ID   FGD3_MOUSE              Reviewed;         733 AA.
AC   O88842; A2RT26; Q8BQ72;
DT   15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1998, sequence version 1.
DT   08-NOV-2023, entry version 140.
DE   RecName: Full=FYVE, RhoGEF and PH domain-containing protein 3;
GN   Name=Fgd3;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, AND TISSUE SPECIFICITY.
RC   TISSUE=Spleen;
RX   PubMed=10721717; DOI=10.1016/s0378-1119(99)00518-1;
RA   Pasteris N.G., Nagata K., Hall A., Gorski J.L.;
RT   "Isolation, characterization, and mapping of the mouse Fgd3 gene, a new
RT   faciogenital dysplasia (FGD1; Aarskog syndrome) gene homologue.";
RL   Gene 242:237-247(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   STRAIN=C57BL/6J; TISSUE=Spinal ganglion;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA   Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA   Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA   Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA   Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA   Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA   Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA   Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA   Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA   Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA   Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA   Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA   Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA   Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA   Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA   Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA   Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA   Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA   Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA   Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA   van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA   Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA   Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA   Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA   Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA   Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA   Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA   Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA   Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-732, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA   Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA   Thibault P.;
RT   "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL   Immunity 30:143-154(2009).
RN   [5]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Spleen;
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL   Cell 143:1174-1189(2010).
CC   -!- FUNCTION: Promotes the formation of filopodia. May activate CDC42, a
CC       member of the Ras-like family of Rho- and Rac proteins, by exchanging
CC       bound GDP for free GTP. Plays a role in regulating the actin
CC       cytoskeleton and cell shape. {ECO:0000269|PubMed:10721717}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}. Cytoplasm, cytoskeleton
CC       {ECO:0000305}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=O88842-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=O88842-2; Sequence=VSP_013076, VSP_013077;
CC   -!- TISSUE SPECIFICITY: Detected in adult brain, spleen, lung and skeletal
CC       muscle. Detected in embryos from 7 dpc to 17 dpc.
CC       {ECO:0000269|PubMed:10721717}.
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DR   EMBL; AF017369; AAC35431.1; -; mRNA.
DR   EMBL; AK051395; BAC34624.1; -; mRNA.
DR   EMBL; BC132340; AAI32341.1; -; mRNA.
DR   EMBL; BC137954; AAI37955.1; -; mRNA.
DR   CCDS; CCDS26499.1; -. [O88842-1]
DR   AlphaFoldDB; O88842; -.
DR   SMR; O88842; -.
DR   STRING; 10090.ENSMUSP00000105714; -.
DR   iPTMnet; O88842; -.
DR   PhosphoSitePlus; O88842; -.
DR   EPD; O88842; -.
DR   jPOST; O88842; -.
DR   MaxQB; O88842; -.
DR   PaxDb; 10090-ENSMUSP00000105714; -.
DR   PeptideAtlas; O88842; -.
DR   ProteomicsDB; 271748; -. [O88842-1]
DR   ProteomicsDB; 271749; -. [O88842-2]
DR   Pumba; O88842; -.
DR   AGR; MGI:1353657; -.
DR   MGI; MGI:1353657; Fgd3.
DR   eggNOG; KOG4424; Eukaryota.
DR   InParanoid; O88842; -.
DR   PhylomeDB; O88842; -.
DR   Reactome; R-MMU-193648; NRAGE signals death through JNK.
DR   Reactome; R-MMU-416482; G alpha (12/13) signalling events.
DR   Reactome; R-MMU-9013148; CDC42 GTPase cycle.
DR   ChiTaRS; Fgd3; mouse.
DR   PRO; PR:O88842; -.
DR   Proteomes; UP000000589; Unplaced.
DR   RNAct; O88842; Protein.
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:UniProtKB-KW.
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; IDA:UniProtKB.
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; 1.
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   Alternative splicing; Cytoplasm; Cytoskeleton;
KW   Guanine-nucleotide releasing factor; Metal-binding; Phosphoprotein;
KW   Reference proteome; Repeat; Zinc; Zinc-finger.
FT   CHAIN           1..733
FT                   /note="FYVE, RhoGEF and PH domain-containing protein 3"
FT                   /id="PRO_0000080945"
FT   DOMAIN          153..337
FT                   /note="DH"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00062"
FT   DOMAIN          366..465
FT                   /note="PH 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT   DOMAIN          612..711
FT                   /note="PH 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT   ZN_FING         528..584
FT                   /note="FYVE-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT   REGION          1..134
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          481..535
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          586..612
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          712..733
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        72..92
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        486..506
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        520..535
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         534
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT   BINDING         537
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT   BINDING         551
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT   BINDING         554
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT   BINDING         559
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT   BINDING         562
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT   BINDING         576
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT   BINDING         579
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT   MOD_RES         124
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q5JSP0"
FT   MOD_RES         732
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:19144319"
FT   VAR_SEQ         516..532
FT                   /note="IESRKSSSKTRRDKEKP -> VSDPHPGISRSERCLGR (in isoform
FT                   2)"
FT                   /evidence="ECO:0000303|PubMed:16141072"
FT                   /id="VSP_013076"
FT   VAR_SEQ         533..733
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:16141072"
FT                   /id="VSP_013077"
FT   CONFLICT        7
FT                   /note="S -> P (in Ref. 2; BAC34624)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        126
FT                   /note="V -> M (in Ref. 2; BAC34624)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   733 AA;  80624 MW;  86CDFEBB5DC1E8E3 CRC64;
     MELGRSSSTP QEEAISPLGV LGTGPSSSPL GKLQALPIGP GAHRGAHSSS APAGDSSTRE
     PSGAMKIPNR DSGIDSPSSS VASENFPCEE SSEGSPSPAI LGLPSETASD SRVPQDNPQE
     EEDSGVGEEP DPKVTLFRPQ EDVSLTQCSD PQKLLHIAQE LLHTEEAYVK RLHLLDQVFC
     TKLTEAGIPL EVTTGIFSNI SSIYRFHGQF LLPELQKRIT EEWDTNPRLG DILQKLAPFL
     KMYGEYVKNF DRAMGLVSTW TQRSPQFKDV IHTIQKQEVC GNLTLQHHML EPVQRVPRYE
     LLLKDYLKRL PRDAPDRKDA ERSLELISTA ADHSNAAIRK MEKMHKLLEV YEQLGGEEDI
     VNPANELIKE GSIQKLSAKN GTTQDRHLFL FNNVMLYCVP KLRLMGQKLS VREKMDISDL
     QVQDIVKPNA ACTFIITGRK RSLELQTRTE EEKKEWIQVI QATVEKHKQK SETFRAFGGA
     CSQDEEPTLS PDQPVMSTSS VEPAGVADSN GGTPGIESRK SSSKTRRDKE KPGCKSCGET
     FNSITKRRYR CKLCGEVICR KCSEFKAENS KQSRVCRECF LEEPLVPPSP SSETPTELKQ
     NAEKPPSVDP RPSLLCGTLN LSDDGTTWNE VWAAIPESDP QVLDLLAGSQ AGRLLYSIPL
     SGCNITMPDP EEGLEAGCAW KLHQGSQTWW LSAPSTKLQQ CWLKALGTAV HGDTAGDRPG
     ASQPQAPAGT DTP
//