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Database: UniProt
Entry: I3L837_PIG
LinkDB: I3L837_PIG
Original site: I3L837_PIG 
ID   I3L837_PIG              Unreviewed;       735 AA.
AC   I3L837;
DT   11-JUL-2012, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 2.
DT   24-JAN-2024, entry version 85.
DE   SubName: Full=FYVE, RhoGEF and PH domain containing 3 {ECO:0000313|Ensembl:ENSSSCP00000020195.2};
DE   SubName: Full=FYVE, RhoGEF and PH domain-containing protein 3 {ECO:0000313|EMBL:HDC41167.1, ECO:0000313|EMBL:HDC43690.1};
GN   Name=FGD3 {ECO:0000313|Ensembl:ENSSSCP00000020195.2,
GN   ECO:0000313|VGNC:VGNC:88096};
OS   Sus scrofa (Pig).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX   NCBI_TaxID=9823 {ECO:0000313|Ensembl:ENSSSCP00000020195.2, ECO:0000313|Proteomes:UP000008227};
RN   [1] {ECO:0000313|Ensembl:ENSSSCP00000020195.2, ECO:0000313|Proteomes:UP000008227}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Duroc {ECO:0000313|Ensembl:ENSSSCP00000020195.2,
RC   ECO:0000313|Proteomes:UP000008227};
RG   Porcine genome sequencing project;
RL   Submitted (NOV-2009) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:HDC41167.1}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=30723633; DOI=.7717/peerj.6374;
RA   Gilbert D.G.;
RT   "Genes of the pig, Sus scrofa, reconstructed with EvidentialGene.";
RL   PeerJ 7:E6374-E6374(2019).
RN   [3] {ECO:0000313|Ensembl:ENSSSCP00000020195.2}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (JUL-2023) to UniProtKB.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC       {ECO:0000256|ARBA:ARBA00004245}.
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DR   EMBL; DQIR01285689; HDC41167.1; -; Transcribed_RNA.
DR   EMBL; DQIR01288212; HDC43690.1; -; Transcribed_RNA.
DR   STRING; 9823.ENSSSCP00000020195; -.
DR   PaxDb; 9823-ENSSSCP00000020195; -.
DR   Ensembl; ENSSSCT00000031246.3; ENSSSCP00000020195.2; ENSSSCG00000028185.4.
DR   VGNC; VGNC:88096; FGD3.
DR   eggNOG; KOG4424; Eukaryota.
DR   GeneTree; ENSGT00940000159597; -.
DR   HOGENOM; CLU_011755_1_1_1; -.
DR   OMA; RITGEWE; -.
DR   OrthoDB; 5385125at2759; -.
DR   TreeFam; TF316247; -.
DR   Reactome; R-SSC-193648; NRAGE signals death through JNK.
DR   Reactome; R-SSC-416482; G alpha (12/13) signalling events.
DR   Reactome; R-SSC-9013148; CDC42 GTPase cycle.
DR   Proteomes; UP000008227; Chromosome 3.
DR   Bgee; ENSSSCG00000028185; Expressed in blood and 40 other cell types or tissues.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
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   GO; GO:0007010; P:cytoskeleton organization; IBA:GO_Central.
DR   GO; GO:0046847; P:filopodium assembly; IBA:GO_Central.
DR   CDD; cd15740; FYVE_FGD3; 1.
DR   CDD; cd13387; PH1_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   1: Evidence at protein level;
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW   Cytoskeleton {ECO:0000256|ARBA:ARBA00023212};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Proteomics identification {ECO:0007829|PeptideAtlas:I3L837};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008227};
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          167..351
FT                   /note="DH"
FT                   /evidence="ECO:0000259|PROSITE:PS50010"
FT   DOMAIN          380..479
FT                   /note="PH"
FT                   /evidence="ECO:0000259|PROSITE:PS50003"
FT   DOMAIN          542..598
FT                   /note="FYVE-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50178"
FT   DOMAIN          626..727
FT                   /note="PH"
FT                   /evidence="ECO:0000259|PROSITE:PS50003"
FT   REGION          1..163
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          518..548
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          601..623
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        56..95
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        145..163
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        534..548
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   735 AA;  80249 MW;  6C9DA719DFD636E5 CRC64;
     MEPGGGSSMP PAPIAALGEP DAGPSSSSLE LPSTDPGKLQ ALPVGPGVHC GDPASGSPDS
     QVSVGDSPQD MGSIGEPSSS TKIPNRDSGI DSPSCSVVSE HFPCEEGSEA APGPTIKGLH
     PETASEGTTP REEADSDVGE GSSEEPEAEN SRPRADADPA KCSKPQKLLH IAQELLHTEE
     TYVKRLHLLD QVFCTQLTEA GIPSEVTTGI FSNISSIYRF HGQFLLPELQ TRITTEWDTN
     PRLGDILQKL APFLKMYGEY VKNFDRAVEL VSTWTQRSPL FKDIVQGIQK QEMCGNLTLQ
     HHMLEPVQRV PRYELLLKDY LKRLPEDAPD WKDAERSLEL ISTAANHSNA AIRKMEKMHK
     LLEVYERLGG EEDIVNPANE LIKEGHIQKL SAKNGTAQDR HLFLFNSMIL YCVPKLRLMG
     QKFSVREKMD ISGLQVQDSI KPNSAHTFII TGKKRSLELQ TRTEEEKKEW IQVIEATIEK
     HKQNSQTFKA FSGSFGQDED SSFTADPPMV NTSSEVPAVV ASGGGGAAGL EPRRASSRTR
     RDKEKQGCRS CGETFNSITK RKHHCKLCGA VICGKCSEFK AENGRQSRVC RECFLTQPAA
     PLNPSPDVPL EPKQSTEKPA AVDHPPSLLC GPLQVSDGST AWSKVWAAIP ESGPPELVLR
     LHGGSQDGQL LCAIPLSGCR VSVPDPADRL DARHMWRLQQ GQQCWCLSAP SVELQQQWLE
     ALSMAARRPP ALAAP
//
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