ID A0A2K6UID1_SAIBB Unreviewed; 500 AA.
AC A0A2K6UID1;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE RecName: Full=TRIM5alpha {ECO:0000256|ARBA:ARBA00032496};
GN Name=TRIM4 {ECO:0000313|Ensembl:ENSSBOP00000031637.1};
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 {ECO:0000313|Ensembl:ENSSBOP00000031637.1, ECO:0000313|Proteomes:UP000233220};
RN [1] {ECO:0000313|Ensembl:ENSSBOP00000031637.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
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:0000256|ARBA:ARBA00011109}.
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DR AlphaFoldDB; A0A2K6UID1; -.
DR STRING; 39432.ENSSBOP00000031637; -.
DR Ensembl; ENSSBOT00000048530.1; ENSSBOP00000031637.1; ENSSBOG00000032029.1.
DR GeneTree; ENSGT00940000163330; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000233220; Unplaced.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0005886; C:plasma membrane; IEA:Ensembl.
DR GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
DR CDD; cd19762; Bbox2_TRIM7-like; 1.
DR CDD; cd15809; SPRY_PRY_TRIM4; 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; IPR035829; PRY/SPRY_TRIM4.
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 PANTHER; PTHR24103; E3 UBIQUITIN-PROTEIN LIGASE TRIM; 1.
DR PANTHER; PTHR24103:SF670; E3 UBIQUITIN-PROTEIN LIGASE TRIM4; 1.
DR Pfam; PF00622; SPRY; 1.
DR Pfam; PF00643; zf-B_box; 1.
DR Pfam; PF15227; zf-C3HC4_4; 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 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000233220};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00024}.
FT DOMAIN 12..53
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT DOMAIN 82..123
FT /note="B box-type"
FT /evidence="ECO:0000259|PROSITE:PS50119"
FT DOMAIN 288..500
FT /note="B30.2/SPRY"
FT /evidence="ECO:0000259|PROSITE:PS50188"
FT COILED 218..249
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 500 AA; 57176 MW; EE075739A36F30A4 CRC64;
MEIKDLQEEL TCSICLDYFR DPVSIECGHN FCRSCLHRSC VPGGGPFPCP ECRHPSAPAA
LRPNWALARL TERTQRRLQG PVPPGLCGRH WEPLRLFCED DQLPVCLVCR ESQQHQTHVM
TPIDEAVESY RKGNLDIHMD EWKRRPVRLL WYHSNQEEKL LQSQRDLGAK MKRVLQLQDA
EAKNATQWKD KIKSQRMRIS AEFSKLHNFL VEEEDLFLQR LSKEEEETKT KLNENRIKLN
QTIASLKKLI LEVGEKRQAS SLEMLQNPKD VLTRSEIQDV NYSLEAPKMK TVCQIPLMKE
MLKRFQVAVN LAEDTAHPKL VFSQEGRYVK NVASASSWPV FSTAWNFVAG WRNPQKTAHV
EKFQHLPCVL GKNVFTSGKH YWEIERRDSL EVAVGVCRED VMGITDRSKM SPDVGIWAIY
WSAAGCWPLT GFPGSPTQQE PAVHRVGVYL DRGTGNVSFY SAVDGVHLHT FSCSSVSRLR
PFFWLSPLAS LVIPPVTDGK
//
