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TRIM5_GORGO
ID   TRIM5_GORGO             Reviewed;         493 AA.
AC   Q5C8T6; Q0NNY0; Q3ZEE7; Q50EX0; Q5D7I7;
DT   23-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT   12-APR-2005, sequence version 1.
DT   03-AUG-2022, entry version 105.
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   Gorilla gorilla gorilla (Western lowland gorilla).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Gorilla.
OX   NCBI_TaxID=9595;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
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   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=15857996; DOI=10.1128/jvi.79.10.6111-6121.2005;
RA   Song B., Gold B., O'Huigin C., Javanbakht H., Li X., Stremlau M.,
RA   Winkler C., Dean M., Sodroski J.;
RT   "The B30.2(SPRY) domain of the retroviral restriction factor TRIM5alpha
RT   exhibits lineage-specific length and sequence variation in primates.";
RL   J. Virol. 79:6111-6121(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=AG05251;
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 [GENOMIC DNA].
RX   PubMed=16460575; DOI=10.1186/1742-4690-3-11;
RA   Ortiz M., Bleiber G., Martinez R., Kaessmann H., Telenti A.;
RT   "Patterns of evolution of host proteins involved in retroviral
RT   pathogenesis.";
RL   Retrovirology 3:11-11(2006).
RN   [5]
RP   SEQUENCE REVISION TO 384-385; 289; 396 AND 420.
RA   Ortiz M., Bleiber G., Martinez R., Telenti A.;
RL   Submitted (FEB-2005) to the EMBL/GenBank/DDBJ databases.
RN   [6]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 300-493.
RX   PubMed=16912305; DOI=10.1128/jvi.00688-06;
RA   Ohkura S., Yap M.W., Sheldon T., Stoye J.P.;
RT   "All three variable regions of the TRIM5alpha B30.2 domain can contribute
RT   to the specificity of retrovirus restriction.";
RL   J. Virol. 80:8554-8565(2006).
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. Plays a role in regulating autophagy
CC       through activation of autophagy regulator BECN1 by causing its
CC       dissociation from its inhibitors BCL2 and TAB2.
CC       {ECO:0000250|UniProtKB:Q9C035}.
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 BTBD1 and BTBD2. Interacts with
CC       PSMC4, PSMC5, PSMD7 and HSPA8/HSC70. Interacts (via B30.2/SPRY domain)
CC       with HSPA1A/B. Interacts with PSMC2, MAP3K7/TAK1, TAB2 and TAB3.
CC       Interacts with SQSTM1. Interacts with TRIM6 and TRIM34. Interacts with
CC       ULK1 (phosphorylated form), GABARAP, GABARAPL1, GABARAPL2, MAP1LC3A,
CC       MAP1LC3C and BECN1. {ECO:0000250|UniProtKB:Q0PF16,
CC       ECO:0000250|UniProtKB:Q9C035}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q0PF16}. Nucleus
CC       {ECO:0000250|UniProtKB:Q0PF16}. Note=Predominantly localizes in
CC       cytoplasmic bodies. Localization may be influenced by the coexpression
CC       of other TRIM proteins, hence partial nuclear localization is observed
CC       in the presence of TRIM22 or TRIM27. In cytoplasmic bodies, colocalizes
CC       with proteasomal subunits and SQSTM1. {ECO:0000250|UniProtKB:Q0PF16}.
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. The coiled coil domain is
CC       important for higher order multimerization by promoting the initial
CC       dimerization. {ECO:0000250|UniProtKB:Q0PF16,
CC       ECO:0000250|UniProtKB:Q9C035}.
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 (By similarity). {ECO:0000250}.
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. {ECO:0000250}.
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 (By similarity).
CC       {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the TRIM/RBCC family. {ECO:0000305}.
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DR   EMBL; AY899872; AAX86680.1; -; Genomic_DNA.
DR   EMBL; AY899866; AAX86680.1; JOINED; Genomic_DNA.
DR   EMBL; AY899867; AAX86680.1; JOINED; Genomic_DNA.
DR   EMBL; AY899868; AAX86680.1; JOINED; Genomic_DNA.
DR   EMBL; AY899869; AAX86680.1; JOINED; Genomic_DNA.
DR   EMBL; AY899870; AAX86680.1; JOINED; Genomic_DNA.
DR   EMBL; AY899871; AAX86680.1; JOINED; Genomic_DNA.
DR   EMBL; AY710300; AAW55819.1; -; Genomic_DNA.
DR   EMBL; AY740620; AAW72448.1; -; mRNA.
DR   EMBL; DQ298178; ABC25561.1; -; Genomic_DNA.
DR   EMBL; AY843510; AAV91981.1; -; Genomic_DNA.
DR   EMBL; AY923178; AAY23160.2; -; Genomic_DNA.
DR   EMBL; DQ437600; ABE28402.1; -; Genomic_DNA.
DR   RefSeq; NP_001266478.1; NM_001279549.1.
DR   AlphaFoldDB; Q5C8T6; -.
DR   BMRB; Q5C8T6; -.
DR   SMR; Q5C8T6; -.
DR   STRING; 9593.ENSGGOP00000025332; -.
DR   GeneID; 101133340; -.
DR   KEGG; ggo:101133340; -.
DR   CTD; 85363; -.
DR   eggNOG; KOG2177; Eukaryota.
DR   InParanoid; Q5C8T6; -.
DR   UniPathway; UPA00143; -.
DR   Proteomes; UP000001519; Unplaced.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
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; ISS:UniProtKB.
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; IEA:UniProtKB-KW.
DR   GO; GO:0051607; P:defense response to virus; IEA:UniProtKB-KW.
DR   GO; GO:0045087; P:innate immune response; IBA:GO_Central.
DR   GO; GO:0010508; P:positive regulation of autophagy; IBA:GO_Central.
DR   GO; GO:0043123; P:positive regulation of I-kappaB kinase/NF-kappaB signaling; ISS: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; ISS: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; IBA:GO_Central.
DR   GO; GO:0046596; P:regulation of viral entry into host cell; IBA:GO_Central.
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   2: Evidence at transcript level;
KW   Acetylation; Antiviral defense; Autophagy; Coiled coil; Cytoplasm;
KW   Immunity; Innate immunity; Metal-binding; Nucleus; Phosphoprotein;
KW   Reference proteome; Transferase; Ubl conjugation; Ubl conjugation pathway;
KW   Zinc; Zinc-finger.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250|UniProtKB:Q9C035"
FT   CHAIN           2..493
FT                   /note="Tripartite motif-containing protein 5"
FT                   /id="PRO_0000273458"
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          131..240
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:0000250|UniProtKB:Q9C035"
FT   MOD_RES         86
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9C035"
FT   CONFLICT        44
FT                   /note="E -> K (in Ref. 1; AAX86680, 3; ABC25561/AAV91981
FT                   and 4; AAY23160)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        138
FT                   /note="C -> Y (in Ref. 1; AAX86680, 3; ABC25561/AAV91981
FT                   and 4; AAY23160)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        237
FT                   /note="H -> R (in Ref. 4; AAY23160)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        253
FT                   /note="V -> I (in Ref. 4; AAY23160)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        483
FT                   /note="R -> K (in Ref. 4; AAY23160)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   493 AA;  56382 MW;  6ECD040ECD6B89CD CRC64;
     MASGILVNVK EEVTCPICLE LLTQPLSLDC GHSFCQACLT ANHEKSMLDK GESSCPVCRI
     SYQPENIRPN RHVANIVEKL REVKLSPEGQ KVDHCARHGE KLLLFCQEDG KVICWLCERS
     QEHRGHHTFL TEEVAQECQV KLQAALEMLR QKQQEAEELE ADIREEKASW KTQIQYDKTN
     VLADFEQLRD ILDWEESNEL QNLEKEEEDI LKRLTKSETE MVQQTQSVRE LISDLEHRLQ
     GSVMELLQGV DGVIKRMENV TLKKPETFPK NRRRVFRAPD LKGMLEVFRE LTDVRRYWVD
     VTVAPNNISC AVISEDMRQV SSPKPQIIYG AQGTRYQTFM NFNYCTGILG SQSITSGKHY
     WEVDVSKKSA WILGVCAGFQ PDATCNIEKN ENYQPKYGYW VIGLEEGVKC SAFQDGSFHT
     PSAPFIVPLS VIICPDRVGV FLDYEACTVS FFNITNHGFL IYKFSHCSFS QPVFPYLNPR
     KCRVPMTLCS PSS
 
 
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