FGD6_MOUSE
ID FGD6_MOUSE Reviewed; 1399 AA.
AC Q69ZL1; Q8C8W5; Q8K3B0; Q9D3Y7;
DT 15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2005, sequence version 2.
DT 03-AUG-2022, entry version 146.
DE RecName: Full=FYVE, RhoGEF and PH domain-containing protein 6;
GN Name=Fgd6; Synonyms=Kiaa1362;
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 TISSUE=Pancreatic islet;
RX PubMed=15368895; DOI=10.1093/dnares/11.3.205;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA Saga Y., Seino S., Nishimura M., Kaisho T., Hoshino K., Kitamura H.,
RA Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: IV.
RT The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL DNA Res. 11:205-218(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 1-1156 (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Retina, and Testis;
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] OF 457-1399 (ISOFORM 1).
RC STRAIN=FVB/N; TISSUE=Mammary gland;
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 SER-583, 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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-583, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, and Testis;
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 [6]
RP STRUCTURE BY NMR OF 1303-1398.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of the pleckstrin homology domain of mouse ethanol
RT decreased 4 protein.";
RL Submitted (NOV-2004) to the PDB data bank.
CC -!- FUNCTION: May activate CDC42, a member of the Ras-like family of
CC Rho- and Rac proteins, by exchanging bound GDP for free GTP. May play a
CC role in regulating the actin cytoskeleton and cell shape (By
CC similarity). {ECO:0000250}.
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=Q69ZL1-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q69ZL1-2; Sequence=VSP_013093;
CC -!- SEQUENCE CAUTION:
CC Sequence=BAD32435.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AK173157; BAD32435.1; ALT_INIT; mRNA.
DR EMBL; AK016940; BAB30510.2; -; mRNA.
DR EMBL; AK044341; BAC31876.1; -; mRNA.
DR EMBL; BC026860; AAH26860.2; -; mRNA.
DR CCDS; CCDS48674.1; -. [Q69ZL1-1]
DR RefSeq; NP_444302.4; NM_053072.3. [Q69ZL1-1]
DR PDB; 1WGQ; NMR; -; A=1303-1398.
DR PDBsum; 1WGQ; -.
DR AlphaFoldDB; Q69ZL1; -.
DR SMR; Q69ZL1; -.
DR BioGRID; 199529; 3.
DR STRING; 10090.ENSMUSP00000020208; -.
DR iPTMnet; Q69ZL1; -.
DR PhosphoSitePlus; Q69ZL1; -.
DR EPD; Q69ZL1; -.
DR MaxQB; Q69ZL1; -.
DR PaxDb; Q69ZL1; -.
DR PeptideAtlas; Q69ZL1; -.
DR PRIDE; Q69ZL1; -.
DR ProteomicsDB; 271567; -. [Q69ZL1-1]
DR ProteomicsDB; 271568; -. [Q69ZL1-2]
DR Antibodypedia; 1926; 106 antibodies from 17 providers.
DR DNASU; 13998; -.
DR Ensembl; ENSMUST00000020208; ENSMUSP00000020208; ENSMUSG00000020021. [Q69ZL1-1]
DR GeneID; 13998; -.
DR KEGG; mmu:13998; -.
DR UCSC; uc011xlz.1; mouse. [Q69ZL1-1]
DR CTD; 55785; -.
DR MGI; MGI:1261419; Fgd6.
DR VEuPathDB; HostDB:ENSMUSG00000020021; -.
DR eggNOG; KOG1729; Eukaryota.
DR GeneTree; ENSGT00940000156334; -.
DR HOGENOM; CLU_004959_0_0_1; -.
DR InParanoid; Q69ZL1; -.
DR OMA; DEFQMSE; -.
DR OrthoDB; 652460at2759; -.
DR PhylomeDB; Q69ZL1; -.
DR TreeFam; TF343077; -.
DR BioGRID-ORCS; 13998; 0 hits in 71 CRISPR screens.
DR ChiTaRS; Fgd6; mouse.
DR EvolutionaryTrace; Q69ZL1; -.
DR PRO; PR:Q69ZL1; -.
DR Proteomes; UP000000589; Chromosome 10.
DR RNAct; Q69ZL1; protein.
DR Bgee; ENSMUSG00000020021; Expressed in animal zygote and 206 other tissues.
DR Genevisible; Q69ZL1; MM.
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:0043087; P:regulation of GTPase activity; IEA:InterPro.
DR CDD; cd15793; PH1_FGD6; 1.
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; IPR037743; FGD6_N_PH.
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 3D-structure; Alternative splicing; Cytoplasm; Cytoskeleton;
KW Guanine-nucleotide releasing factor; Metal-binding; Phosphoprotein;
KW Reference proteome; Repeat; Zinc; Zinc-finger.
FT CHAIN 1..1399
FT /note="FYVE, RhoGEF and PH domain-containing protein 6"
FT /id="PRO_0000080953"
FT DOMAIN 841..1030
FT /note="DH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00062"
FT DOMAIN 1059..1153
FT /note="PH 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT DOMAIN 1302..1398
FT /note="PH 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT ZN_FING 1191..1250
FT /note="FYVE-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT REGION 1..99
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 138..164
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 185..210
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 235..281
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 299..341
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 367..479
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 515..542
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 631..650
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 657..678
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 768..840
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 20..35
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 73..99
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 148..164
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 244..261
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 262..280
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 377..476
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 815..840
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 1197
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 1200
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 1213
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 1216
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 1221
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 1224
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 1242
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 1245
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT MOD_RES 494
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6ZV73"
FT MOD_RES 531
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6ZV73"
FT MOD_RES 583
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19144319,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 670
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6ZV73"
FT MOD_RES 697
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6ZV73"
FT MOD_RES 1167
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6ZV73"
FT VAR_SEQ 1..934
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_013093"
FT CONFLICT 126
FT /note="Q -> L (in Ref. 2; BAC31876)"
FT /evidence="ECO:0000305"
FT CONFLICT 262
FT /note="R -> H (in Ref. 2; BAC31876)"
FT /evidence="ECO:0000305"
FT CONFLICT 286
FT /note="V -> D (in Ref. 2; BAC31876)"
FT /evidence="ECO:0000305"
FT CONFLICT 347..348
FT /note="YC -> S (in Ref. 2; BAC31876)"
FT /evidence="ECO:0000305"
FT CONFLICT 368
FT /note="V -> A (in Ref. 2; BAC31876)"
FT /evidence="ECO:0000305"
FT CONFLICT 517
FT /note="Y -> H (in Ref. 2; BAC31876 and 3; AAH26860)"
FT /evidence="ECO:0000305"
FT CONFLICT 637
FT /note="A -> T (in Ref. 2; BAC31876 and 3; AAH26860)"
FT /evidence="ECO:0000305"
FT CONFLICT 791
FT /note="K -> Q (in Ref. 2; BAC31876 and 3; AAH26860)"
FT /evidence="ECO:0000305"
FT STRAND 1306..1314
FT /evidence="ECO:0007829|PDB:1WGQ"
FT STRAND 1320..1327
FT /evidence="ECO:0007829|PDB:1WGQ"
FT STRAND 1330..1335
FT /evidence="ECO:0007829|PDB:1WGQ"
FT STRAND 1343..1347
FT /evidence="ECO:0007829|PDB:1WGQ"
FT STRAND 1349..1355
FT /evidence="ECO:0007829|PDB:1WGQ"
FT STRAND 1362..1370
FT /evidence="ECO:0007829|PDB:1WGQ"
FT STRAND 1373..1379
FT /evidence="ECO:0007829|PDB:1WGQ"
FT HELIX 1383..1397
FT /evidence="ECO:0007829|PDB:1WGQ"
SQ SEQUENCE 1399 AA; 155169 MW; CB91142F176E5A2F CRC64;
MTSAAELKKP PLAPKPKLVG TNNKPPPPPI APKPDIGSAS VPRLTKKTKP AIAPKPKVPT
NSVVQDIKHP PSKKPTLNLE EREPELPEST GKSNCKDVRD PHSDYILPTC SCSSGCIHEP
RTRETQCVEQ LVLEPLGMKE NLENSKNGES SKRGSSWDSS SEKCRGQSGV VLKASILEEK
LKEVLTQQRS PCGSPGRHRA PKKPEMNGDH SCTRQIRIEF ADVSSSLTGF EKVPAHHNCH
PQLPRDESQT LKTCQDGSAE SRGHTDSCEP ENKRVASDGI SQKTEVKGLG PLEIHLLPYT
SKFPTPKPRK THAAARLRRQ KHVDTPGEST EEPGNSNNGS SCLLEDYCLK NNKVSVLRQN
ALYNQGPVDE VRPANQRALT GDSNSGGQDS VGSQKAVQQQ TPSLDTDSSL TSDSSGSGVS
PAVDKETTYT QCSTQPLSLP KQVTSACTDQ PPATCNPEVS APPIQKESSS SRIIPKKPQR
HSLPAAGVLK KAASEELVEK SSSGKETNVE KGLHRNYLHH PGPPNHGASA SPFDMPNPTS
EKPVWKLPHP ILPFSGSPEA LKRVTLSLNN EPSVSLTKPR AKSLSAVDAD RCNKPCKDPP
KKTSFKKLIN VKLSIGFIKS DFQKIRSKSC QHGDVSAGHP LAREPKGLES DWQGLATGEE
KRSKPTKAHS AENCSLESQK VKSWGQSSAV NGQRAESLDD RILSRHTSCT GDFGPEYENV
RHYEEIPEYE NLPFVMAGRN TPDLGWQNSS SVEDTDASLY EVEEPYNAPD GQLQLDPRHQ
PCSSGTSQEG KDALHLGLSD LPSDEEVINS SDEDDVSSES SKGEPDPLED KQDEDAGMKS
KVHHIAKEIM SSEKVFVDVL KLLHIDFRGA VAHASRQLGK PVIEDRILNQ ILYYLPQLYE
LNRDLLKELE ERMLTWTEQQ RIADIFVKKG PYLKMYSTYI KEFDKNVALL DEQCKKNPGF
AAVVREFEMS PRCANLALKH YLLKPVQRIP QYRLLLTDYL KNLLEDSVDH RDTQDALAVV
IEVANHANDT MKQGDNFQKL MQIQYSLSGH HEIVQPGRVF LKEGTLMKLS RKVMQPRMFF
LFNDALLYTT PMQSGMYKLN NMLSLAGMKV RKPTQEAYQN ELKIESVERS FILSASSAAE
RDDWLEAISS SIEEYAKKRI TFCPSRSLDE DSERKEEVSP LGAKAPIWIP DTRATMCMIC
TSEFTLTWRR HHCRACGKIV CQACSSNKYG LDYLKGQLAR VCEHCFQELQ KLDHQLSPRV
GSPGNHKSPS SALSSVLHSI PSGRKQKKIP AALKEVSANT EDSTMSGYLY RSKGSKKPWK
HLWFVIKNKV LYTYAASEDV AALESQPLLG FTVTLVKDEN SESKVFQLLH KGMVFYVFKA
DDAHSTQRWI DAFQEGTVL
