ID A0A452RZU1_URSAM Unreviewed; 955 AA.
AC A0A452RZU1;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 17.
DE SubName: Full=HECT and RLD domain containing E3 ubiquitin protein ligase 4 {ECO:0000313|Ensembl:ENSUAMP00000025094.1};
GN Name=HERC4 {ECO:0000313|Ensembl:ENSUAMP00000025094.1};
OS Ursus americanus (American black bear) (Euarctos americanus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Ursidae; Ursus.
OX NCBI_TaxID=9643 {ECO:0000313|Ensembl:ENSUAMP00000025094.1, ECO:0000313|Proteomes:UP000291022};
RN [1] {ECO:0000313|Proteomes:UP000291022}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Korstanje R., Srivastava A., Sarsani V.K., Sheehan S.M., Seger R.L.,
RA Barter M.E., Lindqvist C., Brody L.C., Mullikin J.C.;
RT "De novo assembly and RNA-Seq shows season-dependent expression and editing
RT in black bear kidneys.";
RL Submitted (JUN-2016) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSUAMP00000025094.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
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DR AlphaFoldDB; A0A452RZU1; -.
DR Ensembl; ENSUAMT00000028032.1; ENSUAMP00000025094.1; ENSUAMG00000017078.1.
DR GeneTree; ENSGT00940000158924; -.
DR Proteomes; UP000291022; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IEA:InterPro.
DR GO; GO:0000209; P:protein polyubiquitination; IEA:InterPro.
DR CDD; cd00078; HECTc; 1.
DR Gene3D; 3.30.2160.10; Hect, E3 ligase catalytic domain; 1.
DR Gene3D; 3.30.2410.10; Hect, E3 ligase catalytic domain; 1.
DR Gene3D; 3.90.1750.10; Hect, E3 ligase catalytic domains; 1.
DR Gene3D; 2.130.10.30; Regulator of chromosome condensation 1/beta-lactamase-inhibitor protein II; 2.
DR InterPro; IPR044611; E3A/B/C-like.
DR InterPro; IPR000569; HECT_dom.
DR InterPro; IPR035983; Hect_E3_ubiquitin_ligase.
DR InterPro; IPR009091; RCC1/BLIP-II.
DR InterPro; IPR000408; Reg_chr_condens.
DR PANTHER; PTHR45700:SF8; HECT DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR45700; UBIQUITIN-PROTEIN LIGASE E3C; 1.
DR Pfam; PF00632; HECT; 1.
DR Pfam; PF00415; RCC1; 6.
DR PRINTS; PR00633; RCCNDNSATION.
DR SMART; SM00119; HECTc; 1.
DR SUPFAM; SSF56204; Hect, E3 ligase catalytic domain; 1.
DR SUPFAM; SSF50985; RCC1/BLIP-II; 1.
DR PROSITE; PS50237; HECT; 1.
DR PROSITE; PS00626; RCC1_2; 3.
DR PROSITE; PS50012; RCC1_3; 6.
PE 4: Predicted;
KW Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000291022};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786,
KW ECO:0000256|PROSITE-ProRule:PRU00104}.
FT TRANSMEM 334..357
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 692..719
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT REPEAT 1..52
FT /note="RCC1"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00235"
FT REPEAT 53..102
FT /note="RCC1"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00235"
FT REPEAT 103..155
FT /note="RCC1"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00235"
FT REPEAT 156..208
FT /note="RCC1"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00235"
FT REPEAT 209..260
FT /note="RCC1"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00235"
FT REPEAT 288..312
FT /note="RCC1"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00235"
FT DOMAIN 628..955
FT /note="HECT"
FT /evidence="ECO:0000259|PROSITE:PS50237"
FT ACT_SITE 923
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00104"
SQ SEQUENCE 955 AA; 107709 MW; 95417D5988D877AE CRC64;
MLCWGNASFG QLGLGGIDEE IVLEPRKSDF FINKKVRDVG CGLRHTVFVL DDGTVYTCGC
NDLGQLGHEK SRKKPEQVVA LDAQNIVAVS CGEAHTLALN DKGQVYAWGL DSDGQLGLLG
SEECIRVPRN IKSLSDIQIV QVACGYYHSL ALSKGNEVFC WGQNKYGQLG LGIDCKKQAS
PQLIKSLLGI PFTQVAAGGA HSFVLTLSGA IFGWGRNKFG QLGLNDENDR YVPNLLKSLR
TQKIVYICCG EDHTAALTKP NVGRNQELNA QLTELTRQHT SAFVPSSGRI YSFGLGGNGQ
LGTGSTSNRK SPFTVKGNWF PYTGQCPPDI GKFCYINVLL FPSLSLSLFS FFVFFFYSND
DHYRTGTKFS GVDMNAARLL FHKLIQPDHP QISQQVAASL EKNLIPKLTS SLPDVEALRF
YLTLPECPLM SDSNNFTTIA IPFGTALVNL EKAPLKVLEN WWSVLEPPLF LKIVELFKEV
VVHLLKLYKI GIPPSERRIF NNFLHTALKV LEILHRVNEK TGQIIQYDKF YIHEVQELID
IRNDYINWLA DIPVTICTYP FVFDAQAKTT LLQTDAVLQM QMAIDQAHRQ NVSSLFLPVI
ESVNPCLILV VRRENIVGDA MEVLRKTKNI DYKKPLKVIF VGEDAVDAGG VRKEFFLLIM
RELLDPKYGM FRYYEESRLI WFSDKTFEDS DLFHLIGVIC GLAIYNFTIV DLHFPLALYK
KLLKKKPSLD DLKELVPDVG RSMQQLLDYP EDDVEETFCL NFTITVENFG ATEVKELVLN
GADTAVNKQN RQEFVDAYVD YIFNKSVASL FDAFHAGFHK VCGGKVLQLF QPNELQAMVI
GNTNYDWKEL EKNTEYKGEY WAEHPTIKIF WEVFHELPLE KKKQFLLFLT GSDRIPILGM
KSLKLVIQST GGGEEYLPVS HTCFNLLDLP KYTEKETLRS KLIQAIDHNE GFSLI
//
