ID V9KKN2_CALMI Unreviewed; 664 AA.
AC V9KKN2;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 24-JAN-2024, entry version 24.
DE SubName: Full=Rho GTPase-activating protein 17 {ECO:0000313|EMBL:AFO98560.1};
DE Flags: Fragment;
OS Callorhinchus milii (Ghost shark).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Chondrichthyes;
OC Holocephali; Chimaeriformes; Callorhinchidae; Callorhinchus.
OX NCBI_TaxID=7868 {ECO:0000313|EMBL:AFO98560.1};
RN [1] {ECO:0000313|EMBL:AFO98560.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Gills {ECO:0000313|EMBL:AFO98560.1};
RX PubMed=24402279; DOI=10.1038/nature12826;
RG International Elephant Shark Genome Sequencing Consortium;
RA Venkatesh B., Lee A.P., Ravi V., Maurya A.K., Lian M.M., Swann J.B.,
RA Ohta Y., Flajnik M.F., Sutoh Y., Kasahara M., Hoon S., Gangu V., Roy S.W.,
RA Irimia M., Korzh V., Kondrychyn I., Lim Z.W., Tay B.H., Tohari S.,
RA Kong K.W., Ho S., Lorente-Galdos B., Quilez J., Marques-Bonet T.,
RA Raney B.J., Ingham P.W., Tay A., Hillier L.W., Minx P., Boehm T.,
RA Wilson R.K., Brenner S., Warren W.C.;
RT "Elephant shark genome provides unique insights into gnathostome
RT evolution.";
RL Nature 505:174-179(2014).
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DR EMBL; JW866043; AFO98560.1; -; mRNA.
DR AlphaFoldDB; V9KKN2; -.
DR GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR GO; GO:0005096; F:GTPase activator activity; IEA:InterPro.
DR GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR CDD; cd04386; RhoGAP_nadrin; 1.
DR Gene3D; 1.20.1270.60; Arfaptin homology (AH) domain/BAR domain; 1.
DR Gene3D; 1.10.555.10; Rho GTPase activation protein; 1.
DR InterPro; IPR027267; AH/BAR_dom_sf.
DR InterPro; IPR004148; BAR_dom.
DR InterPro; IPR047165; RHG17/44/SH3BP1-like.
DR InterPro; IPR008936; Rho_GTPase_activation_prot.
DR InterPro; IPR000198; RhoGAP_dom.
DR PANTHER; PTHR14130; 3BP-1 RELATED RHOGAP; 1.
DR PANTHER; PTHR14130:SF3; RHO GTPASE-ACTIVATING PROTEIN 17; 1.
DR Pfam; PF03114; BAR; 1.
DR Pfam; PF00620; RhoGAP; 1.
DR SMART; SM00721; BAR; 1.
DR SMART; SM00324; RhoGAP; 1.
DR SUPFAM; SSF103657; BAR/IMD domain-like; 1.
DR SUPFAM; SSF48350; GTPase activation domain, GAP; 1.
DR PROSITE; PS51021; BAR; 1.
DR PROSITE; PS50238; RHOGAP; 1.
PE 2: Evidence at transcript level;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553}.
FT DOMAIN 14..249
FT /note="BAR"
FT /evidence="ECO:0000259|PROSITE:PS51021"
FT DOMAIN 255..445
FT /note="Rho-GAP"
FT /evidence="ECO:0000259|PROSITE:PS50238"
FT REGION 468..664
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 169..196
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 471..497
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 548..563
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 565..597
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 644..664
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 664
FT /evidence="ECO:0000313|EMBL:AFO98560.1"
SQ SEQUENCE 664 AA; 72437 MW; D3A97BD0940630DA CRC64;
MKKQFNRMKQ LASQTVGRAE KTEVLSDDLL QIEKRIDTIR VVSHNTHKRL LTCLQVPQGT
EVEKRHKKIP LMGLSQCMQE GFTSMGDDSL IGKLLEICSE AESKLAWELA QHEVQIEKDV
LDPFSSLVEV DIPNIQKQRK QLARLVLDWD SAKIRHYQMQ KTSFSGANIQ AVAAKVDSLR
EEMEEAGNKV EQCKDQLASD MYNFTSKEGD YANYYVTLLE AQADYHRKSL AVLERVLPTI
HTQQETWTEK PAFGTALEEH LQRSGREIAL PLEACVMMLL ETGMKEEGLF RIAAGASKLK
KLKAALDCST SQLEEFYSDP HAVAGALKSY LRELPEPLMT YQLYEEWIHA AGLSDPERKL
QALWTVCNKL PQPNHTNLSY LIKFLAKLAQ NRDINKMTPT NIAIVLGPNL LWAKSEGTMS
DMTAATSVQA VTVIEPILHH ADWFFPDEID FNKSGMFSPM APASLNSECE SGTLERKRPV
SLPAAEDPGK KDGSAKSKDA GSTPPLVRNA SAGLGMGTGH GQLGAPPSTG TGPSPHVTRR
ATKKPAPAPP KTSNPPPGQP AGQGANPQPG GQSGGLSPGQ PVVQPRRHSS NQTSIHAPSH
PPPQPPAQGR EQGSHSPPGT PTSPGIPTIG AHSSGYQFVQ DPPAHPSLPS PTGSLQRPRP
TPKP
//
