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Tripartite motif-containing protein 5 (EC 2.3.2.27) (RING-type E3 ubiquitin transferase TRIM5) (TRIM5alpha)

 TRIM5_ATEGE             Reviewed;         547 AA.
Q5D7I1; Q5C8U0;
23-JAN-2007, integrated into UniProtKB/Swiss-Prot.
29-MAR-2005, sequence version 1.
05-DEC-2018, entry version 78.
RecName: Full=Tripartite motif-containing protein 5;
EC=2.3.2.27;
AltName: Full=RING-type E3 ubiquitin transferase TRIM5 {ECO:0000305};
AltName: Full=TRIM5alpha;
Name=TRIM5;
Ateles geoffroyi (Black-handed spider monkey) (Geoffroy's spider
monkey).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Platyrrhini; Atelidae; Atelinae; Ateles.
NCBI_TaxID=9509;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=15857996; DOI=10.1128/JVI.79.10.6111-6121.2005;
Song B., Gold B., O'Huigin C., Javanbakht H., Li X., Stremlau M.,
Winkler C., Dean M., Sodroski J.;
"The B30.2(SPRY) domain of the retroviral restriction factor
TRIM5alpha exhibits lineage-specific length and sequence variation in
primates.";
J. Virol. 79:6111-6121(2005).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=15689398; DOI=10.1073/pnas.0409853102;
Sawyer S.L., Wu L.I., Emerman M., Malik H.S.;
"Positive selection of primate TRIM5alpha identifies a critical
species-specific retroviral restriction domain.";
Proc. Natl. Acad. Sci. U.S.A. 102:2832-2837(2005).
-!- FUNCTION: Capsid-specific restriction factor that prevents
infection from non-host-adapted retroviruses. Blocks viral
replication early in the life cycle, after viral entry but before
reverse transcription. In addition to acting as a capsid-specific
restriction factor, also acts as a pattern recognition receptor
that activates innate immune signaling in response to the
retroviral capsid lattice. Binding to the viral capsid triggers
its E3 ubiquitin ligase activity, and in concert with the
heterodimeric ubiquitin conjugating enzyme complex UBE2V1-UBE2N
(also known as UBC13-UEV1A complex) generates 'Lys-63'-linked
polyubiquitin chains, which in turn are catalysts in the
autophosphorylation of the MAP3K7/TAK1 complex (includes TAK1,
TAB2, and TAB3). Activation of the MAP3K7/TAK1 complex by
autophosphorylation results in the induction and expression of NF-
kappa-B and MAPK-responsive inflammatory genes, thereby leading to
an innate immune response in the infected cell. Plays a role in
regulating autophagy through activation of autophagy regulator
BECN1 by causing its dissociation from its inhibitors BCL2 and
TAB2. {ECO:0000250|UniProtKB:Q9C035}.
-!- CATALYTIC ACTIVITY:
Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-
cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-
conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor
protein]-L-lysine.; EC=2.3.2.27;
-!- PATHWAY: Protein modification; protein ubiquitination.
-!- SUBUNIT: Can form homodimers and homotrimers. In addition to
lower-order dimerization, also exhibits a higher-order
multimerization and both low- and high-order multimerizations are
essential for its restriction activity. Interacts with BTBD1 and
BTBD2. Interacts with PSMC4, PSMC5, PSMD7 and HSPA8/HSC70.
Interacts (via B30.2/SPRY domain) with HSPA1A/B. Interacts with
PSMC2, MAP3K7/TAK1, TAB2 and TAB3. Interacts with SQSTM1.
Interacts with TRIM6 and TRIM34. Interacts with ULK1
(phosphorylated form), GABARAP, GABARAPL1, GABARAPL2, MAP1LC3A,
MAP1LC3C and BECN1. {ECO:0000250|UniProtKB:Q0PF16,
ECO:0000250|UniProtKB:Q9C035}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q0PF16}.
Nucleus {ECO:0000250|UniProtKB:Q0PF16}. Note=Predominantly
localizes in cytoplasmic bodies. Localization may be influenced by
the coexpression of other TRIM proteins, hence partial nuclear
localization is observed in the presence of TRIM22 or TRIM27. In
cytoplasmic bodies, colocalizes with proteasomal subunits and
SQSTM1. {ECO:0000250|UniProtKB:Q0PF16}.
-!- DOMAIN: The B box-type zinc finger domain and the coiled-coil
domain contribute to the higher and low order multimerization
respectively which is essential for restriction activity. The
coiled coil domain is important for higher order multimerization
by promoting the initial dimerization.
{ECO:0000250|UniProtKB:Q0PF16, ECO:0000250|UniProtKB:Q9C035}.
-!- DOMAIN: The B30.2/SPRY domain acts as a capsid recognition domain.
Polymorphisms in this domain explain the observed species-specific
differences among orthologs (By similarity). {ECO:0000250}.
-!- DOMAIN: The RING-type zinc finger domain confers E3 ubiquitin
ligase activity and is essential for retrovirus restriction
activity, autoubiquitination and higher-order multimerization.
{ECO:0000250}.
-!- PTM: Degraded in a proteasome-independent fashion in the absence
of viral infection but in a proteasome-dependent fashion following
exposure to restriction sensitive virus. {ECO:0000250}.
-!- PTM: Autoubiquitinated in a RING finger- and UBE2D2-dependent
manner. Monoubiquitinated by TRIM21. Deubiquitinated by Yersinia
YopJ. Ubiquitination may not lead to proteasomal degradation (By
similarity). {ECO:0000250}.
-!- SIMILARITY: Belongs to the TRIM/RBCC family. {ECO:0000305}.
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EMBL; AY740616; AAW72444.1; -; mRNA.
EMBL; AY843516; AAV91987.1; -; Genomic_DNA.
ProteinModelPortal; Q5D7I1; -.
SMR; Q5D7I1; -.
PRIDE; Q5D7I1; -.
HOVERGEN; HBG001357; -.
UniPathway; UPA00143; -.
GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
GO; GO:0000932; C:P-body; ISS:UniProtKB.
GO; GO:0008329; F:signaling pattern recognition receptor activity; ISS:UniProtKB.
GO; GO:0004842; F:ubiquitin-protein transferase activity; ISS:UniProtKB.
GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
GO; GO:0002218; P:activation of innate immune response; ISS:UniProtKB.
GO; GO:0006914; P:autophagy; IEA:UniProtKB-KW.
GO; GO:0051607; P:defense response to virus; IEA:UniProtKB-KW.
GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
GO; GO:0043123; P:positive regulation of I-kappaB kinase/NF-kappaB signaling; ISS:UniProtKB.
GO; GO:0043410; P:positive regulation of MAPK cascade; ISS:UniProtKB.
GO; GO:0051092; P:positive regulation of NF-kappaB transcription factor activity; ISS:UniProtKB.
GO; GO:0070534; P:protein K63-linked ubiquitination; ISS:UniProtKB.
GO; GO:0031664; P:regulation of lipopolysaccharide-mediated signaling pathway; ISS:UniProtKB.
CDD; cd00021; BBOX; 1.
Gene3D; 3.30.40.10; -; 1.
InterPro; IPR001870; B30.2/SPRY.
InterPro; IPR003879; Butyrophylin_SPRY.
InterPro; IPR013320; ConA-like_dom_sf.
InterPro; IPR003877; SPRY_dom.
InterPro; IPR032917; TRIM5.
InterPro; IPR000315; Znf_B-box.
InterPro; IPR001841; Znf_RING.
InterPro; IPR013083; Znf_RING/FYVE/PHD.
InterPro; IPR017907; Znf_RING_CS.
PANTHER; PTHR24103:SF426; PTHR24103:SF426; 2.
Pfam; PF00622; SPRY; 1.
Pfam; PF00643; zf-B_box; 1.
PRINTS; PR01407; BUTYPHLNCDUF.
SMART; SM00336; BBOX; 1.
SMART; SM00184; RING; 1.
SMART; SM00449; SPRY; 1.
SUPFAM; SSF49899; SSF49899; 2.
PROSITE; PS50188; B302_SPRY; 1.
PROSITE; PS50119; ZF_BBOX; 1.
PROSITE; PS00518; ZF_RING_1; 1.
PROSITE; PS50089; ZF_RING_2; 1.
2: Evidence at transcript level;
Acetylation; Antiviral defense; Autophagy; Coiled coil; Cytoplasm;
Immunity; Innate immunity; Metal-binding; Nucleus; Phosphoprotein;
Transferase; Ubl conjugation; Ubl conjugation pathway; Zinc;
Zinc-finger.
INIT_MET 1 1 Removed. {ECO:0000250|UniProtKB:Q9C035}.
CHAIN 2 547 Tripartite motif-containing protein 5.
/FTId=PRO_0000273449.
DOMAIN 280 547 B30.2/SPRY. {ECO:0000255|PROSITE-
ProRule:PRU00548}.
ZN_FING 15 59 RING-type. {ECO:0000255|PROSITE-
ProRule:PRU00175}.
ZN_FING 91 132 B box-type. {ECO:0000255|PROSITE-
ProRule:PRU00024}.
REGION 186 199 Required for interaction with GABARAP and
for autophagy.
{ECO:0000250|UniProtKB:Q0PF16}.
COILED 132 225 {ECO:0000255}.
MOD_RES 2 2 N-acetylalanine.
{ECO:0000250|UniProtKB:Q9C035}.
MOD_RES 86 86 Phosphoserine.
{ECO:0000250|UniProtKB:Q9C035}.
CONFLICT 4 4 E -> G (in Ref. 1; AAW72444).
{ECO:0000305}.
CONFLICT 88 88 E -> K (in Ref. 1; AAW72444).
{ECO:0000305}.
CONFLICT 162 162 A -> V (in Ref. 1; AAW72444).
{ECO:0000305}.
CONFLICT 291 291 E -> G (in Ref. 1; AAW72444).
{ECO:0000305}.
CONFLICT 359 359 D -> N (in Ref. 1; AAW72444).
{ECO:0000305}.
CONFLICT 486 486 T -> A (in Ref. 1; AAW72444).
{ECO:0000305}.
SEQUENCE 547 AA; 62555 MW; 42FD567F17C373AC CRC64;
MASEILLNIK EEVTCPICLE LLTEPLSLDC GHSFCQACIT ANHKESTLHQ GERSCPLCRV
SYQSENLRPN RHLANIAERL REVMLSPEEG QKVDRCARHG EKLLLFCQQH GNVICWLCER
SQEHRGHSTF LVEEVAQKYQ EKLQVALEMM RQKQQDAEKL EADVREEQAS WKIQIENDKT
NILAEFKQLR DILDCEESNE LQNLEKEEEN LLKTLAQSEN DMVLQTQSMR VLIADLEHRL
QGSVMELLQD VEGVIKRIKN VTLQKPKTFL NEKRRVFRAP DLKGMLQVFK ELKEVQCYWA
HVTLVPSHPS CTVISEDERQ VRYQEQIHQP SVKVKYFCGV LGSPGFTSGK HYWEVDVSDK
SAWILGVCVS LKCTANVPGI ENYQPKNGYW VIGLQNANNY SAFQDAVPGT ENYQPKNGNR
RNKGLRNADN YSAFRDTFQP INDSWVTGLR NVDNYNAFQD AVKYSDFQDG SCSTPSAPLM
VPLFMTICPK RVGVFLDCKA CTVSFFNVTS NGCLIYKFSK CHFSYPVFPY FSPMICKLPM
TLCSPSS


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25-217 This protein is a member of the tripartite motif (TRIM) family. The TRIM motif includes three zinc-binding domains, a RING, a B-box type 1 and a B-box type 2, and a coiled-coil region. This protein lo 0.05 mg
28-782 TRIM23 is a member of the tripartite motif (TRIM) family. The TRIM motif includes three zinc-binding domains, a RING, a B-box type 1 and a B-box type 2, and a coiled-coil region. This protein is also 0.1 mg
31-262 TRIM23 is a member of the tripartite motif (TRIM) family. The TRIM motif includes three zinc-binding domains, a RING, a B-box type 1 and a B-box type 2, and a coiled-coil region. This protein is also 0.05 mg
25-041 TRIM23 is a member of the tripartite motif (TRIM) family. The TRIM motif includes three zinc-binding domains, a RING, a B-box type 1 and a B-box type 2, and a coiled-coil region. This protein is also 0.05 mg
28-122 TRIM17 is a member of the tripartite motif (TRIM) family. The TRIM motif includes three zinc-binding domains, a RING, a B-box type 1 and a B-box type 2, and a coiled-coil region. The protein localizes 0.1 mg
25-192 TRIM9 is a member of the tripartite motif (TRIM) family. The TRIM motif includes three zinc-binding domains, a RING, a B-box type 1 and a B-box type 2, and a coiled-coil region. The protein localizes 0.05 mg
28-088 TRIM10 is a member of the tripartite motif (TRIM) family. The TRIM motif includes three zinc-binding domains, a RING, a B-box type 1 and a B-box type 2, and a coiled-coil region. This protein localize 0.1 mg
28-021 TRIM26 is a member of the tripartite motif (TRIM) family. The TRIM motif includes three zinc-binding domains, a RING, a B-box type 1 and a B-box type 2, and a coiled-coil region. The protein localizes 0.1 mg
28-015 The protein encoded by RFP2 is a member of the tripartite motif (TRIM) family. The TRIM motif includes three zinc-binding domains, a RING, a B-box type 1 and a B-box type 2, and a coiled-coil region. 0.1 mg
28-014 The protein encoded by the RFP2 gene is a member of the tripartite motif (TRIM) family. The TRIM motif includes three zinc-binding domains, a RING, a B-box type 1 and a B-box type 2, and a coiled-coil 0.05 mg
27-116 TRIM31 encodes for a member of the tripartite motif (TRIM) family. The TRIM motif includes three zinc-binding domains, a RING, a B-box type 1 and a B-box type 2, and a coiled-coil region. The protein 0.05 mg
27-139 TRIM15 is a member of the tripartite motif (TRIM) family. The TRIM motif includes three zinc-binding domains, a RING, a B-box type 1 and a B-box type 2, and a coiled-coil region. The protein localizes 0.05 mg
31-274 TRIM27 is a member of the tripartite motif (TRIM) family. The TRIM motif includes three zinc-binding domains, a RING, a B-box type 1 and a B-box type 2, and a coiled-coil region. This protein localize 0.05 mg
25-219 TRIM6 is a member of the tripartite motif (TRIM) family. The TRIM motif includes three zinc-binding domains, a RING, a B-box type 1 and a B-box type 2, and a coiled-coil region. The protein localizes 0.05 mg
28-155 TRIM15 is a member of the tripartite motif (TRIM) family. The TRIM motif includes three zinc-binding domains, a RING, a B-box type 1 and a B-box type 2, and a coiled-coil region. The protein localizes 0.1 mg
28-207 TRIM9 is a member of the tripartite motif (TRIM) family. The TRIM motif includes three zinc-binding domains, a RING, a B-box type 1 and a B-box type 2, and a coiled-coil region. The protein localizes 0.1 mg
25-224 TRIM9 is a member of the tripartite motif (TRIM) family. The TRIM motif includes three zinc-binding domains, a RING, a B-box type 1 and a B-box type 2, and a coiled-coil region. The protein localizes 0.05 mg
28-179 The protein encoded byTRIM14 is a member of the tripartite motif (TRIM) family. The TRIM motif includes three zinc-binding domains, a RING, a B-box type 1 and a B-box type 2, and a coiled-coil region. 0.05 mg
28-172 TRIM31 encodes for a member of the tripartite motif (TRIM) family. The TRIM motif includes three zinc-binding domains, a RING, a B-box type 1 and a B-box type 2, and a coiled-coil region. The protein 0.05 mg
28-180 The protein encoded byTRIM14 is a member of the tripartite motif (TRIM) family. The TRIM motif includes three zinc-binding domains, a RING, a B-box type 1 and a B-box type 2, and a coiled-coil region. 0.1 mg


 

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