ID A0A2D0R3V1_ICTPU Unreviewed; 996 AA.
AC A0A2D0R3V1;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE SubName: Full=FYVE, RhoGEF and PH domain-containing protein 1 isoform X1 {ECO:0000313|RefSeq:XP_017324485.1};
GN Name=fgd1 {ECO:0000313|RefSeq:XP_017324485.1};
OS Ictalurus punctatus (Channel catfish) (Silurus punctatus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Siluriformes;
OC Ictaluridae; Ictalurus.
OX NCBI_TaxID=7998 {ECO:0000313|RefSeq:XP_017324485.1};
RN [1] {ECO:0000313|RefSeq:XP_017324485.1}
RP IDENTIFICATION.
RC TISSUE=Blood {ECO:0000313|RefSeq:XP_017324485.1};
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000256|ARBA:ARBA00004245}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR RefSeq; XP_017324485.1; XM_017468996.3.
DR AlphaFoldDB; A0A2D0R3V1; -.
DR STRING; 7998.ENSIPUP00000019128; -.
DR Ensembl; ENSIPUT00000019944; ENSIPUP00000019128; ENSIPUG00000012986.
DR GeneID; 108266043; -.
DR KEGG; ipu:108266043; -.
DR CTD; 2245; -.
DR OMA; QQRWMAV; -.
DR OrthoDB; 5385125at2759; -.
DR Proteomes; UP000221080; Chromosome 5.
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; cd01219; PH1_FGD1; 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; IPR035939; FGD1_PH1.
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: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; 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 4: Predicted;
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 419..607
FT /note="DH"
FT /evidence="ECO:0000259|PROSITE:PS50010"
FT DOMAIN 636..735
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT DOMAIN 777..837
FT /note="FYVE-type"
FT /evidence="ECO:0000259|PROSITE:PS50178"
FT DOMAIN 867..968
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT REGION 1..175
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 204..333
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 376..411
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 974..996
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 11..27
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 28..65
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 105..128
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 141..157
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 240..265
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 306..333
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 996 AA; 111215 MW; 1604D9503BDB6678 CRC64;
MQLNRPRSAL IGFSPPPPSP PAPPSDPNST FSSQFKAMRF SYHLSPQPGS RRTGPSASSP
RLLTKSLSLE PGPCPGAHEA PQRLCSDPGP LGLQHCNGTS ENEPQNAPPL PPKTRPPLPG
PKPLVPPKPA HLQQQGGRRP RPPDKPLPPP PSRPLPADPR QSRTGLPRAE GSSSPTCVLS
LIERFEREQI IMVPDITGGV MCMPRVPDPQ PATDAILPCA SLNEPTEPPS VKKELEKGSE
EEEEKEEEVK EEGEVQEDLE EDDNELGASC SEKRLSTESG YGASDKLLDA MEIRDLGHSE
IPPDRLSLPP QQTDTKLANR DSGIDSISSP SHSEELCFAG DDREVCMSLP RLSSSSSCGC
VEGPAGEGVV AAVEEGARDS EGDSDLEEGS GDESENAMAI QPQPKAERQD SVELSVQQRV
FNIANELLHT EKAYVSRLHL LDQVFCRRLM EEARARGSFP CEVVMGIFSN ICSIYCFHQQ
FLLPALEKRM EEWDVNPRIG DILQKLAPFL KMYGEYVKNF DTAMELVNTW MERSSQFKAI
VHDIQKEEMC GNLTLQHHML EPVQRIPRYE LLLKDYLHRL PEDAEDFKDA QKSLELIATA
AEHSNAAIRK MERMRKLLKA YELLGGEEDI VNPTNELIKE GHILKLSAKN GTSQDRYLIL
FNDRLLYCVP KLRLIGQKFG VRARIDVDGM ELKETSSMNV PRTFLVSGKQ RSLELQARTE
EEKKDWIQAI QATIQRHEQS VETFRMLNCS VREDDCTPPN SPNCTELGKR APTPIREKEV
TLCMKCQEPF NSITKRRHHC KACGHVVCGK CSEFRARLLY DNNRANRVCI DCYTTLVGVP
PSPASLTNIT HRRRSILEKQ ASVAAENSVL CSFLHHMEKG SGRGWQKAWF VVPENEPLVL
YIYGAPQDVK AQRSIPLIGF EVSLPESCDR LERRYAFKMS QSHLTVYFSA DGEELQRRWM
EVLSRAGRGE ELQVHGPISE ALEEEAEEPS PLGEST
//
