ID V9KBJ0_CALMI Unreviewed; 758 AA.
AC V9KBJ0;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 03-MAY-2023, entry version 43.
DE SubName: Full=FYVE, RhoGEF and PH domain-containing protein 3 {ECO:0000313|EMBL:AFO95051.1};
OS Callorhinchus milii (Ghost shark).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Chondrichthyes;
OC Holocephali; Chimaeriformes; Callorhinchidae; Callorhinchus.
OX NCBI_TaxID=7868 {ECO:0000313|EMBL:AFO95051.1};
RN [1] {ECO:0000313|EMBL:AFO95051.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Spleen {ECO:0000313|EMBL:AFO95051.1};
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).
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000256|ARBA:ARBA00004245}.
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DR EMBL; JW862534; AFO95051.1; -; mRNA.
DR AlphaFoldDB; V9KBJ0; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR CDD; cd15740; FYVE_FGD3; 1.
DR CDD; cd13236; PH2_FGD1-4; 1.
DR CDD; cd00160; RhoGEF; 1.
DR Gene3D; 1.20.900.10; Dbl homology (DH) domain; 1.
DR Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 2.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR035899; DBL_dom_sf.
DR InterPro; IPR000219; DH-domain.
DR InterPro; IPR035941; FGD1-4_PH2.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR001849; PH_domain.
DR InterPro; IPR000306; Znf_FYVE.
DR InterPro; IPR017455; Znf_FYVE-rel.
DR InterPro; IPR011011; Znf_FYVE_PHD.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR12673; FACIOGENITAL DYSPLASIA PROTEIN; 1.
DR PANTHER; PTHR12673:SF14; FYVE, RHOGEF AND PH DOMAIN-CONTAINING PROTEIN 3; 1.
DR Pfam; PF01363; FYVE; 1.
DR Pfam; PF00169; PH; 2.
DR Pfam; PF00621; RhoGEF; 1.
DR SMART; SM00064; FYVE; 1.
DR SMART; SM00233; PH; 2.
DR SMART; SM00325; RhoGEF; 1.
DR SUPFAM; SSF48065; DBL homology domain (DH-domain); 1.
DR SUPFAM; SSF57903; FYVE/PHD zinc finger; 1.
DR SUPFAM; SSF50729; PH domain-like; 2.
DR PROSITE; PS50010; DH_2; 1.
DR PROSITE; PS50003; PH_DOMAIN; 2.
DR PROSITE; PS50178; ZF_FYVE; 1.
PE 2: Evidence at transcript level;
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Cytoskeleton {ECO:0000256|ARBA:ARBA00023212};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00091}.
FT DOMAIN 188..372
FT /note="DH"
FT /evidence="ECO:0000259|PROSITE:PS50010"
FT DOMAIN 401..500
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT DOMAIN 562..616
FT /note="FYVE-type"
FT /evidence="ECO:0000259|PROSITE:PS50178"
FT DOMAIN 650..751
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT REGION 1..181
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 515..561
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 623..643
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 43..57
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 58..72
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 91..105
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 118..153
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 532..553
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 758 AA; 84465 MW; 8779A655F55892CE CRC64;
MEPSAQGSSE CVPPDSEPEP EPSGSAEVPS GEEEAGASQA EVSMDVSEHS KSNLVTMKDL
PESERKESHC VSVSTDGETG NRAEDGESSL EQNGKIPNRD SGIDSPSCSG DGEGFPNEEG
VAEDKKGSRP STESETDMEA KPETQPKRDS TQEEDDSDMD DGSSEENEPP ELPKAEQPEA
TKCTEPQKLF NIANELLHTE EAYVKRLHLL DQVFCTKLNE AGIQHDVITG IFSNISSIYR
FHDQFLLPEI KMRITEEWDK NPRIGDILQK LAPFLKMYGE YVKNFDRAMD LVNSCTQRSS
QFKSVIQSIQ KQDVCGNLTL QHHMLEPVQR IPRYELLLKD YLKKLPGDSL DRKDAEKSLE
LISTAANHSN VAIRKMEKMH KLLEVYERLG GEADIVNPAN ELIKEGQIQK LSAKNGSAQD
RYLFVFNNMV LYCVPKLRLM GQKFSVRERI DIAGMQVQEI GKQSATHTFT ITGKQRSLEL
QARTEEEKKG WIQVIQGTIE KHKQNSETFN KAFNSSFSRD EENPPDSPGP GATCSGESTA
GGDFSSQSLM DSGKRASKVK RDKEKQSCKS CSETFNSITK RRHHCKQCNA VICGKCSEFK
PLADNSRHNR VCKECFGLPP LAPPTSGAEN TTDQKKKSTM ERPDSLISDN SVLCNHLSFM
EKGKTWSKAW VAIPKSDPLV LYLHIGSQTQ EGKNVRTIPL PGYEVHPVNA GDAMDKKHAF
KLSQSQQTFY FAAEDEELQR KWIDVASKAA KGEDSIEN
//
