashion following CC exposure to restriction sensitive virus. CC -!- PTM: Autoubiquitinated in a RING finger- and UBE2D2-dependent manner. CC Monoubiquitinated by TRIM21. Deubiquitinated by Yersinia YopJ. CC Ubiquitination may not lead to proteasomal degradation. CC {ECO:0000269|PubMed:18312418}. CC -!- MISCELLANEOUS: [Isoform Beta]: Probable artifact. {ECO:0000305}. CC -!- MISCELLANEOUS: [Isoform Iota]: Has dominant-negative activity against CC TRIM5alpha. Does not inhibit HIV-1 replication. {ECO:0000305}. CC -!- SIMILARITY: Belongs to the TRIM/RBCC family. {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; AF220025; AAG53479.1; -; mRNA. DR EMBL; AF220026; AAG53480.1; -; mRNA. DR EMBL; AF220027; AAG53481.1; -; mRNA. DR EMBL; AF220028; AAG53482.1; -; mRNA. DR EMBL; AF220029; AAG53483.1; -; mRNA. DR EMBL; AY625000; AAT48101.1; -; mRNA. DR EMBL; DQ301444; ABC00997.1; -; Genomic_DNA. DR EMBL; DQ301445; ABC00998.1; -; Genomic_DNA. DR EMBL; DQ301446; ABC00999.1; -; Genomic_DNA. DR EMBL; DQ301447; ABC01000.1; -; Genomic_DNA. DR EMBL; DQ301448; ABC01001.1; -; Genomic_DNA. DR EMBL; DQ301449; ABC01002.1; -; Genomic_DNA. DR EMBL; DQ301450; ABC01003.1; -; Genomic_DNA. DR EMBL; DQ301451; ABC01004.1; -; Genomic_DNA. DR EMBL; DQ301452; ABC01005.1; -; Genomic_DNA. DR EMBL; DQ301453; ABC01006.1; -; Genomic_DNA. DR EMBL; DQ301454; ABC01007.1; -; Genomic_DNA. DR EMBL; DQ301455; ABC01008.1; -; Genomic_DNA. DR EMBL; DQ301456; ABC01009.1; -; Genomic_DNA. DR EMBL; DQ301457; ABC01010.1; -; Genomic_DNA. DR EMBL; DQ301458; ABC01011.1; -; Genomic_DNA. DR EMBL; DQ301459; ABC01012.1; -; Genomic_DNA. DR EMBL; DQ301460; ABC01013.1; -; Genomic_DNA. DR EMBL; DQ301461; ABC01014.1; -; Genomic_DNA. DR EMBL; DQ301462; ABC01015.1; -; Genomic_DNA. DR EMBL; DQ301463; ABC01016.1; -; Genomic_DNA. DR EMBL; DQ301464; ABC01017.1; -; Genomic_DNA. DR EMBL; DQ301465; ABC01018.1; -; Genomic_DNA. DR EMBL; DQ301466; ABC01019.1; -; Genomic_DNA. DR EMBL; DQ301467; ABC01020.1; -; Genomic_DNA. DR EMBL; DQ301468; ABC01021.1; -; Genomic_DNA. DR EMBL; DQ301469; ABC01022.1; -; Genomic_DNA. DR EMBL; DQ301470; ABC01023.1; -; Genomic_DNA. DR EMBL; DQ301471; ABC01024.1; -; Genomic_DNA. DR EMBL; DQ301472; ABC01025.1; -; Genomic_DNA. DR EMBL; DQ301473; ABC01026.1; -; Genomic_DNA. DR EMBL; DQ301474; ABC01027.1; -; Genomic_DNA. DR EMBL; DQ301475; ABC01028.1; -; Genomic_DNA. DR EMBL; DQ301476; ABC01029.1; -; Genomic_DNA. DR EMBL; DQ301477; ABC01030.1; -; Genomic_DNA. DR EMBL; DQ301478; ABC01031.1; -; Genomic_DNA. DR EMBL; DQ301479; ABC01032.1; -; Genomic_DNA. DR EMBL; DQ301480; ABC01033.1; -; Genomic_DNA. DR EMBL; DQ288685; ABB90543.1; -; mRNA. DR EMBL; JF928461; AEN14475.1; -; mRNA. DR EMBL; JF928462; AEN14476.1; -; mRNA. DR EMBL; AK027593; BAB55218.1; -; mRNA. DR EMBL; AC015691; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471064; EAW68771.1; -; Genomic_DNA. DR EMBL; CH471064; EAW68772.1; -; Genomic_DNA. DR EMBL; CH471064; EAW68774.1; -; Genomic_DNA. DR EMBL; CH471064; EAW68775.1; -; Genomic_DNA. DR EMBL; EU260465; ABW96352.1; -; Genomic_DNA. DR EMBL; CH471064; EAW68776.1; -; Genomic_DNA. DR EMBL; CH471064; EAW68777.1; -; Genomic_DNA. DR EMBL; BC021258; AAH21258.1; -; mRNA. DR CCDS; CCDS31392.1; -. [Q9C035-4] DR CCDS; CCDS31393.1; -. [Q9C035-1] DR CCDS; CCDS31394.1; -. [Q9C035-3] DR RefSeq; NP_149023.2; NM_033034.3. [Q9C035-1] DR RefSeq; NP_149083.2; NM_033092.4. [Q9C035-3] DR RefSeq; NP_149084.2; NM_033093.4. [Q9C035-4] DR RefSeq; XP_005253240.1; XM_005253183.4. [Q9C035-1] DR RefSeq; XP_005253241.1; XM_005253184.4. [Q9C035-4] DR PDB; 2ECV; NMR; -; A=1-78. DR PDB; 2YRG; NMR; -; A=86-129. DR PDBsum; 2ECV; -. DR PDBsum; 2YRG; -. DR AlphaFoldDB; Q9C035; -. DR BMRB; Q9C035; -. DR SMR; Q9C035; -. DR BioGRID; 124491; 108. DR ELM; Q9C035; -. DR FunCoup; Q9C035; 205. DR IntAct; Q9C035; 47. DR MINT; Q9C035; -. DR NDEx; IQUERY-CP-TRIM5; 3 NDEx IQuery Curated Pathways. DR STRING; 9606.ENSP00000369373; -. DR MoonDB; Q9C035; Predicted. DR GlyGen; Q9C035; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; Q9C035; -. DR PhosphoSitePlus; Q9C035; -. DR BioMuta; TRIM5; -. DR DMDM; 38605459; -. DR jPOST; Q9C035; -. DR MassIVE; Q9C035; -. DR PaxDb; 9606-ENSP00000369373; -. DR PeptideAtlas; Q9C035; -. DR ProteomicsDB; 79952; -. [Q9C035-1] DR ProteomicsDB; 79953; -. [Q9C035-2] DR ProteomicsDB; 79954; -. [Q9C035-3] DR ProteomicsDB; 79955; -. [Q9C035-4] DR ProteomicsDB; 79956; -. [Q9C035-5] DR Pumba; Q9C035; -. DR Antibodypedia; 4609; 492 antibodies from 39 providers. DR DNASU; 85363; -. DR Ensembl; ENST00000380027.5; ENSP00000369366.1; ENSG00000132256.21. [Q9C035-4] DR Ensembl; ENST00000380034.8; ENSP00000369373.3; ENSG00000132256.21. [Q9C035-1] DR Ensembl; ENST00000396847.7; ENSP00000380058.3; ENSG00000132256.21. [Q9C035-3] DR Ensembl; ENST00000433961.5; ENSP00000393052.1; ENSG00000132256.21. [Q9C035-5] DR Ensembl; ENST00000684655.1; ENSP00000507420.1; ENSG00000132256.21. [Q9C035-1] DR Ensembl; ENST00000957480.1; ENSP00000627539.1; ENSG00000132256.21. [Q9C035-1] DR Ensembl; ENST00000957481.1; ENSP00000627540.1; ENSG00000132256.21. [Q9C035-1] DR GeneID; 85363; -. DR KEGG; hsa:85363; -. DR MANE-Select; ENST00000380034.8; ENSP00000369373.3; NM_033034.3; NP_149023.2. DR UCSC; uc001mbm.3; human. [Q9C035-1] DR AGR; HGNC:16276; -. DR ClinPGx; PA38109; -. DR CTD; 85363; -. DR DisGeNET; 85363; -. DR GeneCards; TRIM5; -. DR HGNC; HGNC:16276; TRIM5. DR HPA; ENSG00000132256; Low tissue specificity. DR MIM; 608487; gene. DR OpenTargets; ENSG00000132256; -. DR VEuPathDB; HostDB:ENSG00000132256; -. DR eggNOG; KOG2177; Eukaryota. DR GeneTree; ENSGT00940000154647; -. DR HOGENOM; CLU_013137_0_3_1; -. DR InParanoid; Q9C035; -. DR OMA; CITANNR; -. DR OrthoDB; 654191at2759; -. DR PAN-GO; Q9C035; 9 GO annotations based on evolutionary models. DR PhylomeDB; Q9C035; -. DR BRENDA; 2.3.2.27; 2681. DR PathwayCommons; Q9C035; -. DR Reactome; R-HSA-877300; Interferon gamma signaling. DR SignaLink; Q9C035; -. DR SIGNOR; Q9C035; -. DR UniPathway; UPA00143; -. DR Agora; ENSG00000132256; -. DR BioGRID-ORCS; 85363; 9 hits in 1196 CRISPR screens. DR CD-CODE; 1C4BF022; Cytoplasmic bodies. DR ChiTaRS; TRIM5; human. DR EvolutionaryTrace; Q9C035; -. DR GeneWiki; TRIM5alpha; -. DR GenomeRNAi; 85363; -. DR Pharos; Q9C035; Tbio. DR PRO; PR:Q9C035; -. DR Proteomes; UP000005640; Chromosome 11. DR RNAct; Q9C035; protein. DR Bgee; ENSG00000132256; Expressed in sural nerve and 156 other cell types or tissues. DR ExpressionAtlas; Q9C035; baseline and differential. DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB. DR GO; GO:0005829; C:cytosol; IDA:HPA. DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell. DR GO; GO:0000932; C:P-body; IDA:UniProtKB. DR GO; GO:0042802; F:identical protein binding; IPI:IntAct. DR GO; GO:0038187; F:pattern recognition receptor activity; IDA:UniProtKB. DR GO; GO:0042803; F:protein homodimerization activity; IPI:UniProtKB. DR GO; GO:0019901; F:protein kinase binding; IPI:UniProtKB. DR GO; GO:0030674; F:protein-macromolecule adaptor activity; IPI:UniProtKB. DR GO; GO:0003713; F:transcription coactivator activity; IDA:ARUK-UCL. DR GO; GO:0061630; F:ubiquitin protein ligase activity; IBA:GO_Central. DR GO; GO:0004842; F:ubiquitin-protein transferase activity; IDA:UniProtKB. DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-KW. DR GO; GO:0002218; P:activation of innate immune response; IDA:UniProtKB. DR GO; GO:0006914; P:autophagy; IDA:UniProtKB. DR GO; GO:0051607; P:defense response to virus; TAS:UniProtKB. DR GO; GO:0046597; P:host-mediated suppression of symbiont invasion; IDA:UniProtKB. DR GO; GO:0045087; P:innate immune response; IDA:UniProtKB. DR GO; GO:0043123; P:positive regulation of canonical NF-kappaB signal transduction; IDA:UniProtKB. DR GO; GO:0043410; P:positive regulation of MAPK cascade; IMP:UniProtKB. DR GO; GO:0070534; P:protein K63-linked ubiquitination; IDA:UniProtKB. DR GO; GO:0010468; P:regulation of gene expression; IBA:GO_Central. DR GO; GO:0031664; P:regulation of lipopolysaccharide-mediated signaling pathway; IMP:UniProtKB. DR GO; GO:0032880; P:regulation of protein localization; IMP:UniProtKB. DR GO; GO:0046596; P:regulation of viral entry into host cell; IBA:GO_Central. DR GO; GO:0044790; P:suppression of viral release by host; IDA:UniProtKB. DR CDD; cd19761; Bbox2_TRIM5-like; 1. DR CDD; cd16591; RING-HC_TRIM5-like_C-IV; 1. DR CDD; cd15822; SPRY_PRY_TRIM5; 1. DR FunFam; 2.60.120.920:FF:000023; Tripartite motif-containing 5 (Predicted); 1. DR FunFam; 3.30.160.60:FF:000386; Tripartite motif-containing 5 (Predicted); 1. DR FunFam; 3.30.40.10:FF:000144; Tripartite motif-containing 5 (Predicted); 1. DR Gene3D; 2.60.120.920; -; 1. DR Gene3D; 3.30.160.60; Classic Zinc Finger; 1. DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1. DR InterPro; IPR001870; B30.2/SPRY. DR InterPro; IPR043136; B30.2/SPRY_sf. DR InterPro; IPR003879; Butyrophylin_SPRY. DR InterPro; IPR013320; ConA-like_dom_sf. DR InterPro; IPR003877; SPRY_dom. DR InterPro; IPR050143; TRIM/RBCC. DR InterPro; IPR027370; Znf-RING_euk. DR InterPro; IPR000315; Znf_B-box. DR InterPro; IPR001841; Znf_RING. DR InterPro; IPR013083; Znf_RING/FYVE/PHD. DR InterPro; IPR017907; Znf_RING_CS. DR PANTHER; PTHR24103; E3 UBIQUITIN-PROTEIN LIGASE TRIM; 1. DR Pfam; PF00622; SPRY; 1. DR Pfam; PF00643; zf-B_box; 1. DR Pfam; PF13445; zf-RING_UBOX; 1. DR PRINTS; PR01407; BUTYPHLNCDUF. DR SMART; SM00336; BBOX; 1. DR SMART; SM00184; RING; 1. DR SMART; SM00449; SPRY; 1. DR SUPFAM; SSF57845; B-box zinc-binding domain; 1. DR SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 1. DR SUPFAM; SSF57850; RING/U-box; 1. DR PROSITE; PS50188; B302_SPRY; 1. DR PROSITE; PS50119; ZF_BBOX; 1. DR PROSITE; PS00518; ZF_RING_1; 1. DR PROSITE; PS50089; ZF_RING_2; 1. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Alternative splicing; Antiviral defense; KW Autophagy; Coiled coil; Cytoplasm; Host-virus interaction; Immunity; KW Innate immunity; Metal-binding; Nucleus; Phosphoprotein; KW Proteomics identification; Reference proteome; Transferase; KW Ubl conjugation; Ubl conjugation pathway; Zinc; Zinc-finger. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0007744|PubMed:22223895" FT CHAIN 2..493 FT /note="Tripartite motif-containing protein 5" FT /id="PRO_0000056201" FT DOMAIN 281..493 FT /note="B30.2/SPRY" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00548" FT ZN_FING 15..59 FT /note="RING-type" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175" FT ZN_FING 90..132 FT /note="B box-type" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024" FT REGION 185..198 FT /note="Required for interaction with GABARAP and for FT autophagy" FT /evidence="ECO:0000250|UniProtKB:Q0PF16" FT COILED 130..241 FT /evidence="ECO:0000255" FT BINDING 95 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024" FT BINDING 98 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024" FT BINDING 117 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024" FT BINDING 123 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024" FT MOD_RES 2 FT /note="N-acetylalanine" FT /evidence="ECO:0007744|PubMed:22223895" FT MOD_RES 86 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT VAR_SEQ 249..271 FT /note="GVDGVIKRTENVTLKKPETFPKN -> DGERDLEEARNFSKKSKESVSSS FT (in isoform Epsilon)" FT /evidence="ECO:0000303|PubMed:11331580, FT ECO:0000303|PubMed:21632761" FT /id="VSP_009016" FT VAR_SEQ 249..257 FT /note="GVDGVIKRT -> VKSGKKPEH (in isoform Iota)" FT /evidence="ECO:0000305" FT /id="VSP_044095" FT VAR_SEQ 258..493 FT /note="Missing (in isoform Iota)" FT /evidence="ECO:0000305" FT /id="VSP_044096" FT VAR_SEQ 272..493 FT /note="Missing (in isoform Epsilon)" FT /evidence="ECO:0000303|PubMed:11331580, FT ECO:0000303|PubMed:21632761" FT /id="VSP_009017" FT VAR_SEQ 299..347 FT /note="VDVTVAPNNISCAVISEDKRQVSSPKPQIIYGARGTRYQTFVNFNYCTG -> FT GKEKSHYHKPPCGLSLLLSLSFRILCSLLGSCFKIYDSPSKTHITYPSL (in FT isoform Gamma)" FT /evidence="ECO:0000303|PubMed:11331580, FT ECO:0000303|PubMed:15489334" FT /id="VSP_009012" FT VAR_SEQ 299..326 FT /note="VDVTVAPNNISCAVISEDKRQVSSPKPQ -> GWSAMARSRFTATSTSQIQA FT ILLPQPPK (in isoform Delta)" FT /evidence="ECO:0000303|PubMed:11331580" FT /id="VSP_009014" FT VAR_SEQ 327..493 FT /note="Missing (in isoform Delta)" FT /evidence="ECO:0000303|PubMed:11331580" FT /id="VSP_009015" FT VAR_SEQ 348..493 FT /note="Missing (in isoform Gamma)" FT /evidence="ECO:0000303|PubMed:11331580, FT ECO:0000303|PubMed:15489334" FT /id="VSP_009013" FT VAR_SEQ 390..400 FT /note="NENYQPKYGYW -> KRFMILLPRHT (in isoform Beta)" FT /evidence="ECO:0000303|PubMed:11331580" FT /id="VSP_009010" FT VAR_SEQ 401..493 FT /note="Missing (in isoform Beta)" FT /evidence="ECO:0000303|PubMed:11331580" FT /id="VSP_009011" FT VARIANT 31 FT /note="G -> S (in dbSNP:rs59896509)" FT /evidence="ECO:0000269|Ref.9" FT /id="VAR_060707" FT VARIANT 43 FT /note="H -> Y (in dbSNP:rs3740996)" FT /evidence="ECO:0000269|PubMed:16401428, ECO:0000269|Ref.9" FT /id="VAR_017397" FT VARIANT 58 FT /note="C -> Y (in dbSNP:rs61432120)" FT /evidence="ECO:0000269|Ref.9" FT /id="VAR_060708" FT VARIANT 110 FT /note="G -> E (in dbSNP:rs56348930)" FT /evidence="ECO:0000269|Ref.9" FT /id="VAR_060709" FT VARIANT 112 FT /note="V -> F (in dbSNP:rs11601507)" FT /evidence="ECO:0000269|Ref.9" FT /id="VAR_030154" FT VARIANT 136 FT /note="R -> Q (in dbSNP:rs10838525)" FT /evidence="ECO:0000269|PubMed:11331580, FT ECO:0000269|PubMed:14702039, ECO:0000269|PubMed:18312418, FT ECO:0000269|Ref.9" FT /id="VAR_017398" FT VARIANT 249 FT /note="G -> D (in dbSNP:rs11038628)" FT /evidence="ECO:0000269|PubMed:16401428, ECO:0000269|Ref.9" FT /id="VAR_030155" FT VARIANT 419 FT /note="H -> Y (in dbSNP:rs28381981)" FT /evidence="ECO:0000269|Ref.9" FT /id="VAR_030156" FT VARIANT 467 FT /note="C -> S (in dbSNP:rs59218593)" FT /evidence="ECO:0000269|Ref.9" FT /id="VAR_060710" FT VARIANT 479 FT /note="P -> L (in dbSNP:rs7104422)" FT /evidence="ECO:0000269|Ref.9" FT /id="VAR_030157" FT MUTAGEN 15 FT /note="C->A: Abolishes E3 ligase activity." FT /evidence="ECO:0000269|PubMed:18312418" FT MUTAGEN 332 FT /note="R->A,G,H,P,Q,S: Increases strongly cell restriction FT against HIV-1 and SIVmac infection." FT /evidence="ECO:0000269|PubMed:16809279" FT MUTAGEN 332 FT /note="R->D,E,L: Increases strongly cell restriction FT against HIV-1 infection." FT /evidence="ECO:0000269|PubMed:16809279" FT MUTAGEN 332 FT /note="R->K: No effect on HIV-1 and SIVmac infection." FT /evidence="ECO:0000269|PubMed:16809279" FT CONFLICT 76 FT /note="I -> L (in Ref. 2; BAB55218)" FT /evidence="ECO:0000305" FT CONFLICT 130 FT /note="L -> P (in Ref. 2; BAB55218)" FT /evidence="ECO:0000305" FT TURN 16..18 FT /evidence="ECO:0007829|PDB:2ECV" FT STRAND 29..31 FT /evidence="ECO:0007829|PDB:2ECV" FT HELIX 38..48 FT /evidence="ECO:0007829|PDB:2ECV" FT TURN 56..58 FT /evidence="ECO:0007829|PDB:2ECV" FT STRAND 64..66 FT /evidence="ECO:0007829|PDB:2ECV" FT STRAND 92..94 FT /evidence="ECO:0007829|PDB:2YRG" FT TURN 96..98 FT /evidence="ECO:0007829|PDB:2YRG" FT STRAND 104..106 FT /evidence="ECO:0007829|PDB:2YRG" FT TURN 107..109 FT /evidence="ECO:0007829|PDB:2YRG" FT STRAND 111..113 FT /evidence="ECO:0007829|PDB:2YRG" FT HELIX 115..118 FT /evidence="ECO:0007829|PDB:2YRG" FT TURN 121..125 FT /evidence="ECO:0007829|PDB:2YRG" FT STRAND 128..130 FT /evidence="ECO:0007829|PDB:2YRG" SQ SEQUENCE 493 AA; 56338 MW; 8E61AAFD508AF6C0 CRC64; MASGILVNVK EEVTCPICLE LLTQPLSLDC GHSFCQACLT ANHKKSMLDK GESSCPVCRI SYQPENIRPN RHVANIVEKL REVKLSPEGQ KVDHCARHGE KLLLFCQEDG KVICWLCERS QEHRGHHTFL TEEVAREYQV KLQAALEMLR QKQQEAEELE ADIREEKASW KTQIQYDKTN VLADFEQLRD ILDWEESNEL QNLEKEEEDI LKSLTNSETE MVQQTQSLRE LISDLEHRLQ GSVMELLQGV DGVIKRTENV TLKKPETFPK NQRRVFRAPD LKGMLEVFRE LTDVRRYWVD VTVAPNNISC AVISEDKRQV SSPKPQIIYG ARGTRYQTFV NFNYCTGILG SQSITSGKHY WEVDVSKKTA WILGVCAGFQ PDAMCNIEKN ENYQPKYGYW VIGLEEGVKC SAFQDSSFHT PSVPFIVPLS VIICPDRVGV FLDYEACTVS FFNITNHGFL IYKFSHCSFS QPVFPYLNPR KCGVPMTLCS PSS //