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Database: UniProt
Entry: K9J6H5_PIG
LinkDB: K9J6H5_PIG
Original site: K9J6H5_PIG 
ID   K9J6H5_PIG              Unreviewed;       465 AA.
AC   K9J6H5;
DT   06-FEB-2013, integrated into UniProtKB/TrEMBL.
DT   06-FEB-2013, sequence version 1.
DT   27-MAR-2024, entry version 61.
DE   SubName: Full=E3 ubiquitin-protein ligase TRIM38 isoform X1 {ECO:0000313|EMBL:HCZ78941.1};
DE   SubName: Full=Tripartite motif containing 38 {ECO:0000313|EMBL:JAA53559.1, ECO:0000313|Ensembl:ENSSSCP00000059249.1};
GN   Name=TRIM38 {ECO:0000313|EMBL:JAA53559.1,
GN   ECO:0000313|Ensembl:ENSSSCP00000059249.1,
GN   ECO:0000313|VGNC:VGNC:94411};
OS   Sus scrofa (Pig).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX   NCBI_TaxID=9823 {ECO:0000313|EMBL:JAA53559.1};
RN   [1] {ECO:0000313|Ensembl:ENSSSCP00000059249.1, ECO:0000313|Proteomes:UP000008227}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Duroc {ECO:0000313|Ensembl:ENSSSCP00000059249.1,
RC   ECO:0000313|Proteomes:UP000008227};
RG   Porcine genome sequencing project;
RL   Submitted (NOV-2009) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:JAA53559.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Dawson H.D., Chen C.T.;
RT   "Global Gene Expression Profiling of Alveolar Macrophages by Deep
RT   Sequencing.";
RL   Submitted (FEB-2013) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|EMBL:HCZ78941.1}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=30723633; DOI=.7717/peerj.6374;
RA   Gilbert D.G.;
RT   "Genes of the pig, Sus scrofa, reconstructed with EvidentialGene.";
RL   PeerJ 7:E6374-E6374(2019).
RN   [4] {ECO:0000313|Ensembl:ENSSSCP00000059249.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
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DR   EMBL; DQIR01023466; HCZ78941.1; -; Transcribed_RNA.
DR   EMBL; DQIR01167015; HDB22492.1; -; Transcribed_RNA.
DR   EMBL; GACC01000248; JAA53559.1; -; mRNA.
DR   STRING; 9823.ENSSSCP00000059249; -.
DR   Ensembl; ENSSSCT00000060157.2; ENSSSCP00000059249.1; ENSSSCG00000035153.3.
DR   VGNC; VGNC:94411; TRIM38.
DR   GeneTree; ENSGT00940000160468; -.
DR   OMA; FRVYQHS; -.
DR   OrthoDB; 3453019at2759; -.
DR   Proteomes; UP000008227; Chromosome 7.
DR   Bgee; ENSSSCG00000035153; Expressed in blood and 43 other cell types or tissues.
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:0042803; F:protein homodimerization activity; IBA:GO_Central.
DR   GO; GO:0019901; F:protein kinase binding; IBA:GO_Central.
DR   GO; GO:0003713; F:transcription coactivator activity; IEA:Ensembl.
DR   GO; GO:0061630; F:ubiquitin protein ligase activity; IBA:GO_Central.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
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 canonical NF-kappaB signal transduction; IBA:GO_Central.
DR   GO; GO:0046598; P:positive regulation of viral entry into host cell; IEA:Ensembl.
DR   GO; GO:0000209; P:protein polyubiquitination; IBA:GO_Central.
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   CDD; cd19761; Bbox2_TRIM5-like; 1.
DR   CDD; cd16600; RING-HC_TRIM38_C-IV; 1.
DR   CDD; cd15815; SPRY_PRY_TRIM38; 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; IPR006574; PRY.
DR   InterPro; IPR035790; SPRY/PRY_TRIM38.
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:SF47; E3 UBIQUITIN-PROTEIN LIGASE TRIM38; 1.
DR   Pfam; PF13765; PRY; 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; SM00589; PRY; 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:UP000008227};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW   ProRule:PRU00024}.
FT   DOMAIN          16..63
FT                   /note="RING-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50089"
FT   DOMAIN          88..129
FT                   /note="B box-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50119"
FT   DOMAIN          274..465
FT                   /note="B30.2/SPRY"
FT                   /evidence="ECO:0000259|PROSITE:PS50188"
FT   COILED          133..160
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          202..236
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   465 AA;  53567 MW;  32A14B507F8F3E16 CRC64;
     MASTTTTRKM REEATCSICL HLMSKPVSIS CGHSYCHSCI VNFFENLCRM QPWLETFSCP
     QCRVPFKMSS LRPNVQLGGL IEAIKEMDQE MSCEEHGEKL HLFCENEGKL ICWRCDRGPQ
     HRGHATTLVE DACQGYKEEL QKAVTQLKQL EEECMKLKMF TAKQITEWNE KIEIQKQKIQ
     SDFKNLQRFL HEEEKSYLWK LEKEKEQTLR RLRDNKVHLE QQSHELQSHI LELENKCQGS
     AQNLLQDVKD TLSRSWAVKL DKPEPLSLDL HTVCNVSERY FDVKKILRSH QVSVTLDPDT
     AHYELVLSED RRQVTRGSPQ ENLESSSRRF SALPCILGCE GFTSGKHYFE VDVGEGTGWD
     LGVCMENVQR DTGLVQTPQS GFWAIRLCKK KGYVALTSPL TSLQLREQPL VVGIFLDCEA
     GVVSFYNMTT GSHIFTFPKA SFSDTLRPYF QVYQYSPLFL PPPDE
//
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