RING2_CAEEL
ID RING2_CAEEL Reviewed; 2476 AA.
AC H2KYH3; Q22463;
DT 23-FEB-2022, integrated into UniProtKB/Swiss-Prot.
DT 21-MAR-2012, sequence version 1.
DT 03-AUG-2022, entry version 75.
DE RecName: Full=E3 ubiquitin-protein ligase RING2 homolog spat-3 {ECO:0000305};
DE AltName: Full=RING domain-containing protein spat-3 {ECO:0000303|PubMed:19211678};
DE EC=2.3.2.27 {ECO:0000250|UniProtKB:Q99496};
GN Name=spat-3 {ECO:0000312|WormBase:T13H2.5a};
GN ORFNames=T13H2.5 {ECO:0000312|WormBase:T13H2.5a};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239 {ECO:0000312|Proteomes:UP000001940};
RN [1] {ECO:0000312|Proteomes:UP000001940}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2 {ECO:0000312|Proteomes:UP000001940};
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [2] {ECO:0000305}
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=19211678; DOI=10.1242/dev.029363;
RA Karakuzu O., Wang D.P., Cameron S.;
RT "MIG-32 and SPAT-3A are PRC1 homologs that control neuronal migration in
RT Caenorhabditis elegans.";
RL Development 136:943-953(2009).
CC -!- FUNCTION: E3 ubiquitin-protein ligase playing a central role in histone
CC code and gene regulation (By similarity). Involved in ubiquitination of
CC histone H2A (PubMed:19211678). Plays a role in the formation of the
CC male-specific genital sensilla (simple sense organs) known as rays
CC (PubMed:19211678). Required for normal migration of the hermaphrodite
CC specific neurons (HSN) and for extension of some neuronal processes
CC (PubMed:19211678). Represses vulval fates in hypodermal cells that do
CC not normally contribute to vulval development (PubMed:19211678).
CC {ECO:0000250|UniProtKB:Q99496, ECO:0000269|PubMed:19211678}.
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:0000250|UniProtKB:Q99496};
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000250|UniProtKB:Q99496}.
CC -!- SUBUNIT: Component of chromatin-associated Polycomb (PcG) complexes (By
CC similarity). Component of a PRC1-like complex (By similarity).
CC {ECO:0000250|UniProtKB:Q99496, ECO:0000250|UniProtKB:Q9CQJ4}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=a {ECO:0000312|WormBase:T13H2.5a};
CC IsoId=H2KYH3-1; Sequence=Displayed;
CC Name=b {ECO:0000312|WormBase:T13H2.5b};
CC IsoId=H2KYH3-2; Sequence=VSP_061241;
CC -!- DISRUPTION PHENOTYPE: RNAi-mediated knockdown in a lin-15 mutant
CC background causes a multiple vulva (Muv) phenotype.
CC {ECO:0000269|PubMed:19211678}.
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DR EMBL; BX284606; CCD63269.1; -; Genomic_DNA.
DR EMBL; BX284606; CCD63270.1; -; Genomic_DNA.
DR RefSeq; NP_001024904.2; NM_001029733.2.
DR RefSeq; NP_001024905.1; NM_001029734.1.
DR AlphaFoldDB; H2KYH3; -.
DR SMR; H2KYH3; -.
DR IntAct; H2KYH3; 1.
DR STRING; 6239.T13H2.5a; -.
DR EPD; H2KYH3; -.
DR PaxDb; H2KYH3; -.
DR PeptideAtlas; H2KYH3; -.
DR EnsemblMetazoa; T13H2.5a.1; T13H2.5a.1; WBGene00020496. [H2KYH3-1]
DR EnsemblMetazoa; T13H2.5b.1; T13H2.5b.1; WBGene00020496. [H2KYH3-2]
DR GeneID; 259704; -.
DR KEGG; cel:CELE_T13H2.5; -.
DR CTD; 259704; -.
DR WormBase; T13H2.5a; CE44993; WBGene00020496; spat-3.
DR WormBase; T13H2.5b; CE31236; WBGene00020496; spat-3.
DR eggNOG; KOG0311; Eukaryota.
DR HOGENOM; CLU_226831_0_0_1; -.
DR InParanoid; H2KYH3; -.
DR OMA; MNPARME; -.
DR OrthoDB; 893926at2759; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000001940; Chromosome X.
DR Bgee; WBGene00020496; Expressed in embryo and 4 other tissues.
DR ExpressionAtlas; H2KYH3; baseline and differential.
DR GO; GO:0031519; C:PcG protein complex; IBA:GO_Central.
DR GO; GO:0000151; C:ubiquitin ligase complex; IBA:GO_Central.
DR GO; GO:0003682; F:chromatin binding; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IBA:GO_Central.
DR GO; GO:0035518; P:histone H2A monoubiquitination; IBA:GO_Central.
DR GO; GO:0033522; P:histone H2A ubiquitination; IMP:WormBase.
DR GO; GO:0045814; P:negative regulation of gene expression, epigenetic; IGI:WormBase.
DR GO; GO:0040027; P:negative regulation of vulval development; IGI:WormBase.
DR GO; GO:0045138; P:nematode male tail tip morphogenesis; IMP:WormBase.
DR GO; GO:0030334; P:regulation of cell migration; IMP:WormBase.
DR GO; GO:0000003; P:reproduction; IMP:WormBase.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR043540; RING1/RING2.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR017907; Znf_RING_CS.
DR PANTHER; PTHR46076; PTHR46076; 1.
DR SMART; SM00184; RING; 1.
DR PROSITE; PS00518; ZF_RING_1; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 3: Inferred from homology;
KW Alternative splicing; Coiled coil; Metal-binding; Reference proteome;
KW Transferase; Zinc; Zinc-finger.
FT CHAIN 1..2476
FT /note="E3 ubiquitin-protein ligase RING2 homolog spat-3"
FT /id="PRO_0000454046"
FT ZN_FING 162..202
FT /note="RING-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT REGION 1..85
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 263..510
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 532..644
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 703..791
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 890..929
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 971..1043
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1296..1454
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1728..1762
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1809..1837
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2049..2070
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2186..2205
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1990..2088
FT /evidence="ECO:0000255"
FT COMPBIAS 35..75
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 283..347
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 348..367
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 386..404
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 496..510
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 532..570
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 611..638
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 720..771
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1304..1376
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1386..1418
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2049..2064
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 1..1384
FT /note="Missing (in isoform b)"
FT /evidence="ECO:0000305"
FT /id="VSP_061241"
SQ SEQUENCE 2476 AA; 276431 MW; BB60F77416888847 CRC64;
MDDSPGPSTS KSARDKAENA EENTSDSSSD SEVSSASEKS EESRPSSEKK KVITRVIPVR
PPTRDKGHRV NLLESGNESE TKSLYQRAKE GIPSYKGKPE IKLPTTSEQY YDLEEVLMNP
ARMEGRELTL NAYDAVRNKY NVLPGKSVCE ADLQKVIGSF SCDVCQELIQ GSIMTKKCGH
RFCDQCILVA FMRSGNTCPT CRQNLGSKRE LQQDPRFDQL IYQVVESRSI VGRMMAENRE
HEKDVYFGRK GYIEGGSDWN KRYGIDPNSK LKAPRPLKSA GRKKIRWFHE SDEDGSVRKV
MESKKGAPKE DDTNYLENDK EGTSVAAEKE VLEEGEMDFP IEIKSSDEEQ TDLDDEEESM
LDSDFEISDN EDVSKPSCST SKKTTNRSRD SSESDNDSRD NELQKKKRKM KRKNVPKTDG
SDVSNESFDE DASGEVVATK LIKESKKKPC GRPKKKFAPE LIEGDIPTPS EDSLTSSDEE
RDDNAADPYA FVFQKEFNRD PRRDGHPEKD KLYNFDFMID MNHQVDRKFE KDGEIHVISD
DSNSEHESDE AEDRESSIDS EHEKEISKFL SHRQPLPNPT SVDDDCQVIT VVKKDVKQSA
ITSKPGETSP DSSSKIEEKP DKVSEEVSDD EMTPEHITAD KGTDTFLNNI MEHDDEMYGG
YLFRPGDTGI SRPKVQRAPG TNRLSMNVCP EAVYVVYPQP VLKEGKKKLV IPPEDYEISS
DETVTLSDSE ETSPSAEMEQ SETSEAGPST IIKTSGTERE TQGSSSPSEP STSRDRKMHK
RKLDTRRRKL ADDSDLSDFD VFSIDGNELV ATGKPIIKHK VFYDSANRMP SKSNLDFTGR
RNAREIPMEE ISRLAEEQVA HEEYKIHRRR QVVLEAVEAA SKKLNVYVDT TEEEEIEEEE
TPEEEVVKVA SPTAPIATEN PTTSTAPFEE GVAMKETPIE EIFFDPDEPC SSAQAAQREL
IIERVGKEQQ IIEDSLEQNR KPSSKTVKES ESREAQEPRI EKDEMESEQQ KKDADNPTVE
VDKESEASSS ESDKSDFEDE TLDAQSKTVK ISLKHEKTVS DEEIEDFDTK FGEFVATADA
KMIKRTIGEY VSTEFLKLVA QQPAVTDEVL ALGFCVRNTD QEFSTIKETG KRTNKNPDDV
RLESMVKNFR ESFAAKHRPV PRKLPTNIER MYIERAHMVK YKHVVDMEPL HMKILIALQK
QQIAATCANL SQPVTVTPEE HAEQVQLLHN LQNPSILRPL LNNPQFALTL HKAQQQAIQQ
QRAQQKAQTQ KELAARQAEQ ARVEELARKR IAQEDAEKAL RQKGEQMSNV SGIPVSSDQN
AQSSNAQQTG LIENQTTTTN SDSLTRPNTL ADNSHLGESQ QIPVIESIQS STSEALKESE
NYKDMPILTP ASTVSSKSSA PATRRPSRPC SSYDRPSSPS VVIRERLGSD GALINRPPNR
CNIDKSRSRS PISRAPVETV RINDHGQNET ILAGNITHTV ETTILEEGTS IGQDSTIRYD
GECSTTQYID KTIDLDNSKN GTNVDEEQSN VLKLRENDLN REMLRYANRY HPSTMLAMGN
LSINERHNKV QQVLASQELQ DLIARHTSGA VSQTQVEVVG GEGVCAGTSD AIGETDEDDD
VEEEPEFTVD QLELAKKILK QRQGLESSED SDSDEDMVYD NVDGSVIRRA PHKKRETRKK
KNIFVPNIPP KIRRKYVDKK IEMERAKYRA RIKSQKMASI RIAVPQKPTQ QFATPQQPVR
GPGKHSAAAA ARATPKPKKA KMSNVQMSIV QPPLPLHQLQ GHMSAPTKIT AVPNVAAGFH
QNQQQLYSDM AQAPQSTPIR TTPQPGTGSA PQAQTPQSHL AQLGQFVNGA NQQQAPQQQG
MYTAAQLQAM QAAVAQTAQA AQAAYAAEAA YQAQVAQQAR AAPPQQLVQR QVPVGHPGQV
NVPMPAQMLN QGNPQMAVNP AQAQMMDERR KMEEVNAVYH LMQSRGQFPP TNQELFQVQF
AQAQADLRSA AAQAAQAAQA QAQMTNMRAQ AEAVARQQAM MKQEQARAQA AAKEAARLKA
ETEAAKAKVQ AEAEARRKAE QEMRVRQAQA AQTQAAQAQA QSQAHAQNQA QTQAIVEIQR
MIQSGQPLSM QQMQQLQQMS QVQMQHAQQV QQMQQMQMQQ LQMQQFAARM QQGTPKPAVS
QQAVQQGMPA GIQGMPTGMG MQQLQGLGMP GMQLPQQAGQ SQQTSQAQQQ QLFMQLQLQQ
QQLMQHQLQQ QLQMQQHQQH QQQQQQIQMQ QQQQLAQQGL VPNVSSAWLQ QQAQLAQQQQ
QVVQQNLLMR VPSAQTPVAP RAPTVAPQSV VQQAPAPATP IAISVATTQV TRPETVEPFR
SISSGTGTGT ERINNNVELE LWPTNGYSEK KRKEGSQASP IFGASAGDST FYHVACLIRS
RSACNADDVG SLWVLRLEDQ TLLQFQLQQT LAEAQRFVGK QHLVIFYDDV MSGEVQQSKE
YVINREFKPS NRQIPN
