GenomeNet

Database: UniProt
Entry: A0A2I0M6B5_COLLI
LinkDB: A0A2I0M6B5_COLLI
Original site: A0A2I0M6B5_COLLI 
ID   A0A2I0M6B5_COLLI        Unreviewed;       257 AA.
AC   A0A2I0M6B5;
DT   28-FEB-2018, integrated into UniProtKB/TrEMBL.
DT   28-FEB-2018, sequence version 1.
DT   24-JAN-2024, entry version 19.
DE   RecName: Full=E3 ubiquitin-protein ligase RNF170 {ECO:0000256|ARBA:ARBA00014068};
DE            EC=2.3.2.27 {ECO:0000256|ARBA:ARBA00012483};
DE   AltName: Full=RING finger protein 170 {ECO:0000256|ARBA:ARBA00031107};
DE   AltName: Full=RING-type E3 ubiquitin transferase RNF170 {ECO:0000256|ARBA:ARBA00030110};
GN   Name=RNF170 {ECO:0000313|EMBL:PKK25217.1};
GN   ORFNames=A306_00009572 {ECO:0000313|EMBL:PKK25217.1};
OS   Columba livia (Rock dove).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Columbiformes; Columbidae; Columba.
OX   NCBI_TaxID=8932 {ECO:0000313|EMBL:PKK25217.1, ECO:0000313|Proteomes:UP000053872};
RN   [1] {ECO:0000313|EMBL:PKK25217.1, ECO:0000313|Proteomes:UP000053872}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   TISSUE=Blood {ECO:0000313|EMBL:PKK25217.1};
RX   PubMed=23371554; DOI=10.1126/science.1230422;
RA   Shapiro M.D., Kronenberg Z., Li C., Domyan E.T., Pan H., Campbell M.,
RA   Tan H., Huff C.D., Hu H., Vickrey A.I., Nielsen S.C., Stringham S.A.,
RA   Hu H., Willerslev E., Gilbert M.T., Yandell M., Zhang G., Wang J.;
RT   "Genomic diversity and evolution of the head crest in the rock pigeon.";
RL   Science 339:1063-1067(2013).
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: Endoplasmic reticulum membrane
CC       {ECO:0000256|ARBA:ARBA00004477}; Multi-pass membrane protein
CC       {ECO:0000256|ARBA:ARBA00004477}. Membrane
CC       {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC       {ECO:0000256|ARBA:ARBA00004141}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:PKK25217.1}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AKCR02000034; PKK25217.1; -; Genomic_DNA.
DR   RefSeq; XP_005514222.1; XM_005514165.1.
DR   AlphaFoldDB; A0A2I0M6B5; -.
DR   STRING; 8932.A0A2I0M6B5; -.
DR   GeneID; 102090746; -.
DR   KEGG; clv:102090746; -.
DR   CTD; 81790; -.
DR   InParanoid; A0A2I0M6B5; -.
DR   OrthoDB; 154493at2759; -.
DR   Proteomes; UP000053872; Unassembled WGS sequence.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0061630; F:ubiquitin protein ligase activity; IEA:InterPro.
DR   CDD; cd16553; RING-HC_RNF170; 1.
DR   Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR   InterPro; IPR010652; DUF1232.
DR   InterPro; IPR038896; RNF170.
DR   InterPro; IPR027370; Znf-RING_euk.
DR   InterPro; IPR001841; Znf_RING.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   InterPro; IPR017907; Znf_RING_CS.
DR   PANTHER; PTHR22894:SF1; E3 UBIQUITIN-PROTEIN LIGASE RNF170; 1.
DR   PANTHER; PTHR22894; UNCHARACTERIZED; 1.
DR   Pfam; PF06803; DUF1232; 1.
DR   Pfam; PF13445; zf-RING_UBOX; 1.
DR   SMART; SM00184; RING; 1.
DR   SUPFAM; SSF57850; RING/U-box; 1.
DR   PROSITE; PS00518; ZF_RING_1; 1.
DR   PROSITE; PS50089; ZF_RING_2; 1.
PE   4: Predicted;
KW   Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00022824};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000053872};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius};
KW   Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW   ProRule:PRU00175}.
FT   TRANSMEM        27..46
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        190..212
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        224..247
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          88..131
FT                   /note="RING-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50089"
SQ   SEQUENCE   257 AA;  29632 MW;  CFEB36D8AFCD0BA0 CRC64;
     MMASHQAEVQ SLKLDNDSVI EGISDQVLVA VVLSFTFIAA LVYTILRNEH QNIHPENQEL
     VRALRQQLQT EQDASAGDRH RFYTDMSCPV CLQQATFPIE TNCGHLFCGS CIIAYWRYGS
     WLGAIRCPIC RQTVTLFLPL FGEDQQDATQ VLQDVNDYNR RFSGQPRSIM ERIMDLPTLL
     RHAFREMFSV GGLFWMFRIR IFLCLLGALL YLASPLDFLP EALFGILGFL DDFFVIFLLL
     IYISIMYREV VTQRLNR
//
DBGET integrated database retrieval system