GenomeNet

Database: UniProt
Entry: A0A3P9NKK8_POERE
LinkDB: A0A3P9NKK8_POERE
Original site: A0A3P9NKK8_POERE 
ID   A0A3P9NKK8_POERE        Unreviewed;       378 AA.
AC   A0A3P9NKK8;
DT   13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT   13-FEB-2019, sequence version 1.
DT   27-MAR-2024, entry version 26.
DE   SubName: Full=Ring finger protein 13 {ECO:0000313|Ensembl:ENSPREP00000010115.1};
OS   Poecilia reticulata (Guppy) (Acanthophacelus reticulatus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Ovalentaria; Atherinomorphae; Cyprinodontiformes; Poeciliidae; Poeciliinae;
OC   Poecilia.
OX   NCBI_TaxID=8081 {ECO:0000313|Ensembl:ENSPREP00000010115.1, ECO:0000313|Proteomes:UP000242638};
RN   [1] {ECO:0000313|Proteomes:UP000242638}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Guanapo {ECO:0000313|Proteomes:UP000242638};
RA   Kuenstner A., Dreyer C.;
RT   "The genomic landscape of the Guanapo guppy.";
RL   Submitted (NOV-2013) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSPREP00000010115.1}
RP   IDENTIFICATION.
RC   STRAIN=Guanapo {ECO:0000313|Ensembl:ENSPREP00000010115.1};
RG   Ensembl;
RL   Submitted (SEP-2023) to UniProtKB.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004479}; Single-
CC       pass type I membrane protein {ECO:0000256|ARBA:ARBA00004479}.
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DR   RefSeq; XP_008405055.1; XM_008406833.2.
DR   RefSeq; XP_008405056.1; XM_008406834.2.
DR   AlphaFoldDB; A0A3P9NKK8; -.
DR   STRING; 8081.ENSPREP00000010115; -.
DR   Ensembl; ENSPRET00000010231.1; ENSPREP00000010115.1; ENSPREG00000006887.1.
DR   GeneID; 103463470; -.
DR   KEGG; pret:103463470; -.
DR   CTD; 11342; -.
DR   GeneTree; ENSGT00940000154942; -.
DR   OMA; GHIVLIP; -.
DR   OrthoDB; 5474929at2759; -.
DR   Proteomes; UP000242638; Unassembled WGS sequence.
DR   Bgee; ENSPREG00000006887; Expressed in head and 1 other cell type or tissue.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProt.
DR   GO; GO:0012505; C:endomembrane system; IEA:UniProt.
DR   GO; GO:0043229; C:intracellular organelle; IEA:UniProt.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0043227; C:membrane-bounded organelle; IEA:UniProt.
DR   GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   CDD; cd02123; PA_C_RZF_like; 1.
DR   CDD; cd16796; RING-H2_RNF13; 1.
DR   Gene3D; 3.50.30.30; -; 1.
DR   Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR   InterPro; IPR046450; PA_dom_sf.
DR   InterPro; IPR003137; PA_domain.
DR   InterPro; IPR001841; Znf_RING.
DR   InterPro; IPR011016; Znf_RING-CH.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   InterPro; IPR044744; ZNRF4/RNF13/RNF167_PA.
DR   PANTHER; PTHR47168:SF6; PROTEASE-ASSOCIATED (PA) RING_U-BOX ZINC FINGER FAMILY PROTEIN; 1.
DR   PANTHER; PTHR47168; RING ZINC FINGER DOMAIN SUPERFAMILY PROTEIN-RELATED; 1.
DR   Pfam; PF02225; PA; 1.
DR   Pfam; PF13639; zf-RING_2; 1.
DR   SMART; SM00184; RING; 1.
DR   SMART; SM00744; RINGv; 1.
DR   SUPFAM; SSF52025; PA domain; 1.
DR   SUPFAM; SSF57850; RING/U-box; 1.
DR   PROSITE; PS50089; ZF_RING_2; 1.
PE   4: Predicted;
KW   Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000242638};
KW   Signal {ECO:0000256|ARBA:ARBA00022729};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}; Zinc {ECO:0000256|ARBA:ARBA00022833};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW   ProRule:PRU00175}.
FT   TRANSMEM        181..206
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          239..281
FT                   /note="RING-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50089"
FT   REGION          284..378
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        305..335
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        338..353
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   378 AA;  42228 MW;  BCD54CA05757CEB8 CRC64;
     MLLSLGMLML SATQVYTIFT VQLFAFLNLL PVEADIAAYS FDNKTETFDD MPARFGYRLP
     SDGLKGFLIG ARPENACEPI EPPPRENMTG AFIVLIKRYD CNFDMKVLNA QKAGYKAAIV
     HNVDSDDLIS MGSNDLDVLK QIVIPSVFVS ELTANALKDD YMYDKGGHLV LIPDFSLPLE
     YYLIPFLIIV GICLILIVVF MITKFVQDRR RARRSRLRKD QLKKLPIHKF KKGDNYDVCA
     ICLDEYEDGD KLRVLPCSHA YHSKCVDPWL TKTKKTCPVC KQKVVPSQGD SDSDSEEGDS
     GPDENEVSES TPLLRSQAST SAHSFGTMSG ASRSEQDSSE YDDDDELGSS DSEEEVTVET
     VVVQMQQPCS DEHDLPRA
//
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