ID A0A2K5HRA8_COLAP Unreviewed; 926 AA.
AC A0A2K5HRA8;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 24-JAN-2024, entry version 28.
DE RecName: Full=FYVE, RhoGEF and PH domain containing 1 {ECO:0008006|Google:ProtNLM};
OS Colobus angolensis palliatus (Peters' Angolan colobus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Colobinae; Colobus.
OX NCBI_TaxID=336983 {ECO:0000313|Ensembl:ENSCANP00000006876.1, ECO:0000313|Proteomes:UP000233080};
RN [1] {ECO:0000313|Ensembl:ENSCANP00000006876.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000256|ARBA:ARBA00004245}.
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DR AlphaFoldDB; A0A2K5HRA8; -.
DR Ensembl; ENSCANT00000025846.1; ENSCANP00000006876.1; ENSCANG00000022364.1.
DR Proteomes; UP000233080; Unplaced.
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; cd15741; FYVE_FGD1_2_4; 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; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR12673; FACIOGENITAL DYSPLASIA PROTEIN; 1.
DR PANTHER; PTHR12673:SF79; FYVE, RHOGEF AND PH DOMAIN-CONTAINING PROTEIN 1; 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; SSF50729; PH domain-like; 2.
DR PROSITE; PS50010; DH_2; 1.
DR PROSITE; PS50003; PH_DOMAIN; 2.
DR PROSITE; PS50178; ZF_FYVE; 1.
PE 4: Predicted;
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Cytoskeleton {ECO:0000256|ARBA:ARBA00023212};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000233080};
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 350..538
FT /note="DH"
FT /evidence="ECO:0000259|PROSITE:PS50010"
FT DOMAIN 567..671
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT DOMAIN 695..755
FT /note="FYVE-type"
FT /evidence="ECO:0000259|PROSITE:PS50178"
FT DOMAIN 786..886
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT REGION 1..191
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 203..233
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 246..290
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 302..333
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 667..689
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 890..926
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 118..167
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 206..231
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 260..277
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 313..329
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 926 AA; 102834 MW; 72209208AADB0042 CRC64;
PSAAVAAAAS ARLLPPHPLS QGSFPPAAAE PQAEAGEDTG ARPSLGAAPG HRVLPCGPSP
QHHRALRFSY HLEGSQPRPG LHQGNRILVK SLSLDPGQSL EPHPEGPQRL RSDPGPPTET
PSQRPSPLKR APGPKPQVPP KPSYLQMPRM PPPLEPIPPP PSRPLPADPR VAKGLAPRAE
ASPSSAAVSS LIEKFEREPV IVASDRPAPG PSPGPPEPAM LPQPPSQPPV PQLLEGEASR
CLFLLAPGPR DGEKVPNRDS GIDSISSPSN SEETCFVSDD GPPSHSLCPG PAALASVPVA
LADPHRPGSQ EVDSDLEEED DEEEEEEKDR EIPVPPMERQ ESVELTVQQK VFHIANELLQ
TEKAYVSRLH LLDQVFCARL LEEARNRSSF PADVVHGIFS NICSIYCFHQ QFLLPELEKR
MEEWDRYPRI GDILQKLAPF LKMYGEYVKN FDRAVELVNT WTERSTQFKV IIHEVQKEEA
CGNLTLQHHM LEPVQRIPRY ELLLKDYLLK LPHGSPDSKD AQKSLELIAT AAEHSNAAIR
KMERMHKLLK VYELLGGEED IVSPTKELIK EGHILKLSAK NGTTQDRYLI LFNDRLLYCV
PRLRLLGQKF SVRARIDVDG MELKESSNLN LPRTFLVSGK QRSLELQAIN STLLKHEQTL
ETFKLLNSTN REDEDTPPNS PNVDLGKRAP TPIREKEVTM CMRCQEPFNS ITKRRHHCKA
CGHVVCGKCS EFRARLVYDN NRSNRVCTDC YVALHGVPGS SPACSQHTPQ RRRSILEKQA
SVAAENSVIC SFLHYMEKGG KGWHKAWFVV PENEPLVLYI YGAPQDVKAQ RSLPLIGFEV
GPPEAGERPD RRHVFKITQS HLSWYFSPET EELQRRWMAV LGRAGRGDTF CPGPTLSEDR
EMEEAPVATL GATAEPPESP QTRDKT
//