ID A0A2D0RSF0_ICTPU Unreviewed; 372 AA.
AC A0A2D0RSF0;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 24-JAN-2024, entry version 30.
DE RecName: Full=RING-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012483};
DE EC=2.3.2.27 {ECO:0000256|ARBA:ARBA00012483};
GN Name=rnf13 {ECO:0000313|RefSeq:XP_017333425.1,
GN ECO:0000313|RefSeq:XP_017333427.1, ECO:0000313|RefSeq:XP_017333429.1,
GN ECO:0000313|RefSeq:XP_047013970.1};
OS Ictalurus punctatus (Channel catfish) (Silurus punctatus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Siluriformes;
OC Ictaluridae; Ictalurus.
OX NCBI_TaxID=7998 {ECO:0000313|RefSeq:XP_017333429.1};
RN [1] {ECO:0000313|RefSeq:XP_017333425.1, ECO:0000313|RefSeq:XP_017333427.1}
RP IDENTIFICATION.
RC TISSUE=Blood {ECO:0000313|RefSeq:XP_017333425.1,
RC ECO:0000313|RefSeq:XP_017333427.1};
RG RefSeq;
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: Membrane {ECO:0000256|ARBA:ARBA00004479}; Single-
CC pass type I membrane protein {ECO:0000256|ARBA:ARBA00004479}.
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DR RefSeq; XP_017333425.1; XM_017477936.2.
DR RefSeq; XP_017333426.1; XM_017477937.1.
DR RefSeq; XP_017333427.1; XM_017477938.2.
DR RefSeq; XP_017333429.1; XM_017477940.2.
DR RefSeq; XP_047013970.1; XM_047158014.2.
DR STRING; 7998.ENSIPUP00000034886; -.
DR GeneID; 108270921; -.
DR KEGG; ipu:108270921; -.
DR CTD; 11342; -.
DR OrthoDB; 5474929at2759; -.
DR Proteomes; UP000221080; Chromosome 10.
DR GO; GO:0012505; C:endomembrane system; IEA:UniProt.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR044744; ZNRF4/RNF13/RNF167_PA.
DR PANTHER; PTHR45931:SF2; E3 UBIQUITIN-PROTEIN LIGASE RNF6; 1.
DR PANTHER; PTHR45931; SI:CH211-59O9.10; 1.
DR Pfam; PF02225; PA; 1.
DR Pfam; PF13639; zf-RING_2; 1.
DR SMART; SM00184; RING; 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|SAM:Phobius};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00175}.
FT SIGNAL 1..28
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 29..372
FT /note="RING-type E3 ubiquitin transferase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5013510580"
FT TRANSMEM 178..203
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 236..278
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT REGION 286..372
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 318..336
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 372 AA; 41498 MW; AC464A96C77F25E4 CRC64;
MLLPIAMLML TLTQIFIITF ISLLPVEADI AAYSADNQTE TFDDAPARFG YRLPNQGLKG
FLIGARPENG CVPIDPPPIK DNSSSSSSFI VLIKRYHCNF DIKVLNAQRA GYIAAIVHNV
DSEELVNMGS DDLEVVKQIN IPSVFVGEKV SKSLMEEYSY ERGGYVILMP DFSLPLEYYL
IPFLIIVGIC LILIVVFMIT KFVQDRRRSR RSRLRKDQLK KLPIHKYKKG DVYDVCAICL
DEYEEGEKLR VLPCSHAYHC KCVDPWLTKT KRTCPVCKQK VVLAGSESDS DSDSGGDESD
EVSESTPLLR PQPPARIRTP SLASTHSAST SHPDCSDSDS DSTEEEVEGE VVTVETVVVL
QQERPDDDLI NA
//