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Database: UniProt
Entry: F6UD69_CALJA
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ID   F6UD69_CALJA            Unreviewed;       474 AA.
AC   F6UD69;
DT   27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT   27-JUL-2011, sequence version 1.
DT   27-MAR-2024, entry version 73.
DE   RecName: Full=TRIM5alpha {ECO:0000256|ARBA:ARBA00032496};
GN   Name=TRIM4 {ECO:0000313|EMBL:JAB04237.1,
GN   ECO:0000313|Ensembl:ENSCJAP00000028904.2};
OS   Callithrix jacchus (White-tufted-ear marmoset).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Platyrrhini; Cebidae;
OC   Callitrichinae; Callithrix; Callithrix.
OX   NCBI_TaxID=9483 {ECO:0000313|Ensembl:ENSCJAP00000028904.2, ECO:0000313|Proteomes:UP000008225};
RN   [1] {ECO:0000313|Ensembl:ENSCJAP00000028904.2}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Warren W., Ye L., Minx P., Worley K., Gibbs R., Wilson R.K.;
RL   Submitted (MAR-2009) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:JAB04237.1}
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Bladder {ECO:0000313|EMBL:JAB04237.1}, Cerebellum
RC   {ECO:0000313|EMBL:JAB49810.1}, Cerebral cortex
RC   {ECO:0000313|EMBL:JAB23932.1}, Hippocampus
RC   {ECO:0000313|EMBL:JAB16468.1}, and Skeletal muscle
RC   {ECO:0000313|EMBL:JAB35575.1};
RX   PubMed=25243066; DOI=10.1186/2047-217X-3-14;
RA   Maudhoo M.D., Ren D., Gradnigo J.S., Gibbs R.M., Lubker A.C.,
RA   Moriyama E.N., French J.A., Norgren R.B.Jr.;
RT   "De novo assembly of the common marmoset transcriptome from NextGen mRNA
RT   sequences.";
RL   Gigascience 3:14-14(2014).
RN   [3] {ECO:0000313|Ensembl:ENSCJAP00000028904.2}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (NOV-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   EMBL; GAMT01007624; JAB04237.1; -; mRNA.
DR   EMBL; GAMS01006668; JAB16468.1; -; mRNA.
DR   EMBL; GAMR01010000; JAB23932.1; -; mRNA.
DR   EMBL; GAMQ01006276; JAB35575.1; -; mRNA.
DR   EMBL; GAMP01002945; JAB49810.1; -; mRNA.
DR   RefSeq; XP_008981078.1; XM_008982830.2.
DR   Ensembl; ENSCJAT00000030545.5; ENSCJAP00000028904.2; ENSCJAG00000015702.5.
DR   GeneID; 100389001; -.
DR   KEGG; cjc:100389001; -.
DR   CTD; 89122; -.
DR   GeneTree; ENSGT00940000163330; -.
DR   HOGENOM; CLU_013137_0_3_1; -.
DR   OrthoDB; 3453019at2759; -.
DR   UniPathway; UPA00143; -.
DR   Proteomes; UP000008225; Chromosome 2.
DR   Bgee; ENSCJAG00000015702; Expressed in testis and 6 other cell types or tissues.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
DR   CDD; cd19760; Bbox2_TRIM4-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   2: Evidence at transcript level;
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008225};
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          262..474
FT                   /note="B30.2/SPRY"
FT                   /evidence="ECO:0000259|PROSITE:PS50188"
FT   COILED          192..223
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   474 AA;  53901 MW;  244AC91C82004A52 CRC64;
     MEVKDLQEEL TCSICLDYFR DPVSIECGHN FCRSCLHRSR VPGSGPFPCP ECRHPSAPTA
     LRPNWALARL TEKTQRRRQG PVPPGLCGRH WEPLRLFCED DQRPVCLVCR ESQEHQTHAM
     APIDEAVESY REKLLQSQCN LGDKMKTLLE LQEIEAKIAT RWKDKIKSQR MRISTEFSKL
     HNFLVEEEDL FIQRLSKEEE ETKTKLNENR LKLNQTISSL KKLIVEVGEK RQAPTLELLQ
     NPKDVLTRSE IQDVNYSLEA PKVKTVCQIP LMKEMLKRFQ VAVNLAEDTA HPKLVFSQEG
     RYVKNVASAS SWPAFSAAWN FVAGWRNPQK TAHVEKFQHL PCVLGKNVFT SGKHYWEIER
     RDGLDVAVGV CREDVMGITD HSKMSPDVGI WAIYWSVAGC WPLTGFPGSP IQPEPTAHRV
     GVYLDRGTGN VSFYSAVDGV HLHTFSCSSV SRLRPFFWLS PLASLVIPPV TDGK
//
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