ID A0A3B5Q9M7_XIPMA Unreviewed; 402 AA.
AC A0A3B5Q9M7;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 24-JAN-2024, entry version 23.
DE RecName: Full=RING-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012483};
DE EC=2.3.2.27 {ECO:0000256|ARBA:ARBA00012483};
OS Xiphophorus maculatus (Southern platyfish) (Platypoecilus maculatus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Cyprinodontiformes; Poeciliidae; Poeciliinae;
OC Xiphophorus.
OX NCBI_TaxID=8083 {ECO:0000313|Ensembl:ENSXMAP00000026816.1, ECO:0000313|Proteomes:UP000002852};
RN [1] {ECO:0000313|Proteomes:UP000002852}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JP 163 A {ECO:0000313|Proteomes:UP000002852};
RA Walter R., Schartl M., Warren W.;
RL Submitted (JAN-2012) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000002852}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JP 163 A {ECO:0000313|Proteomes:UP000002852};
RX PubMed=23542700; DOI=10.1038/ng.2604;
RA Schartl M., Walter R.B., Shen Y., Garcia T., Catchen J., Amores A.,
RA Braasch I., Chalopin D., Volff J.N., Lesch K.P., Bisazza A., Minx P.,
RA Hillier L., Wilson R.K., Fuerstenberg S., Boore J., Searle S.,
RA Postlethwait J.H., Warren W.C.;
RT "The genome of the platyfish, Xiphophorus maculatus, provides insights into
RT evolutionary adaptation and several complex traits.";
RL Nat. Genet. 45:567-572(2013).
RN [3] {ECO:0000313|Ensembl:ENSXMAP00000026816.1}
RP IDENTIFICATION.
RC STRAIN=JP 163 A {ECO:0000313|Ensembl:ENSXMAP00000026816.1};
RG Ensembl;
RL Submitted (JUL-2023) to UniProtKB.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine +
CC [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-
CC cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.;
CC EC=2.3.2.27; Evidence={ECO:0000256|ARBA:ARBA00000900};
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000256|ARBA:ARBA00004906}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004202};
CC Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004202}. Cytoplasm,
CC cytosol {ECO:0000256|ARBA:ARBA00004514}.
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DR AlphaFoldDB; A0A3B5Q9M7; -.
DR STRING; 8083.ENSXMAP00000026816; -.
DR Ensembl; ENSXMAT00000034007.1; ENSXMAP00000026816.1; ENSXMAG00000014052.2.
DR GeneTree; ENSGT00390000012719; -.
DR InParanoid; A0A3B5Q9M7; -.
DR OMA; ACEACNV; -.
DR OrthoDB; 383715at2759; -.
DR Proteomes; UP000002852; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR CDD; cd16706; RING-HC_CARP1; 1.
DR Gene3D; 1.10.720.140; -; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR049320; CARP1_2_FYVE.
DR InterPro; IPR036361; SAP_dom_sf.
DR InterPro; IPR011011; Znf_FYVE_PHD.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR14879; CASPASE REGULATOR, RING FINGER DOMAIN-CONTAINING; 1.
DR PANTHER; PTHR14879:SF17; RING FINGER PROTEIN 34B; 1.
DR Pfam; PF21272; FYVE_CARP1-2; 1.
DR Pfam; PF13920; zf-C3HC4_3; 1.
DR SMART; SM00184; RING; 1.
DR SUPFAM; SSF57903; FYVE/PHD zinc finger; 1.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR SUPFAM; SSF68906; SAP domain; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 4: Predicted;
KW Apoptosis {ECO:0000256|ARBA:ARBA00022703};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000002852};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00175}.
FT DOMAIN 355..390
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT REGION 154..249
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 161..184
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 191..238
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 402 AA; 44114 MW; 3DE1890D78B1ED43 CRC64;
MKAGASSMWA SCCGLLNEVM GTGTVRTPQP GFGAGAGPFR FAPSAGYSTY PPTSSGSAGQ
LCKACGLAFS VFRRKHICCD CKKSFCALCS VLQENLRCCT TCHLLRGTAF QRPRLMQLRV
KDLRQYLLLR NIPTDTCREK EDLVDLVLCH QGTRETPRPV MEEDEEEDED DDTCGDEEED
GGEDTDSLHS LPHSRAASPP SATRSASELS VLSASQGDAL SPSDSSGTPS QEHEDTPTAS
LLNLEPAENI LEVSPATQRR IRASLSDLDN EEAIENLSVR QLKEILARNF VNYSGCCEKW
ELLDRVHRLY RENEQNRKSM ENVSITAVVA YPQPLCNSGV GDGVRAQLAA DENLCRICMD
AIIDCVLLEC GHMVTCTKCG KRMSECPICR QYVVRAVHVF KS
//