TRIM5_MACMU
ID TRIM5_MACMU Reviewed; 497 AA.
AC Q0PF16; Q0PF17; Q2YEN1; Q6GX25; Q6QWE9; Q6QWF0;
DT 23-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 121.
DE RecName: Full=Tripartite motif-containing protein 5;
DE EC=2.3.2.27;
DE AltName: Full=RING-type E3 ubiquitin transferase TRIM5 {ECO:0000305};
DE AltName: Full=TRIM5alpha;
GN Name=TRIM5;
OS Macaca mulatta (Rhesus macaque).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Macaca.
OX NCBI_TaxID=9544;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
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 [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND ALTERNATIVE SPLICING (ISOFORM 1).
RX PubMed=16226405; DOI=10.1016/j.gene.2005.06.045;
RA Liu H.L., Wang Y.Q., Liao C.H., Kuang Y.Q., Zheng Y.T., Su B.;
RT "Adaptive evolution of primate TRIM5alpha, a gene restricting HIV-1
RT infection.";
RL Gene 362:109-116(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX PubMed=17142324; DOI=10.1073/pnas.0605838103;
RA Newman R.M., Hall L., Connole M., Chen G.L., Sato S., Yuste E., Diehl W.,
RA Hunter E., Kaur A., Miller G.M., Johnson W.E.;
RT "Balancing selection and the evolution of functional polymorphism in Old
RT World monkey TRIM5alpha.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:19134-19139(2006).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
RA Stremlau M.H., Sodroski J.;
RL Submitted (JAN-2004) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RA Miller C.J., Dutra J.C.;
RL Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP TRIMERIZATION.
RX PubMed=16254380; DOI=10.1128/jvi.79.22.14446-14450.2005;
RA Mische C.C., Javanbakht H., Song B., Diaz-Griffero F., Stremlau M.,
RA Strack B., Si Z., Sodroski J.;
RT "Retroviral restriction factor TRIM5alpha is a trimer.";
RL J. Virol. 79:14446-14450(2005).
RN [7]
RP TRIMERIZATION.
RX PubMed=16808955; DOI=10.1016/j.virol.2006.05.017;
RA Javanbakht H., Yuan W., Yeung D.F., Song B., Diaz-Griffero F., Li Y.,
RA Li X., Stremlau M., Sodroski J.;
RT "Characterization of TRIM5alpha trimerization and its contribution to human
RT immunodeficiency virus capsid binding.";
RL Virology 353:234-246(2006).
RN [8]
RP SUBUNIT, SUBCELLULAR LOCATION, AND DOMAIN.
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 [9]
RP INTERACTION WITH HSPA1A/B AND HSPA8, AND AUTOUBIQUITINATION.
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 [10]
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 [11]
RP REVIEW.
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 [12]
RP INTERACTION WITH TRIM6 AND TRIM34, MUTAGENESIS OF ILE-165; TRP-172;
RP ILE-176; LEU-194; LEU-202; LEU-205; LEU-216; SER-219; MET-230; ILE-234;
RP LEU-237 AND 247-ASP--LEU-249, AND DOMAIN.
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 [13]
RP FUNCTION, DOMAIN RING, SUBUNIT, AND AUTOUBIQUITINATION.
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 [14]
RP SUBUNIT.
RX PubMed=21187419; DOI=10.1073/pnas.1013426108;
RA Ganser-Pornillos B.K., Chandrasekaran V., Pornillos O., Sodroski J.G.,
RA Sundquist W.I., Yeager M.;
RT "Hexagonal assembly of a restricting TRIM5alpha protein.";
RL Proc. Natl. Acad. Sci. U.S.A. 108:534-539(2011).
RN [15]
RP INTERACTION WITH PSMC2; PSMC4; PSMC5 AND PSMD7, AND SUBCELLULAR LOCATION.
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 [16]
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 [17]
RP REVIEW.
RX PubMed=21994740; DOI=10.3390/v3050423;
RA Diaz-Griffero F.;
RT "Caging the beast: TRIM5-binding to the HIV-1 core.";
RL Viruses 3:423-428(2011).
RN [18]
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 [19]
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 [20]
RP REVIEW.
RX PubMed=22701176; DOI=10.1155/2012/426840;
RA Luban J.;
RT "TRIM5 and the regulation of HIV-1 infectivity.";
RL Mol. Biol. Int. 2012:426840-426840(2012).
RN [21]
RP FUNCTION, INTERACTION WITH BECN1; SQSTM1 AND GABARAP, AND SUBCELLULAR
RP 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 [22]
RP X-RAY CRYSTALLOGRAPHY (1.55 ANGSTROMS) OF 292-497.
RX PubMed=22847415; DOI=10.1073/pnas.1203536109;
RA Biris N., Yang Y., Taylor A.B., Tomashevski A., Guo M., Hart P.J.,
RA Diaz-Griffero F., Ivanov D.N.;
RT "Structure of the rhesus monkey TRIM5alpha PRYSPRY domain, the HIV capsid
RT recognition module.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:13278-13283(2012).
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 human
CC immunodeficiency virus type 1 (HIV-1) and simian immunodeficiency virus
CC (SIV-agm). Plays a role in regulating autophagy through activation of
CC autophagy regulator BECN1 by causing its dissociation from its
CC inhibitors BCL2 and TAB2 (PubMed:25127057). Also plays a role in
CC autophagy by acting as a selective autophagy receptor which recognizes
CC and targets HIV-1 capsid protein p24 for autophagic destruction
CC (PubMed:25127057). {ECO:0000269|PubMed:21035162,
CC ECO:0000269|PubMed:21734049, ECO:0000269|PubMed:22291694,
CC 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. Interacts with MAP3K7/TAK1, TAB2 and TAB3 (By
CC similarity). Interacts with HSPA8/HSC70, PSMC2, PSMC4, PSMC5 and PSMD7
CC (PubMed:20053985, PubMed:22078707). Interacts with SQSTM1
CC (PubMed:20357094, PubMed:25127057). Interacts (via B30.2/SPRY domain)
CC with HSPA1A/B. Interacts with TRIM6 and TRIM34 (PubMed:21680743).
CC Interacts with BECN1; GABARAP (PubMed:25127057). Interacts with ULK1
CC (phosphorylated form), GABARAPL1, GABARAPL2, MAP1LC3A and MAP1LC3C (By
CC similarity). {ECO:0000250|UniProtKB:Q9C035,
CC ECO:0000269|PubMed:17156811, ECO:0000269|PubMed:20053985,
CC ECO:0000269|PubMed:20357094, ECO:0000269|PubMed:21187419,
CC ECO:0000269|PubMed:21680743, ECO:0000269|PubMed:21734049,
CC ECO:0000269|PubMed:22078707, ECO:0000269|PubMed:25127057}.
CC -!- INTERACTION:
CC Q0PF16; Q0PF16: TRIM5; NbExp=3; IntAct=EBI-923856, EBI-923856;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:17156811}. Nucleus
CC {ECO:0000269|PubMed:17156811}. Note=Predominantly localizes in
CC cytoplasmic bodies (PubMed:20357094, PubMed:22078707). 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 (PubMed:17156811). In cytoplasmic bodies, colocalizes with proteasomal
CC subunits and SQSTM1 (PubMed:20357094). {ECO:0000269|PubMed:17156811,
CC ECO:0000269|PubMed:20357094, ECO:0000269|PubMed:22078707}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q0PF16-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q0PF16-2; Sequence=VSP_022569, VSP_022570;
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 (By similarity). The coiled
CC coil domain is important for higher order multimerization by promoting
CC the initial dimerization (PubMed:21680743).
CC {ECO:0000250|UniProtKB:Q9C035, ECO:0000269|PubMed:21680743}.
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. {ECO:0000269|PubMed:21734049}.
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:17156811, ECO:0000269|PubMed:21734049}.
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. {ECO:0000250}.
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:20053985, ECO:0000269|PubMed:21734049}.
CC -!- SIMILARITY: Belongs to the TRIM/RBCC family. {ECO:0000305}.
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DR EMBL; AY625001; AAT48102.1; -; mRNA.
DR EMBL; AY899886; AAX86682.1; -; Genomic_DNA.
DR EMBL; AY899880; AAX86682.1; JOINED; Genomic_DNA.
DR EMBL; AY899881; AAX86682.1; JOINED; Genomic_DNA.
DR EMBL; AY899882; AAX86682.1; JOINED; Genomic_DNA.
DR EMBL; AY899883; AAX86682.1; JOINED; Genomic_DNA.
DR EMBL; AY899884; AAX86682.1; JOINED; Genomic_DNA.
DR EMBL; AY899885; AAX86682.1; JOINED; Genomic_DNA.
DR EMBL; EF113914; ABL14041.1; -; mRNA.
DR EMBL; AY523632; AAS48505.1; -; mRNA.
DR EMBL; AY523633; AAS48506.1; -; mRNA.
DR EMBL; DQ842020; ABG67966.1; -; mRNA.
DR EMBL; DQ842021; ABG67967.1; -; mRNA.
DR RefSeq; NP_001028082.1; NM_001032910.1.
DR PDB; 2LM3; NMR; -; A=292-497.
DR PDB; 3UV9; X-ray; 1.55 A; A=292-325, A=350-497.
DR PDB; 4B3N; X-ray; 3.30 A; A/B=275-493.
DR PDB; 4TKP; X-ray; 2.08 A; B=2-92.
DR PDB; 5EIU; X-ray; 1.91 A; A/D=89-159, A/D=226-265.
DR PDB; 5F7T; X-ray; 2.29 A; E/F/H/L=89-159, E/F/H/L=226-265.
DR PDB; 5IEA; X-ray; 3.26 A; A/B/C/D/F/K=89-159, A/B/C/D/F/K=226-265.
DR PDB; 5K3Q; X-ray; 1.80 A; A/B/C/D=94-154, A/B/C/D=229-261.
DR PDB; 5W9A; X-ray; 2.74 A; A/B=95-287.
DR PDBsum; 2LM3; -.
DR PDBsum; 3UV9; -.
DR PDBsum; 4B3N; -.
DR PDBsum; 4TKP; -.
DR PDBsum; 5EIU; -.
DR PDBsum; 5F7T; -.
DR PDBsum; 5IEA; -.
DR PDBsum; 5K3Q; -.
DR PDBsum; 5W9A; -.
DR AlphaFoldDB; Q0PF16; -.
DR BMRB; Q0PF16; -.
DR SMR; Q0PF16; -.
DR BioGRID; 695095; 11.
DR IntAct; Q0PF16; 1.
DR STRING; 9544.ENSMMUP00000000454; -.
DR GeneID; 574288; -.
DR KEGG; mcc:574288; -.
DR CTD; 85363; -.
DR eggNOG; KOG2177; Eukaryota.
DR HOGENOM; CLU_013137_0_3_1; -.
DR InParanoid; Q0PF16; -.
DR OMA; LTNFNYC; -.
DR OrthoDB; 740493at2759; -.
DR TreeFam; TF338674; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000006718; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IMP:UniProtKB.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005654; C:nucleoplasm; IBA:GO_Central.
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; ISS:UniProtKB.
DR GO; GO:0042803; F:protein homodimerization activity; IBA:GO_Central.
DR GO; GO:0019901; F:protein kinase binding; IBA:GO_Central.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IBA:GO_Central.
DR GO; GO:0004842; F:ubiquitin-protein transferase activity; ISS:UniProtKB.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0002218; P:activation of innate immune response; ISS:UniProtKB.
DR GO; GO:0006914; P:autophagy; IDA:UniProtKB.
DR GO; GO:0051607; P:defense response to virus; TAS:UniProtKB.
DR GO; GO:0045087; P:innate immune response; IDA:UniProtKB.
DR GO; GO:0046597; P:negative regulation of viral entry into host cell; IDA:UniProtKB.
DR GO; GO:0045071; P:negative regulation of viral genome replication; IMP:UniProtKB.
DR GO; GO:0032897; P:negative regulation of viral transcription; IDA:UniProtKB.
DR GO; GO:0010508; P:positive regulation of autophagy; IBA:GO_Central.
DR GO; GO:0051091; P:positive regulation of DNA-binding transcription factor activity; IDA:UniProtKB.
DR GO; GO:0043123; P:positive regulation of I-kappaB kinase/NF-kappaB signaling; IDA:UniProtKB.
DR GO; GO:0043410; P:positive regulation of MAPK cascade; ISS:UniProtKB.
DR GO; GO:0051092; P:positive regulation of NF-kappaB transcription factor activity; IDA:UniProtKB.
DR GO; GO:0070534; P:protein K63-linked ubiquitination; ISS:UniProtKB.
DR GO; GO:0000209; P:protein polyubiquitination; IBA:GO_Central.
DR GO; GO:0016567; P:protein ubiquitination; IBA:GO_Central.
DR GO; GO:0010468; P:regulation of gene expression; IBA:GO_Central.
DR GO; GO:0031664; P:regulation of lipopolysaccharide-mediated signaling pathway; ISS: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 Gene3D; 2.60.120.920; -; 1.
DR Gene3D; 3.30.40.10; -; 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; IPR027370; Znf-RING_LisH.
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 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; SSF49899; SSF49899; 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; Immunity; Innate immunity;
KW Metal-binding; Nucleus; Phosphoprotein; Reference proteome; Transferase;
KW Ubl conjugation; Ubl conjugation pathway; Zinc; Zinc-finger.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q9C035"
FT CHAIN 2..497
FT /note="Tripartite motif-containing protein 5"
FT /id="PRO_0000273465"
FT DOMAIN 283..497
FT /note="B30.2/SPRY"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00548"
FT ZN_FING 15..60
FT /note="RING-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT ZN_FING 92..133
FT /note="B box-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT REGION 187..200
FT /note="Required for interaction with GABARAP and for
FT autophagy"
FT /evidence="ECO:0000269|PubMed:25127057"
FT COILED 137..225
FT /evidence="ECO:0000255"
FT BINDING 97
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT BINDING 100
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT BINDING 119
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT BINDING 125
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:0000250|UniProtKB:Q9C035"
FT MOD_RES 87
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9C035"
FT VAR_SEQ 301..333
FT /note="VDVTLAPNNISHAVIAEDKRQVSSRNPQIMYQA -> GKEKSHYHQPPCGLS
FT LLLSLSFRILYSLLGLVF (in isoform 2)"
FT /evidence="ECO:0000303|Ref.4"
FT /id="VSP_022569"
FT VAR_SEQ 334..497
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|Ref.4"
FT /id="VSP_022570"
FT MUTAGEN 165
FT /note="I->K: No effect on dimerization or higher order
FT self-association."
FT /evidence="ECO:0000269|PubMed:21680743"
FT MUTAGEN 172
FT /note="W->K: No effect on dimerization or higher order
FT self-association; when associated with K-176."
FT /evidence="ECO:0000269|PubMed:21680743"
FT MUTAGEN 176
FT /note="I->K: No effect on dimerization or higher order
FT self-association; when associated with K-172."
FT /evidence="ECO:0000269|PubMed:21680743"
FT MUTAGEN 194
FT /note="L->K: Fails to dimerise and exhibits reduced higher
FT order self association."
FT /evidence="ECO:0000269|PubMed:21680743"
FT MUTAGEN 202
FT /note="L->K: No effect on dimerization or higher order
FT self-association."
FT /evidence="ECO:0000269|PubMed:21680743"
FT MUTAGEN 205
FT /note="L->K: No effect on dimerization or higher order
FT self-association."
FT /evidence="ECO:0000269|PubMed:21680743"
FT MUTAGEN 216
FT /note="L->K: No effect on dimerization or higher order
FT self-association."
FT /evidence="ECO:0000269|PubMed:21680743"
FT MUTAGEN 219
FT /note="S->K: No effect on dimerization or higher order
FT self-association."
FT /evidence="ECO:0000269|PubMed:21680743"
FT MUTAGEN 230
FT /note="M->K: No effect on dimerization or higher order
FT self-association."
FT /evidence="ECO:0000269|PubMed:21680743"
FT MUTAGEN 234
FT /note="I->K: No effect on dimerization or higher order
FT self-association."
FT /evidence="ECO:0000269|PubMed:21680743"
FT MUTAGEN 237
FT /note="L->K: No effect on dimerization or higher order
FT self-association."
FT /evidence="ECO:0000269|PubMed:21680743"
FT MUTAGEN 247..249
FT /note="DLL->KDD: No effect on dimerization but exhibits a
FT 3-fold decrease in the efficiency of higher order
FT association."
FT /evidence="ECO:0000269|PubMed:21680743"
FT CONFLICT 7
FT /note="L -> V (in Ref. 1; AAT48102)"
FT /evidence="ECO:0000305"
FT CONFLICT 174
FT /note="I -> T (in Ref. 2; AAX86682)"
FT /evidence="ECO:0000305"
FT CONFLICT 177
FT /note="D -> Q (in Ref. 2; AAX86682)"
FT /evidence="ECO:0000305"
FT CONFLICT 184
FT /note="S -> L (in Ref. 2; AAX86682)"
FT /evidence="ECO:0000305"
FT CONFLICT 192
FT /note="E -> D (in Ref. 2; AAX86682)"
FT /evidence="ECO:0000305"
FT CONFLICT 218
FT /note="K -> N (in Ref. 2; AAX86682)"
FT /evidence="ECO:0000305"
FT CONFLICT 221
FT /note="T -> M (in Ref. 5; ABG67967)"
FT /evidence="ECO:0000305"
FT CONFLICT 229..230
FT /note="YM -> SL (in Ref. 2; AAX86682)"
FT /evidence="ECO:0000305"
FT CONFLICT 236
FT /note="E -> D (in Ref. 2; AAX86682 and 5; ABG67966)"
FT /evidence="ECO:0000305"
FT CONFLICT 307
FT /note="P -> T (in Ref. 1; AAT48102, 3; ABL14041 and 4;
FT AAS48505)"
FT /evidence="ECO:0000305"
FT CONFLICT 333
FT /note="A -> S (in Ref. 5; ABG67966)"
FT /evidence="ECO:0000305"
FT CONFLICT 339..341
FT /note="TFP -> Q (in Ref. 5; ABG67966)"
FT /evidence="ECO:0000305"
FT HELIX 6..12
FT /evidence="ECO:0007829|PDB:4TKP"
FT TURN 16..18
FT /evidence="ECO:0007829|PDB:4TKP"
FT STRAND 23..27
FT /evidence="ECO:0007829|PDB:4TKP"
FT STRAND 33..35
FT /evidence="ECO:0007829|PDB:4TKP"
FT HELIX 36..38
FT /evidence="ECO:0007829|PDB:4TKP"
FT TURN 57..59
FT /evidence="ECO:0007829|PDB:4TKP"
FT HELIX 72..79
FT /evidence="ECO:0007829|PDB:4TKP"
FT TURN 98..100
FT /evidence="ECO:0007829|PDB:5K3Q"
FT STRAND 106..108
FT /evidence="ECO:0007829|PDB:5K3Q"
FT TURN 109..112
FT /evidence="ECO:0007829|PDB:5K3Q"
FT STRAND 113..115
FT /evidence="ECO:0007829|PDB:5K3Q"
FT HELIX 117..121
FT /evidence="ECO:0007829|PDB:5K3Q"
FT HELIX 123..125
FT /evidence="ECO:0007829|PDB:5K3Q"
FT STRAND 130..132
FT /evidence="ECO:0007829|PDB:5K3Q"
FT HELIX 133..159
FT /evidence="ECO:0007829|PDB:5EIU"
FT HELIX 226..242
FT /evidence="ECO:0007829|PDB:5EIU"
FT HELIX 245..249
FT /evidence="ECO:0007829|PDB:5EIU"
FT HELIX 252..261
FT /evidence="ECO:0007829|PDB:5EIU"
FT HELIX 282..286
FT /evidence="ECO:0007829|PDB:5W9A"
FT HELIX 292..296
FT /evidence="ECO:0007829|PDB:3UV9"
FT HELIX 297..299
FT /evidence="ECO:0007829|PDB:3UV9"
FT STRAND 319..323
FT /evidence="ECO:0007829|PDB:4B3N"
FT STRAND 327..329
FT /evidence="ECO:0007829|PDB:2LM3"
FT TURN 330..332
FT /evidence="ECO:0007829|PDB:2LM3"
FT STRAND 334..336
FT /evidence="ECO:0007829|PDB:2LM3"
FT STRAND 352..356
FT /evidence="ECO:0007829|PDB:4B3N"
FT STRAND 360..368
FT /evidence="ECO:0007829|PDB:3UV9"
FT STRAND 375..381
FT /evidence="ECO:0007829|PDB:3UV9"
FT TURN 384..390
FT /evidence="ECO:0007829|PDB:3UV9"
FT HELIX 391..394
FT /evidence="ECO:0007829|PDB:3UV9"
FT HELIX 399..401
FT /evidence="ECO:0007829|PDB:3UV9"
FT STRAND 403..409
FT /evidence="ECO:0007829|PDB:3UV9"
FT TURN 410..412
FT /evidence="ECO:0007829|PDB:3UV9"
FT STRAND 413..418
FT /evidence="ECO:0007829|PDB:3UV9"
FT STRAND 429..432
FT /evidence="ECO:0007829|PDB:3UV9"
FT STRAND 440..447
FT /evidence="ECO:0007829|PDB:3UV9"
FT TURN 448..451
FT /evidence="ECO:0007829|PDB:3UV9"
FT STRAND 452..457
FT /evidence="ECO:0007829|PDB:3UV9"
FT TURN 458..462
FT /evidence="ECO:0007829|PDB:3UV9"
FT STRAND 463..468
FT /evidence="ECO:0007829|PDB:3UV9"
FT STRAND 477..482
FT /evidence="ECO:0007829|PDB:3UV9"
FT STRAND 490..492
FT /evidence="ECO:0007829|PDB:4B3N"
SQ SEQUENCE 497 AA; 57299 MW; 950166879B2E1A6F CRC64;
MASGILLNVK EEVTCPICLE LLTEPLSLHC GHSFCQACIT ANHKKSMLYK EGERSCPVCR
ISYQPENIQP NRHVANIVEK LREVKLSPEE GQKVDHCARH GEKLLLFCQE DSKVICWLCE
RSQEHRGHHT FLMEEVAQEY HVKLQTALEM LRQKQQEAEK LEADIREEKA SWKIQIDYDK
TNVSADFEQL REILDWEESN ELQNLEKEEE DILKSLTKSE TEMVQQTQYM RELISELEHR
LQGSMMDLLQ GVDGIIKRIE NMTLKKPKTF HKNQRRVFRA PDLKGMLDMF RELTDARRYW
VDVTLAPNNI SHAVIAEDKR QVSSRNPQIM YQAPGTLFTF PSLTNFNYCT GVLGSQSITS
GKHYWEVDVS KKSAWILGVC AGFQSDAMYN IEQNENYQPK YGYWVIGLQE GVKYSVFQDG
SSHTPFAPFI VPLSVIICPD RVGVFVDYEA CTVSFFNITN HGFLIYKFSQ CSFSKPVFPY
LNPRKCTVPM TLCSPSS
