FGD5_MOUSE
ID FGD5_MOUSE Reviewed; 1219 AA.
AC Q80UZ0; Q8BHM5;
DT 15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2005, sequence version 2.
DT 03-AUG-2022, entry version 129.
DE RecName: Full=FYVE, RhoGEF and PH domain-containing protein 5;
GN Name=Fgd5;
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 [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=C57BL/6J, and FVB/N; TISSUE=Brain, and Mammary tumor;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=C57BL/6J; TISSUE=Heart;
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 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-555, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brown adipose tissue, Heart, Kidney, Lung, and 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).
RN [5]
RP TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=22328776; DOI=10.1161/atvbaha.111.244004;
RA Kurogane Y., Miyata M., Kubo Y., Nagamatsu Y., Kundu R.K., Uemura A.,
RA Ishida T., Quertermous T., Hirata K., Rikitake Y.;
RT "FGD5 mediates proangiogenic action of vascular endothelial growth factor
RT in human vascular endothelial cells.";
RL Arterioscler. Thromb. Vasc. Biol. 32:988-996(2012).
CC -!- FUNCTION: Activates CDC42, a member of the Ras-like family of Rho- and
CC Rac proteins, by exchanging bound GDP for free GTP. Mediates VEGF-
CC induced CDC42 activation. May regulate proangiogenic action of VEGF in
CC vascular endothelial cells, including network formation, directional
CC movement and proliferation. May play a role in regulating the actin
CC cytoskeleton and cell shape (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000250}. Cell
CC projection, ruffle membrane {ECO:0000250}. Endoplasmic reticulum
CC {ECO:0000250}. Golgi apparatus {ECO:0000250}. Early endosome
CC {ECO:0000250}. Note=In peripheral membrane ruffles, colocolizes with F-
CC actin. {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q80UZ0-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q80UZ0-2; Sequence=VSP_013089;
CC -!- TISSUE SPECIFICITY: Expressed in highly vascularized tissues, such as
CC lung, kidney and ovary. {ECO:0000269|PubMed:22328776}.
CC -!- DEVELOPMENTAL STAGE: Detected at 10 dpc in the intersomitic vessels,
CC dorsal aorta and brain vasculature. In retina, strongly expressed in
CC the developing retinal vasculature at postnatal day 4 and down-
CC regulated in preformed vessels at postnatal day 8. Predominantly
CC detected in capillaries and veins, and particularly at the advancing
CC vascular fronts, as compared to arteries.
CC {ECO:0000269|PubMed:22328776}.
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DR EMBL; BC042732; AAH42732.1; -; mRNA.
DR EMBL; BC060664; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AK049341; BAC33694.1; -; mRNA.
DR EMBL; AK086031; BAC39597.1; -; mRNA.
DR RefSeq; NP_766319.3; NM_172731.3.
DR AlphaFoldDB; Q80UZ0; -.
DR SMR; Q80UZ0; -.
DR BioGRID; 231234; 1.
DR IntAct; Q80UZ0; 1.
DR STRING; 10090.ENSMUSP00000086748; -.
DR iPTMnet; Q80UZ0; -.
DR PhosphoSitePlus; Q80UZ0; -.
DR jPOST; Q80UZ0; -.
DR MaxQB; Q80UZ0; -.
DR PaxDb; Q80UZ0; -.
DR PRIDE; Q80UZ0; -.
DR ProteomicsDB; 271565; -. [Q80UZ0-1]
DR ProteomicsDB; 271566; -. [Q80UZ0-2]
DR DNASU; 232237; -.
DR GeneID; 232237; -.
DR KEGG; mmu:232237; -.
DR UCSC; uc009cyo.1; mouse. [Q80UZ0-2]
DR CTD; 152273; -.
DR MGI; MGI:2443369; Fgd5.
DR eggNOG; KOG1729; Eukaryota.
DR eggNOG; KOG3531; Eukaryota.
DR InParanoid; Q80UZ0; -.
DR OrthoDB; 652460at2759; -.
DR PhylomeDB; Q80UZ0; -.
DR Reactome; R-MMU-9013149; RAC1 GTPase cycle.
DR BioGRID-ORCS; 232237; 0 hits in 71 CRISPR screens.
DR ChiTaRS; Fgd5; mouse.
DR PRO; PR:Q80UZ0; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; Q80UZ0; protein.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0005769; C:early endosome; IEA:UniProtKB-SubCell.
DR GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-SubCell.
DR GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0032587; C:ruffle membrane; 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 CDD; cd00160; RhoGEF; 1.
DR Gene3D; 1.20.900.10; -; 1.
DR Gene3D; 2.30.29.30; -; 2.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR035899; DBL_dom_sf.
DR InterPro; IPR000219; DH-domain.
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 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; SSF48065; 1.
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; Cell membrane; Cell projection; Cytoplasm;
KW Cytoskeleton; Endoplasmic reticulum; Endosome; Golgi apparatus;
KW Guanine-nucleotide releasing factor; Membrane; Metal-binding;
KW Phosphoprotein; Reference proteome; Repeat; Zinc; Zinc-finger.
FT CHAIN 1..1219
FT /note="FYVE, RhoGEF and PH domain-containing protein 5"
FT /id="PRO_0000080951"
FT DOMAIN 647..840
FT /note="DH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00062"
FT DOMAIN 869..963
FT /note="PH 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT DOMAIN 1120..1218
FT /note="PH 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT ZN_FING 998..1057
FT /note="FYVE-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT REGION 1..85
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 94..113
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 201..227
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 310..367
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 586..644
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..16
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 20..46
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 95..113
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 201..218
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 323..337
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 342..367
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 1004
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 1007
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 1020
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 1023
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 1028
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 1031
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 1049
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 1052
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT MOD_RES 555
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT VAR_SEQ 1..1001
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_013089"
SQ SEQUENCE 1219 AA; 134719 MW; 35F0AF51DD0911B4 CRC64;
MGSPESEVSP DVQEQEAATD NPEVFEEDSA DAAEGEDQIE QEEPPNCDEE AYNRDAAAAT
MQVGEDLGEE GDHVQEDPAE ESCQIIPFES DSVEEDFSPT LTENPYEIFP TESTSFCNNT
YSLDESANGH EPVCEICVEE VPGVGPPLNQ HDSLPDGSGE DSPVVPDVVV VPENEGPVDD
ALSSPYVMGV GLLSLGEGAQ SDTQAASGTL SGYSTWEEGD SEGGQVPVDR KNIATRARPH
SGKVAGHVPE TVLEETGPET CSSGMGIRDT SDEVRKIGIL PEGKPPECVR ALPAKPRAFT
LYPRSFSVEG RESPLSMFRE PEGAGLDSHR VRRKEDNLSL PGAIGSSGSF SQRSHLPSSG
TSTPSSVVDI PPPFDLACIT KKPITKSSPS LLIDGDTLEK ASKKKKSSFK RFLELTFRKK
TESKVHVDMN LSSSRSSSES SYHGPARVLE LDRRSLSNSP QLKCRTGKLR ASDSPAALIF
YRDSKRKGVP FSRTVSRVES FEDRSRPPFL PLPLTKPRSI SFPNADTSDY ENIPAMNSDY
ENIQIPPRRP VRTGTFTKLF EEQSRALSTA NENDGYVDMS SFNAFESKQQ SSEQEAESAY
TEPYKVCPIS AAPREDLTSD EEQGSSEEED SASRDPSLSH KGEGQSRALV IAQELLSSEK
AYVQMLQHLS LDFHGAVLRA LENVEQEGRE PLAQEELRQG LRELPAICDL HQGILESLEQ
RLGDCGEGQP QVADIFLARE QEFEHHAAHI LQFDRYLGLL AESCLLSPRL ATTVREFEQS
SQGGGQSMKH RMLRVVQRLF QYQVLLTDYL NNLCPDSAEY DNTQSALTLI SKVTDRANES
MEQGENLQKL VHIEYSVRGQ GDLLQPGREF LKEGTLMRVR GKSRHPRHLF LMNDTLLYTH
PQKDGKYRLK SSLPVANMKV SRPVMDKVPY ALKIETPESC LTLSASSCAE RDEWHYCLSR
ALPEDYKTQA LAAFHHSVEI RERLGISLGE RLPTLVPVTH AMMCMNCGCD FSLTVRRHHC
HACGKIVCRN CSRNKYPLKC LKNRMAKVCD GCFRELKLRN GPVPGSMRER PVSMSFPLSS
SRFSSGSALS SVFQSISPST FKKQKKVPSA LSEVAASGEG SAISGYLSRC KSGKRRWKKL
WLVIKGKVLY TYLASEDKVA MESIPLLGFT IAPEKEEGSS EVGPVFHLYH KKTLFYSFKA
EDSNSAQRWM EAMEDASVL
