CNT2_CAEEL
ID CNT2_CAEEL Reviewed; 1107 AA.
AC Q9XX14; Q9U2M2; Q9XX09; Q9XZQ3; Q9XZQ4;
DT 15-FEB-2017, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2001, sequence version 2.
DT 03-AUG-2022, entry version 181.
DE RecName: Full=Arf-GAP with ANK repeat and PH domain-containing protein cnt-2 {ECO:0000305};
DE AltName: Full=Centaurin-gamma-like protein cnt-2 {ECO:0000305};
GN Name=cnt-2 {ECO:0000312|WormBase:Y39A1A.15a};
GN ORFNames=Y39A1A.15 {ECO:0000312|WormBase:Y39A1A.15a};
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|EMBL:CAA10737.1}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS A AND B).
RC STRAIN=Bristol N2 {ECO:0000312|EMBL:CAA10737.1};
RA Harrington L.S., Baylis H.A., Jackson T.R.;
RT "Investigating the functions of the centaurin proteins in phosphoinositide
RT signalling in C. elegans.";
RL Submitted (FEB-1999) to the EMBL/GenBank/DDBJ databases.
RN [2] {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 [3] {ECO:0000305}
RP FUNCTION, ALTERNATIVE SPLICING, DOMAIN, DISRUPTION PHENOTYPE, AND
RP MUTAGENESIS OF CYS-837; CYS-840 AND ARG-865.
RX PubMed=21596567; DOI=10.1016/j.cub.2011.04.025;
RA Singhvi A., Teuliere J., Talavera K., Cordes S., Ou G., Vale R.D.,
RA Prasad B.C., Clark S.G., Garriga G.;
RT "The Arf GAP CNT-2 regulates the apoptotic fate in C. elegans asymmetric
RT neuroblast divisions.";
RL Curr. Biol. 21:948-954(2011).
CC -!- FUNCTION: GTPase-activating protein for the ADP ribosylation factor
CC family (Probable). During neurogenesis, involved in cell autonomous
CC neuroblast asymmetric divisions that generate one precursor cell and
CC one apoptotic cell probably by controlling endocytosis. In oocytes,
CC involved in vitellogenin vit-2 uptake by regulating receptor rme-2
CC endocytosis. {ECO:0000269|PubMed:21596567, ECO:0000305}.
CC -!- FUNCTION: [Isoform b]: During neurogenesis, involved in cell autonomous
CC neuroblast asymmetric divisions that generate one precursor cell and
CC one apoptotic cell probably by controlling endocytosis.
CC {ECO:0000269|PubMed:21596567}.
CC -!- INTERACTION:
CC Q9XX14; G5EGG0: uso-1; NbExp=3; IntAct=EBI-330314, EBI-311986;
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=a {ECO:0000312|WormBase:Y39A1A.15a};
CC IsoId=Q9XX14-1; Sequence=Displayed;
CC Name=b {ECO:0000312|WormBase:Y39A1A.15b};
CC IsoId=Q9XX14-2; Sequence=VSP_058773;
CC Name=c {ECO:0000312|WormBase:Y39A1A.15c};
CC IsoId=Q9XX14-3; Sequence=VSP_058772;
CC -!- DOMAIN: The N-terminal domain is required for the positive control of
CC neuroblast asymmetric divisions. {ECO:0000269|PubMed:21596567}.
CC -!- DISRUPTION PHENOTYPE: RNAi-mediated knockdown in a ced-3 n2436 mutant
CC background results in the production of extra A/PVM neurons; the
CC precursor Q.pp, which is normally fated to die, acquires the fate of
CC its sister Q.pa. {ECO:0000269|PubMed:21596567}.
CC -!- SIMILARITY: Belongs to the centaurin gamma-like family. {ECO:0000305}.
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DR EMBL; AJ132700; CAA10736.1; -; mRNA.
DR EMBL; AJ132701; CAA10737.1; -; mRNA.
DR EMBL; BX284603; CAA21026.2; -; Genomic_DNA.
DR EMBL; BX284603; CAA21027.1; -; Genomic_DNA.
DR EMBL; BX284603; CAA21032.1; -; Genomic_DNA.
DR PIR; T26737; T26737.
DR PIR; T26738; T26738.
DR PIR; T26743; T26743.
DR RefSeq; NP_001022836.1; NM_001027665.2. [Q9XX14-1]
DR RefSeq; NP_001022837.1; NM_001027666.3. [Q9XX14-2]
DR RefSeq; NP_001022838.1; NM_001027667.2. [Q9XX14-3]
DR AlphaFoldDB; Q9XX14; -.
DR SMR; Q9XX14; -.
DR DIP; DIP-25025N; -.
DR IntAct; Q9XX14; 1.
DR STRING; 6239.Y39A1A.15a; -.
DR PaxDb; Q9XX14; -.
DR EnsemblMetazoa; Y39A1A.15a.1; Y39A1A.15a.1; WBGene00000566. [Q9XX14-1]
DR EnsemblMetazoa; Y39A1A.15b.1; Y39A1A.15b.1; WBGene00000566. [Q9XX14-2]
DR EnsemblMetazoa; Y39A1A.15b.2; Y39A1A.15b.2; WBGene00000566. [Q9XX14-2]
DR EnsemblMetazoa; Y39A1A.15c.1; Y39A1A.15c.1; WBGene00000566. [Q9XX14-3]
DR GeneID; 176490; -.
DR KEGG; cel:CELE_Y39A1A.15; -.
DR UCSC; Y39A1A.15b; c. elegans.
DR CTD; 176490; -.
DR WormBase; Y39A1A.15a; CE28116; WBGene00000566; cnt-2. [Q9XX14-1]
DR WormBase; Y39A1A.15b; CE19135; WBGene00000566; cnt-2. [Q9XX14-2]
DR WormBase; Y39A1A.15c; CE20232; WBGene00000566; cnt-2. [Q9XX14-3]
DR eggNOG; KOG0705; Eukaryota.
DR GeneTree; ENSGT00940000169062; -.
DR InParanoid; Q9XX14; -.
DR OMA; WYGANIK; -.
DR OrthoDB; 751525at2759; -.
DR PhylomeDB; Q9XX14; -.
DR PRO; PR:Q9XX14; -.
DR Proteomes; UP000001940; Chromosome III.
DR Bgee; WBGene00000566; Expressed in pharyngeal muscle cell (C elegans) and 4 other tissues.
DR ExpressionAtlas; Q9XX14; baseline and differential.
DR GO; GO:0005525; F:GTP binding; IEA:InterPro.
DR GO; GO:0005096; F:GTPase activator activity; IBA:GO_Central.
DR GO; GO:0003924; F:GTPase activity; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0090630; P:activation of GTPase activity; IMP:WormBase.
DR GO; GO:0055059; P:asymmetric neuroblast division; IMP:WormBase.
DR GO; GO:0060582; P:cell fate determination involved in pattern specification; IMP:WormBase.
DR GO; GO:0006897; P:endocytosis; IEA:UniProtKB-KW.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR GO; GO:0048259; P:regulation of receptor-mediated endocytosis; IMP:WormBase.
DR Gene3D; 1.10.220.150; -; 1.
DR Gene3D; 1.25.40.20; -; 1.
DR Gene3D; 2.30.29.30; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR002110; Ankyrin_rpt.
DR InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR InterPro; IPR037278; ARFGAP/RecO.
DR InterPro; IPR001164; ArfGAP_dom.
DR InterPro; IPR038508; ArfGAP_dom_sf.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR001849; PH_domain.
DR InterPro; IPR001806; Small_GTPase.
DR Pfam; PF12796; Ank_2; 1.
DR Pfam; PF01412; ArfGap; 1.
DR Pfam; PF00071; Ras; 1.
DR PRINTS; PR00405; REVINTRACTNG.
DR SMART; SM00248; ANK; 2.
DR SMART; SM00105; ArfGap; 1.
DR SMART; SM00233; PH; 1.
DR SMART; SM00174; RHO; 1.
DR SUPFAM; SSF48403; SSF48403; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR SUPFAM; SSF57863; SSF57863; 1.
DR PROSITE; PS50297; ANK_REP_REGION; 1.
DR PROSITE; PS50088; ANK_REPEAT; 1.
DR PROSITE; PS50115; ARFGAP; 1.
DR PROSITE; PS50003; PH_DOMAIN; 1.
DR PROSITE; PS51419; RAB; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; ANK repeat; Endocytosis; GTPase activation;
KW Metal-binding; Protein transport; Reference proteome; Repeat; Transport;
KW Zinc; Zinc-finger.
FT CHAIN 1..1107
FT /note="Arf-GAP with ANK repeat and PH domain-containing
FT protein cnt-2"
FT /id="PRO_0000438978"
FT DOMAIN 610..802
FT /note="PH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT DOMAIN 822..943
FT /note="Arf-GAP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00288"
FT REPEAT 980..1009
FT /note="ANK 1"
FT /evidence="ECO:0000255"
FT REPEAT 1013..1042
FT /note="ANK 2"
FT /evidence="ECO:0000255"
FT ZN_FING 837..860
FT /note="C4-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00288"
FT REGION 88..176
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 405..509
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 551..581
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 681..764
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1062..1107
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 88..105
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 152..176
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 405..422
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 431..457
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 465..491
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 713..727
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 747..764
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1062..1076
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 1..237
FT /note="MPLIRNYDYYDLLNVAPSTSAHRPTVMVTSSRSYMEPQKSRIYYGKNEWRGG
FT NTTIHDPTEFEETTMDKNANEIAGDDKRKKKRWRDLLFPNSRHSSRKDKENSNVSVATR
FT SLSSVSFRSEKPSRRRESGSLSRHRYIPPPPLPMPPRRIMTSTSMGYSDDAMTSSSSHT
FT TTDYDDIVPVPTPSYVIYPAASIAQASRRQQQGSAKNRIFRSPTYHHDAFVNSHEWTLS
FT RSISEMKL -> MTVASYLLVDFLQWYKSLGASTLSTKYYHKFRI (in isoform
FT c)"
FT /evidence="ECO:0000305"
FT /id="VSP_058772"
FT VAR_SEQ 1..217
FT /note="MPLIRNYDYYDLLNVAPSTSAHRPTVMVTSSRSYMEPQKSRIYYGKNEWRGG
FT NTTIHDPTEFEETTMDKNANEIAGDDKRKKKRWRDLLFPNSRHSSRKDKENSNVSVATR
FT SLSSVSFRSEKPSRRRESGSLSRHRYIPPPPLPMPPRRIMTSTSMGYSDDAMTSSSSHT
FT TTDYDDIVPVPTPSYVIYPAASIAQASRRQQQGSAKNRIFRSPTYHH -> MSRHLLTG
FT GNNTLHSEQIRSEIQRFESVHPCIYQIYDLLNLLPDGCHAISEQIREQIVSVE (in
FT isoform b)"
FT /evidence="ECO:0000305"
FT /id="VSP_058773"
FT MUTAGEN 837
FT /note="C->S: Probable loss of cognate arf binding and
FT production of extra A/PVM neurons, when associated with S-
FT 840."
FT /evidence="ECO:0000269|PubMed:21596567"
FT MUTAGEN 840
FT /note="C->S: Probable loss of cognate arf binding and
FT production of extra A/PVM neurons, when associated with S-
FT 837."
FT /evidence="ECO:0000269|PubMed:21596567"
FT MUTAGEN 865
FT /note="R->K: Probable loss of GTPase-activating protein
FT (GAP) activity. Production of extra A/PVM neurons."
FT /evidence="ECO:0000269|PubMed:21596567"
FT CONFLICT 272
FT /note="K -> G (in Ref. 1; CAA10737)"
FT /evidence="ECO:0000305"
FT CONFLICT 642
FT /note="R -> RR (in Ref. 1; CAA10736)"
FT /evidence="ECO:0000305"
FT CONFLICT 1048
FT /note="I -> T (in Ref. 1; CAA10736)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1107 AA; 123081 MW; 1952FCE4923E7360 CRC64;
MPLIRNYDYY DLLNVAPSTS AHRPTVMVTS SRSYMEPQKS RIYYGKNEWR GGNTTIHDPT
EFEETTMDKN ANEIAGDDKR KKKRWRDLLF PNSRHSSRKD KENSNVSVAT RSLSSVSFRS
EKPSRRRESG SLSRHRYIPP PPLPMPPRRI MTSTSMGYSD DAMTSSSSHT TTDYDDIVPV
PTPSYVIYPA ASIAQASRRQ QQGSAKNRIF RSPTYHHDAF VNSHEWTLSR SISEMKLGIV
GTSQSGKTAL VHRYLTGTYT PDESPEGGRF KKEVVIEGQS HLLLIRDEGQ QHLDVQFCQW
VDAVVFVFNV CSIQSYDSIQ ALAHEMSKYR NISDLPLILV GTKDHISEKR ARVITEDEGR
QLAAQMKRCS YFETSSTYGT NVERVFKEAC CKIIQLRVRS QVGAAAAASS QARTPTPTHS
ESGGRKDYQD PSRYISSNSF VMPSNMRPSF PSNSTRRNTV HHRGEHPQQQ QYQQQPPSSS
RTASERSMSA MLGTPYGNRM PAGVSPSASQ KSVHSIANGC YSRSSAALLD SDTPAVNSYL
IDSMSSAGFP LSQSGANQVS ASTSHLPTPS STPNTQRKNR RISNIFRQKD HQEEKSKMIE
SLNLGIGRAI PIKQGNLYKK SSKSALNREW KKKYVCLYSD GRLTYHTNLK EYMDKTAHGK
EMDLKLATIR ITGRLHPLHS HRVASSVDPM NGGGGGGTPT LKSYEPRRSD VGANSGDGTS
GGGSDDAIKE NQRQHFSPPA MPQTVAGKKK RESRKIGTNS KHNDEEDECF EVINNCLMRW
EFCAGSLEER DEWIQAIGGE IEKSLGKEVA NAKTNNRAVA NRPDIAALRS IPGNGRCADC
GNPSSEWASI NLGIIICIEC SGIHRNLGSH ISKVRGLELD QWPVEHLAVM QAIGNDKANE
MWEFGLLNGE RKPTPESSRE EKERFIDRKY VQKAFLKPIA SGEPVTSQLI SAVLARDVMS
LNVLLANGMS VEEINTTTKD GRTVLHLAAS IGSVELAQLL IWHNADAQIL DNNGRSCLFY
ARSNGFREVF DMLVTAGLSP DYGLPQEIND FSQMPEFFAM GSTSNRDYST SGDEMYGSRR
ISMGPPPQVP ARRYLPQQPE LDETSVI
