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Database: UniProt
Entry: A0A1S3WWU5_ERIEU
LinkDB: A0A1S3WWU5_ERIEU
Original site: A0A1S3WWU5_ERIEU 
ID   A0A1S3WWU5_ERIEU        Unreviewed;       380 AA.
AC   A0A1S3WWU5;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   27-MAR-2024, entry version 27.
DE   RecName: Full=RING-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012483};
DE            EC=2.3.2.27 {ECO:0000256|ARBA:ARBA00012483};
GN   Name=MYLIP {ECO:0000313|RefSeq:XP_016050780.1};
OS   Erinaceus europaeus (Western European hedgehog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Eulipotyphla; Erinaceidae; Erinaceinae;
OC   Erinaceus.
OX   NCBI_TaxID=9365 {ECO:0000313|Proteomes:UP000079721, ECO:0000313|RefSeq:XP_016050780.1};
RN   [1] {ECO:0000313|RefSeq:XP_016050780.1}
RP   IDENTIFICATION.
RG   RefSeq;
RL   Submitted (NOV-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}.
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DR   RefSeq; XP_016050780.1; XM_016195294.1.
DR   AlphaFoldDB; A0A1S3WWU5; -.
DR   CTD; 29116; -.
DR   OrthoDB; 5406876at2759; -.
DR   UniPathway; UPA00143; -.
DR   Proteomes; UP000079721; Unplaced.
DR   GO; GO:0005856; C:cytoskeleton; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
DR   CDD; cd14473; FERM_B-lobe; 1.
DR   CDD; cd13195; FERM_C_MYLIP_IDOL; 1.
DR   CDD; cd16523; RING-HC_MYLIP; 1.
DR   Gene3D; 1.20.80.10; -; 1.
DR   Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1.
DR   Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR   InterPro; IPR019749; Band_41_domain.
DR   InterPro; IPR014352; FERM/acyl-CoA-bd_prot_sf.
DR   InterPro; IPR035963; FERM_2.
DR   InterPro; IPR019748; FERM_central.
DR   InterPro; IPR000299; FERM_domain.
DR   InterPro; IPR018980; FERM_PH-like_C.
DR   InterPro; IPR041790; MYLIP_FERM_C.
DR   InterPro; IPR011993; PH-like_dom_sf.
DR   InterPro; IPR001841; Znf_RING.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   PANTHER; PTHR23280; 4.1 G PROTEIN; 1.
DR   PANTHER; PTHR23280:SF13; E3 UBIQUITIN-PROTEIN LIGASE MYLIP; 1.
DR   Pfam; PF09380; FERM_C; 1.
DR   Pfam; PF00373; FERM_M; 1.
DR   Pfam; PF13920; zf-C3HC4_3; 1.
DR   PRINTS; PR00935; BAND41.
DR   SMART; SM01196; FERM_C; 1.
DR   SUPFAM; SSF50729; PH domain-like; 1.
DR   SUPFAM; SSF57850; RING/U-box; 1.
DR   SUPFAM; SSF47031; Second domain of FERM; 1.
DR   PROSITE; PS50057; FERM_3; 1.
DR   PROSITE; PS50089; ZF_RING_2; 1.
PE   4: Predicted;
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000079721};
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   DOMAIN          1..214
FT                   /note="FERM"
FT                   /evidence="ECO:0000259|PROSITE:PS50057"
FT   DOMAIN          322..357
FT                   /note="RING-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50089"
SQ   SEQUENCE   380 AA;  42349 MW;  77C23B32E2E9BF96 CRC64;
     MDGLAPYRLK LKVKFFVEPH LILQEQTRHI FFLHIKEALL AGHLPCSSEQ AVELSALLAQ
     TKFGDYNQNT AKYSFEELCA KELSSATLNS IVAKHKELEG TSQASAEYQV LQIVSAMENY
     GIEWHSVRDS EGQKLLIGVG PDGISICKED FSPMNRIAYP VVQMATQSGK NVYLTVTKES
     GNSIVLLFKM ISTRAASGLY RAITETHAFY RCDTVTSAVM MQYSRDLKGH LASLFLNENI
     NLGKKYVFDI KRTSKEVYDH ARRALYNAGV VDLVSTSDHS PPNSPLKSTE NGLNCNTCEG
     LSCQQTRALQ EKLRKLKEAM LCMVCCEEEI NSAFCPCGHT VCCESCATQL QSCPVCRSRV
     EHVQHVYLPT HTSLLNLTVI
//
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