ID H2MKT0_ORYLA Unreviewed; 1510 AA.
AC H2MKT0;
DT 21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 2.
DT 27-MAR-2024, entry version 73.
DE RecName: Full=HECT-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012485};
DE EC=2.3.2.26 {ECO:0000256|ARBA:ARBA00012485};
GN Name=hecw2a {ECO:0000313|Ensembl:ENSORLP00000019301.2};
OS Oryzias latipes (Japanese rice fish) (Japanese killifish).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Beloniformes; Adrianichthyidae; Oryziinae;
OC Oryzias.
OX NCBI_TaxID=8090 {ECO:0000313|Ensembl:ENSORLP00000019301.2, ECO:0000313|Proteomes:UP000001038};
RN [1] {ECO:0000313|Ensembl:ENSORLP00000019301.2, ECO:0000313|Proteomes:UP000001038}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Hd-rR {ECO:0000313|Ensembl:ENSORLP00000019301.2,
RC ECO:0000313|Proteomes:UP000001038};
RX PubMed=17554307; DOI=10.1038/nature05846;
RA Kasahara M., Naruse K., Sasaki S., Nakatani Y., Qu W., Ahsan B., Yamada T.,
RA Nagayasu Y., Doi K., Kasai Y., Jindo T., Kobayashi D., Shimada A.,
RA Toyoda A., Kuroki Y., Fujiyama A., Sasaki T., Shimizu A., Asakawa S.,
RA Shimizu N., Hashimoto S., Yang J., Lee Y., Matsushima K., Sugano S.,
RA Sakaizumi M., Narita T., Ohishi K., Haga S., Ohta F., Nomoto H., Nogata K.,
RA Morishita T., Endo T., Shin-I T., Takeda H., Morishita S., Kohara Y.;
RT "The medaka draft genome and insights into vertebrate genome evolution.";
RL Nature 447:714-719(2007).
RN [2] {ECO:0000313|Ensembl:ENSORLP00000019301.2}
RP IDENTIFICATION.
RC STRAIN=Hd-rR {ECO:0000313|Ensembl:ENSORLP00000019301.2};
RG Ensembl;
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=2.3.2.26; Evidence={ECO:0000256|ARBA:ARBA00000885};
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000256|ARBA:ARBA00004906}.
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DR STRING; 8090.ENSORLP00000019301; -.
DR Ensembl; ENSORLT00000019302.2; ENSORLP00000019301.2; ENSORLG00000015420.2.
DR eggNOG; KOG0940; Eukaryota.
DR GeneTree; ENSGT00940000155466; -.
DR HOGENOM; CLU_002173_14_0_1; -.
DR InParanoid; H2MKT0; -.
DR TreeFam; TF313938; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000001038; Chromosome 21.
DR Bgee; ENSORLG00000015420; Expressed in brain and 3 other cell types or tissues.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IBA:GO_Central.
DR GO; GO:0016567; P:protein ubiquitination; IBA:GO_Central.
DR GO; GO:0048814; P:regulation of dendrite morphogenesis; IBA:GO_Central.
DR CDD; cd08691; C2_NEDL1-like; 1.
DR CDD; cd00078; HECTc; 1.
DR CDD; cd00201; WW; 2.
DR Gene3D; 2.20.70.10; -; 2.
DR Gene3D; 2.60.40.2840; -; 1.
DR Gene3D; 2.60.40.150; C2 domain; 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 InterPro; IPR000008; C2_dom.
DR InterPro; IPR035892; C2_domain_sf.
DR InterPro; IPR037795; C2_HECW.
DR InterPro; IPR000569; HECT_dom.
DR InterPro; IPR035983; Hect_E3_ubiquitin_ligase.
DR InterPro; IPR040524; HECW1_helix.
DR InterPro; IPR032348; HECW_N.
DR InterPro; IPR001202; WW_dom.
DR InterPro; IPR036020; WW_dom_sf.
DR PANTHER; PTHR11254:SF127; E3 UBIQUITIN-PROTEIN LIGASE HECW2; 1.
DR PANTHER; PTHR11254; HECT DOMAIN UBIQUITIN-PROTEIN LIGASE; 1.
DR Pfam; PF00168; C2; 1.
DR Pfam; PF00632; HECT; 1.
DR Pfam; PF18436; HECW1_helix; 1.
DR Pfam; PF16562; HECW_N; 1.
DR Pfam; PF00397; WW; 1.
DR SMART; SM00239; C2; 1.
DR SMART; SM00119; HECTc; 1.
DR SMART; SM00456; WW; 2.
DR SUPFAM; SSF49562; C2 domain (Calcium/lipid-binding domain, CaLB); 1.
DR SUPFAM; SSF56204; Hect, E3 ligase catalytic domain; 1.
DR SUPFAM; SSF51045; WW domain; 2.
DR PROSITE; PS50004; C2; 1.
DR PROSITE; PS50237; HECT; 1.
DR PROSITE; PS01159; WW_DOMAIN_1; 2.
DR PROSITE; PS50020; WW_DOMAIN_2; 2.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000001038};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786,
KW ECO:0000256|PROSITE-ProRule:PRU00104}.
FT DOMAIN 194..326
FT /note="C2"
FT /evidence="ECO:0000259|PROSITE:PS50004"
FT DOMAIN 753..786
FT /note="WW"
FT /evidence="ECO:0000259|PROSITE:PS50020"
FT DOMAIN 932..965
FT /note="WW"
FT /evidence="ECO:0000259|PROSITE:PS50020"
FT DOMAIN 1175..1510
FT /note="HECT"
FT /evidence="ECO:0000259|PROSITE:PS50237"
FT REGION 1..41
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 348..411
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 443..465
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 577..598
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 657..739
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 814..838
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 986..1016
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 348..371
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 669..683
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1002..1016
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 1478
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00104"
SQ SEQUENCE 1510 AA; 168844 MW; E13B49D8FF5DF540 CRC64;
MRPSLATAVL PARTRSHNPP NLAVGGREHL SAPRRRSPHL RHTLSPDNLR TLAERGGAAV
DPTSVVSSPV GLTRANSDTD LVSSQSRSSL TASTLEHTLN RGQNLVISWD IKEEVDATDW
IGLYHIDETS PSNVWDCKNR GVNGTQKGQI VWRLEPGPYF MEPETKICFK YYHGVSGALR
ATTPCITVKN PAVLMEGLAE QVGIDHPRKL ISFTLTDLCA TGLKKGMFFN PDPYLKMSIH
PGKRSIFPVF SHHGQERRSA IIANTTNPVW HGEKYTFVAL MTDILYIEVK DKFAKSRPII
KRFLGQLTIP VQRLIEKIPG VQPVTFSLCR RLPTEHVSGQ LQFKVELTST GPDGASPDSI
IGISSLNEAP GTPSDDEDLP HPLPVVVSAG PSPTGSQAMW EGGATASPEK SPSVVGAASR
FVNSDLFAGH DFLQRSLSEG LDAIEAPKGP GERPLGAASP KLQSSFPTHT RLSAMLHIDS
DEDEERSGIH DIAPVPLSPL LMNGEPPDSC CHDEDDLFQQ VPEQLEHLVC EEEPAGAAAE
DLHPEGNEEA DLAFEDVLDT EVFLEVEEGP FIEVSPETAP PEAIEATEQG RGEDPSSEID
TCSMATAPQT VFSSSESCPV TLTTATEANE GAEAAIDPGG NAPSSALLTR LPVNDKHGGQ
AAVSEAEGDA PRASEEGEVE ELSVRRLSLQ ATGGVDEEQE GEETKTRKAV TTDESQQATT
DADRDQGRHV NGHPVRSLPS VRHDIHRYQR VDEPLPPNWE ARIDSHGRIF FVDHVNRTTT
WQRPTGPPAP QGLTRSNSIQ QMEQLNRRYQ SIRRTITNSS RSEESSTELP PEPDNEMMPH
AISEYRRDSS VTHSGGRSRL SLLLQSPSAK FLCSPDFFTV LHSNPSAYRM FTSNTCLKHM
ISKVRRDAHY FERYQHNRDL VTFLNMFANK QLELPRGWEM KHDHTGKPFF VDHNCRSTTF
IDPRLPLQSS RSTGLLAHRQ HLSRQRSHSA GEVVDDSRQS VTPVMPRPSS TFSGSSRSQY
HDVVPVAYND KIVAFLRQPN ILEILQERQP ELARNHSLKE KVQFIRSEGV NGLARLSSDA
DLVMLLSLFE DEVMSYVPSL LHPGYCISSP QSSPGTQRAN ARAPAPYKRD FEAKLRNFYR
KLETKGYGQG PGKVKLIIRR DHLLEDAFNQ IMCYSRKDLQ RSKLYVSFVG EDGLDYSGPS
REFFFLVSRE LFNPYYGLFE YSANDTYTVQ ISPMSAFVDN HHEWFRFSGR ILGLALVHQY
LLDAFFTRPF YKGLLRIPCD LSDLEFLDEE FHQSLQWMKD NDIEDMLDLT FTVNEEVFGQ
ITERELKPGG AGVSVSEKNK KEYIERMVKW RIERGVAQQT ESLVRGFYEV VDVRLVSVFD
ARELELVIAG TAEIDLADWR NNTEYRGGYH DNHIVIRWFW AAVERFNNEQ RLRLLQFVTG
TSSIPYEGFA SLRGSNGPRR FCVEKWGKIT SLPRAHTCFN RLDLPPYPSF SMLYEKLVTA
VEETSTFGLE
//
