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TRIM5_SAIBB
ID   TRIM5_SAIBB             Reviewed;         494 AA.
AC   Q5BN31; Q5C8U2;
DT   23-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT   12-APR-2005, sequence version 1.
DT   03-AUG-2022, entry version 92.
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;
DE   AltName: Full=Tripartite motif-containing antiviral factor;
GN   Name=TRIM5;
OS   Saimiri boliviensis boliviensis (Bolivian squirrel monkey).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Platyrrhini; Cebidae;
OC   Saimiriinae; Saimiri.
OX   NCBI_TaxID=39432;
RN   [1]
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   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=16140735; DOI=10.1128/jvi.79.18.11580-11587.2005;
RA   Ylinen L.M., Keckesova Z., Wilson S.J., Ranasinghe S., Towers G.J.;
RT   "Differential restriction of human immunodeficiency virus type 2 and simian
RT   immunodeficiency virus SIVmac by TRIM5alpha alleles.";
RL   J. Virol. 79:11580-11587(2005).
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; AY740614; AAW72442.1; -; mRNA.
DR   EMBL; AY928202; AAX23597.1; -; mRNA.
DR   AlphaFoldDB; Q5BN31; -.
DR   SMR; Q5BN31; -.
DR   STRING; 39432.ENSSBOP00000024105; -.
DR   UniPathway; UPA00143; -.
DR   Proteomes; UP000233220; Whole Genome Shotgun Assembly.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0000932; C:P-body; ISS:UniProtKB.
DR   GO; GO:0038187; F:pattern recognition receptor activity; ISS:UniProtKB.
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; IEA:UniProtKB-KW.
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:0031664; P:regulation of lipopolysaccharide-mediated signaling pathway; ISS: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; 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   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; Reference proteome;
KW   Transferase; Ubl conjugation; Ubl conjugation pathway; Zinc; Zinc-finger.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250|UniProtKB:Q9C035"
FT   CHAIN           2..494
FT                   /note="Tripartite motif-containing protein 5"
FT                   /id="PRO_0000273476"
FT   DOMAIN          280..494
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         91..132
FT                   /note="B box-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT   REGION          186..199
FT                   /note="Required for interaction with GABARAP and for
FT                   autophagy"
FT                   /evidence="ECO:0000250|UniProtKB:Q0PF16"
FT   COILED          132..223
FT                   /evidence="ECO:0000255"
FT   BINDING         96
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT   BINDING         99
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT   BINDING         118
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT   BINDING         124
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   CONFLICT        7
FT                   /note="G -> V (in Ref. 1; AAW72442)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   494 AA;  57148 MW;  7DB557418A38D02D CRC64;
     MASGILGSIK EEVTCPICLE LLTEPLSLDC GHSFCQACIT ANHKESMLHQ GERSCPLCRL
     PYQSENLRPN RHLASIVERL REVMLRPEER QNVDHCARHG EKLLLFCEQD GNIICWLCER
     SQEHRGHNTF LVEEVAQKYR EKLQVALETM RQKQQDAEKL EADVRQEQAS WKIQIQNDKT
     NIMAEFKQLR DILDCEESNE LQNLEKEEKN ILKRLVQSEN DMVLQTQSVR VLISDLERRL
     QGSVVELLQD VDGVIKRIEK VTLQKPKTFL NEKRRVFRAP DLKRMLQVLK ELTEVQRYWA
     HVTLVPSHPS YTIISEDGRQ VRYQKPIRHL LVKVQYFYGV LGSPSITSGK HYWEVDVSNK
     RAWTLGVCVS LKCTANQSVS GTENYQPKNG YWVIGLRNAG NYRAFQSSFE FRDFLAGSRL
     TLSPPLIVPL FMTICPNRVG VFLDYEARTI SFFNVTSNGF LIYKFSDCHF SYPVFPYFNP
     MTCELPMTLC SPSS
 
 
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