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Database: UniProt
Entry: A0A2K6QYA3_RHIRO
LinkDB: A0A2K6QYA3_RHIRO
Original site: A0A2K6QYA3_RHIRO 
ID   A0A2K6QYA3_RHIRO        Unreviewed;       375 AA.
AC   A0A2K6QYA3;
DT   28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT   28-MAR-2018, sequence version 1.
DT   27-MAR-2024, entry version 31.
DE   RecName: Full=E3 ubiquitin-protein ligase RNF34 {ECO:0000256|ARBA:ARBA00039277};
DE            EC=2.3.2.27 {ECO:0000256|ARBA:ARBA00012483};
DE   AltName: Full=RING finger protein 34 {ECO:0000256|ARBA:ARBA00041475};
DE   AltName: Full=RING-type E3 ubiquitin transferase RNF34 {ECO:0000256|ARBA:ARBA00042270};
GN   Name=RNF34 {ECO:0000313|Ensembl:ENSRROP00000033767.1};
OS   Rhinopithecus roxellana (Golden snub-nosed monkey) (Pygathrix roxellana).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Colobinae; Rhinopithecus.
OX   NCBI_TaxID=61622 {ECO:0000313|Ensembl:ENSRROP00000033767.1, ECO:0000313|Proteomes:UP000233200};
RN   [1] {ECO:0000313|Ensembl:ENSRROP00000033767.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-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}. Endomembrane system
CC       {ECO:0000256|ARBA:ARBA00004184}; Peripheral membrane protein
CC       {ECO:0000256|ARBA:ARBA00004184}. Nucleus speckle
CC       {ECO:0000256|ARBA:ARBA00004324}.
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DR   RefSeq; XP_010366631.1; XM_010368329.1.
DR   AlphaFoldDB; A0A2K6QYA3; -.
DR   Ensembl; ENSRROT00000058208.1; ENSRROP00000033767.1; ENSRROG00000040453.1.
DR   GeneID; 104666276; -.
DR   KEGG; rro:104666276; -.
DR   CTD; 80196; -.
DR   GeneTree; ENSGT00390000012719; -.
DR   OMA; SYSGCCE; -.
DR   OrthoDB; 383715at2759; -.
DR   Proteomes; UP000233200; Unplaced.
DR   GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR   GO; GO:0012505; C:endomembrane system; IEA:UniProtKB-SubCell.
DR   GO; GO:0016607; C:nuclear speck; IEA:UniProtKB-SubCell.
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; cd15769; FYVE_CARP1; 1.
DR   CDD; cd16706; RING-HC_CARP1; 1.
DR   Gene3D; 1.10.720.140; -; 1.
DR   Gene3D; 1.10.720.30; SAP domain; 1.
DR   Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR   InterPro; IPR049320; CARP1_2_FYVE.
DR   InterPro; IPR049323; CARP1_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:SF3; E3 UBIQUITIN-PROTEIN LIGASE RNF34; 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   Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW   Reference proteome {ECO:0000313|Proteomes:UP000233200};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW   ProRule:PRU00175}.
FT   DOMAIN          328..363
FT                   /note="RING-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50089"
FT   REGION          194..258
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        194..218
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        219..243
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   375 AA;  41958 MW;  8B4D2DADD84E1AB6 CRC64;
     MKAGATSMWA SCCGLLNEVM GTGAVRGQQS GFAGATGPFR FTPNPDFSTY PPAATEGPNI
     VCKACGLSFS VFRKKHVCCD CKKDFCSVCS VLQENLRRCS TCHLLQETAF QRPQLMRLKV
     KDLRQYLILR NIPIDTCREK EDLVDLVLCH HGLGSEDDMD TSSLNSSRSQ TSSFFTRSFF
     SNYTAPSATM SSFQGELMDG DQTSRSGVPA QVQSEITSAN TEDDDDDDDE DDEDDDDDEE
     NVEDRNPGLS KERARASLSD LSSLDDVEGM SVRQLKEILA RNFVNYSGCC EKWELVEKVN
     RLYKENEENQ KSYGERLQLQ DEEDDSLCRI CMDAVIDCVL LECGHMVTCT KCGKRMSECP
     ICRQYVVRAV HVFKS
//
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