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Database: UniProt
Entry: A0A2D0RSF0_ICTPU
LinkDB: A0A2D0RSF0_ICTPU
Original site: A0A2D0RSF0_ICTPU 
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
//
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