ID FGD2_HUMAN Reviewed; 655 AA. AC Q7Z6J4; Q5T8I1; Q6P6A8; Q6ZNL5; Q8IZ32; Q8N868; Q9H7M2; DT 15-MAR-2005, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2003, sequence version 1. DT 24-JUL-2024, entry version 177. DE RecName: Full=FYVE, RhoGEF and PH domain-containing protein 2; DE AltName: Full=Zinc finger FYVE domain-containing protein 4; GN Name=FGD2; Synonyms=ZFYVE4; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4). RC TISSUE=Spleen; RX PubMed=11214971; DOI=10.1093/dnares/7.6.357; RA Hattori A., Okumura K., Nagase T., Kikuno R., Hirosawa M., Ohara O.; RT "Characterization of long cDNA clones from human adult spleen."; RL DNA Res. 7:357-366(2000). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3). RC TISSUE=Spleen; RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., RA Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=14574404; DOI=10.1038/nature02055; RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., RA Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., RA Andrews T.D., Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., RA Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., RA Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., RA Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., RA Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., RA French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., RA Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., RA Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., RA Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., RA Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., RA Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., RA Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., RA Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., RA Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., RA Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., RA Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., RA Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., RA Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., RA Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., RA Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., RA West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., RA Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., RA Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., RA Rogers J., Beck S.; RT "The DNA sequence and analysis of human chromosome 6."; RL Nature 425:805-811(2003). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT HIS-32. RC TISSUE=Leukocyte, and Lymph; 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 [5] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-654, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014; RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., RA Ye M., Zou H.; RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver RT phosphoproteome."; RL J. Proteomics 96:253-262(2014). CC -!- FUNCTION: Activates CDC42, a member of the Ras-like family of Rho- and CC Rac proteins, by exchanging bound GDP for free GTP. Activates JNK1 via CC CDC42 but not RAC1. Binds to phosphatidylinositol 4,5-bisphosphate, CC phosphatidylinositol 3,4,5-trisphosphate, phosphatidylinositol 5- CC monophosphate, phosphatidylinositol 4-monophosphate and CC phosphatidylinositol 3-monophosphate (By similarity). {ECO:0000250}. CC -!- INTERACTION: CC Q7Z6J4; Q53G59: KLHL12; NbExp=3; IntAct=EBI-1057190, EBI-740929; CC Q7Z6J4; Q58EX7: PLEKHG4; NbExp=3; IntAct=EBI-1057190, EBI-949255; CC Q7Z6J4; Q9NS64: RPRM; NbExp=3; IntAct=EBI-1057190, EBI-1052363; CC Q7Z6J4; Q8WW34: TMEM239; NbExp=3; IntAct=EBI-1057190, EBI-9675724; CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000305}. Cytoplasm CC {ECO:0000250}. Nucleus {ECO:0000250}. Early endosome {ECO:0000250}. CC Early endosome membrane {ECO:0000250}. Cell projection, ruffle membrane CC {ECO:0000250}. Note=Recruitment to the endosome and ruffle membrane CC requires the presence of phosphoinositides. {ECO:0000250}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=4; CC Name=1; CC IsoId=Q7Z6J4-1; Sequence=Displayed; CC Name=2; CC IsoId=Q7Z6J4-2; Sequence=VSP_013065, VSP_013070, VSP_013072; CC Name=3; CC IsoId=Q7Z6J4-4; Sequence=VSP_013066, VSP_013071; CC Name=4; CC IsoId=Q7Z6J4-5; Sequence=VSP_013067, VSP_013068, VSP_038219; CC -!- DOMAIN: The FYVE-type zinc-finger is necessary for early endosome CC localization. Recruitment to endosomal membranes via this domain CC requires the presence of phosphatidylinositol 3-phosphate or other CC phosphatidylinositides (By similarity). {ECO:0000250}. CC -!- DOMAIN: The PH domain is necessary for localization to the ruffle CC membrane. Recruitment to ruffle membrane occurs through binding of CC phosphoinositides by the PH domain. This domain also contributes to the CC lipid-binding properties of the protein (By similarity). {ECO:0000250}. CC -!- DOMAIN: The DH domain is necessary for its ability to activate JNK1 via CC CDC42. {ECO:0000250}. CC -!- MISCELLANEOUS: [Isoform 4]: May be due to an intron retention. CC {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=BAB15746.1; Type=Erroneous initiation; Evidence={ECO:0000305}; CC Sequence=BAC85129.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305}; CC Sequence=BAC85129.1; Type=Frameshift; Evidence={ECO:0000305}; 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 EMBL; AK024456; BAB15746.1; ALT_INIT; mRNA. DR EMBL; AK097230; BAC04982.1; -; mRNA. DR EMBL; AK131079; BAC85129.1; ALT_SEQ; mRNA. DR EMBL; AL160264; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC023645; AAH23645.1; -; mRNA. DR EMBL; BC053655; AAH53655.1; -; mRNA. DR CCDS; CCDS4829.1; -. [Q7Z6J4-1] DR RefSeq; NP_775829.2; NM_173558.3. [Q7Z6J4-1] DR AlphaFoldDB; Q7Z6J4; -. DR SMR; Q7Z6J4; -. DR BioGRID; 128730; 23. DR IntAct; Q7Z6J4; 11. DR STRING; 9606.ENSP00000274963; -. DR iPTMnet; Q7Z6J4; -. DR PhosphoSitePlus; Q7Z6J4; -. DR BioMuta; FGD2; -. DR DMDM; 61213572; -. DR jPOST; Q7Z6J4; -. DR MassIVE; Q7Z6J4; -. DR PaxDb; 9606-ENSP00000274963; -. DR PeptideAtlas; Q7Z6J4; -. DR ProteomicsDB; 69421; -. [Q7Z6J4-1] DR ProteomicsDB; 69422; -. [Q7Z6J4-2] DR ProteomicsDB; 69423; -. [Q7Z6J4-4] DR ProteomicsDB; 69424; -. [Q7Z6J4-5] DR Antibodypedia; 29766; 74 antibodies from 17 providers. DR DNASU; 221472; -. DR Ensembl; ENST00000274963.13; ENSP00000274963.8; ENSG00000146192.15. [Q7Z6J4-1] DR GeneID; 221472; -. DR KEGG; hsa:221472; -. DR MANE-Select; ENST00000274963.13; ENSP00000274963.8; NM_173558.4; NP_775829.2. DR UCSC; uc010jwp.2; human. [Q7Z6J4-1] DR AGR; HGNC:3664; -. DR CTD; 221472; -. DR DisGeNET; 221472; -. DR GeneCards; FGD2; -. DR HGNC; HGNC:3664; FGD2. DR HPA; ENSG00000146192; Tissue enhanced (lymphoid). DR MIM; 605091; gene. DR neXtProt; NX_Q7Z6J4; -. DR OpenTargets; ENSG00000146192; -. DR PharmGKB; PA28103; -. DR VEuPathDB; HostDB:ENSG00000146192; -. DR eggNOG; KOG4424; Eukaryota. DR GeneTree; ENSGT00940000161251; -. DR HOGENOM; CLU_011755_2_1_1; -. DR InParanoid; Q7Z6J4; -. DR OMA; WTEKCPP; -. DR OrthoDB; 5385125at2759; -. DR PhylomeDB; Q7Z6J4; -. DR TreeFam; TF316247; -. DR PathwayCommons; Q7Z6J4; -. DR Reactome; R-HSA-193648; NRAGE signals death through JNK. DR Reactome; R-HSA-416482; G alpha (12/13) signalling events. DR Reactome; R-HSA-9013148; CDC42 GTPase cycle. DR SignaLink; Q7Z6J4; -. DR SIGNOR; Q7Z6J4; -. DR BioGRID-ORCS; 221472; 10 hits in 1146 CRISPR screens. DR ChiTaRS; FGD2; human. DR GeneWiki; FGD2; -. DR GenomeRNAi; 221472; -. DR Pharos; Q7Z6J4; Tdark. DR PRO; PR:Q7Z6J4; -. DR Proteomes; UP000005640; Chromosome 6. DR RNAct; Q7Z6J4; Protein. DR Bgee; ENSG00000146192; Expressed in monocyte and 179 other cell types or tissues. DR ExpressionAtlas; Q7Z6J4; baseline and differential. DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB. DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell. DR GO; GO:0005829; C:cytosol; TAS:Reactome. DR GO; GO:0031901; C:early endosome membrane; IEA:UniProtKB-SubCell. DR GO; GO:0005794; C:Golgi apparatus; ISS:UniProtKB. DR GO; GO:0030027; C:lamellipodium; ISS:UniProtKB. DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell. DR GO; GO:0001726; C:ruffle; ISS:UniProtKB. DR GO; GO:0032587; C:ruffle membrane; IEA:UniProtKB-SubCell. DR GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; ISS:UniProtKB. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:1901981; F:phosphatidylinositol phosphate binding; IEA:Ensembl. DR GO; GO:0031267; F:small GTPase binding; ISS:UniProtKB. DR GO; GO:0030036; P:actin cytoskeleton organization; ISS:UniProtKB. DR GO; GO:0007010; P:cytoskeleton organization; ISS:UniProtKB. DR GO; GO:0046847; P:filopodium assembly; ISS:UniProtKB. DR GO; GO:0008360; P:regulation of cell shape; ISS:UniProtKB. DR GO; GO:0043087; P:regulation of GTPase activity; ISS:UniProtKB. DR GO; GO:0051056; P:regulation of small GTPase mediated signal transduction; TAS:Reactome. DR CDD; cd15741; FYVE_FGD1_2_4; 1. DR CDD; cd13386; PH1_FGD2; 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; IPR037797; FGD2_PH1. DR InterPro; IPR051092; FYVE_RhoGEF_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; IPR011011; Znf_FYVE_PHD. DR InterPro; IPR013083; Znf_RING/FYVE/PHD. DR PANTHER; PTHR12673; FACIOGENITAL DYSPLASIA PROTEIN; 1. DR PANTHER; PTHR12673:SF82; FYVE, RHOGEF AND PH DOMAIN-CONTAINING PROTEIN 2; 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 Alternative splicing; Cell membrane; Cell projection; Cytoplasm; KW Cytoskeleton; Endosome; Guanine-nucleotide releasing factor; Membrane; KW Metal-binding; Nucleus; Phosphoprotein; Reference proteome; Repeat; Zinc; KW Zinc-finger. FT CHAIN 1..655 FT /note="FYVE, RhoGEF and PH domain-containing protein 2" FT /id="PRO_0000080942" FT DOMAIN 102..290 FT /note="DH" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00062" FT DOMAIN 319..418 FT /note="PH 1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00145" FT DOMAIN 544..641 FT /note="PH 2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00145" FT ZN_FING 458..518 FT /note="FYVE-type" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091" FT REGION 18..64 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 29..49 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT BINDING 464 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091" FT BINDING 467 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091" FT BINDING 481 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091" FT BINDING 484 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091" FT BINDING 489 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091" FT BINDING 492 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091" FT BINDING 510 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091" FT BINDING 513 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091" FT MOD_RES 11 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q8BY35" FT MOD_RES 48 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q8BY35" FT MOD_RES 654 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:24275569" FT VAR_SEQ 1..423 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_013065" FT VAR_SEQ 1..372 FT /note="Missing (in isoform 3)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_013066" FT VAR_SEQ 1..22 FT /note="MKGASEEKLASVSNLVTVFENS -> MFPKKARHPGAPALGICTRQPKSTPG FT TCCCFPCSPGRKPSGLSLLL (in isoform 4)" FT /evidence="ECO:0000303|PubMed:11214971" FT /id="VSP_013067" FT VAR_SEQ 101..104 FT /note="EPEK -> VPEG (in isoform 4)" FT /evidence="ECO:0000303|PubMed:11214971" FT /id="VSP_013068" FT VAR_SEQ 105..655 FT /note="Missing (in isoform 4)" FT /evidence="ECO:0000303|PubMed:11214971" FT /id="VSP_038219" FT VAR_SEQ 424..442 FT /note="NETFKAAAQGPEGDIQEQE -> MGGRRSPRAHSCPTPLNPQ (in FT isoform 2)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_013070" FT VAR_SEQ 488..655 FT /note="VCARCSDYRAELKYDDNRPNRVCLHCYAFLTGNVLPEAKEDKRRGILEKGSS FT ATPDQSLMCSFLQLIGDKWGKSGPRGWCVIPRDDPLVLYVYAAPQDMRAHTSIPLLGYQ FT VTVGPQGDPRVFQLQQSGQLYTFKAETEELKGRWVKAMERAASGWSPSWPNDGDLSD FT -> STPASTPASTCVTQASTCITQASTFPT (in isoform 3)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_013071" FT VAR_SEQ 585..655 FT /note="DMRAHTSIPLLGYQVTVGPQGDPRVFQLQQSGQLYTFKAETEELKGRWVKAM FT ERAASGWSPSWPNDGDLSD -> VRPPPARPPSGPGLPTACV (in isoform 2)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_013072" FT VARIANT 32 FT /note="Q -> H (in dbSNP:rs831510)" FT /evidence="ECO:0000269|PubMed:15489334" FT /id="VAR_021491" SQ SEQUENCE 655 AA; 74892 MW; DB60098249C2B340 CRC64; MKGASEEKLA SVSNLVTVFE NSRTPEAAPR GQRLEDVHHR PECRPPESPG PREKTNVGEA VGSEPRTVSR RYLNSLKNKL SSEAWRKSCQ PVTLSGSGTQ EPEKKIVQEL LETEQAYVAR LHLLDQVFFQ ELLKTARSSK AFPEDVVRVI FSNISSIYQF HSQFFLPELQ RRLDDWTANP RIGDVIQKLA PFLKMYSEYV KNFERAAELL ATWTDKSPLF QEVLTRIQSS EASGSLTLQH HMLEPVQRIP RYELLLKEYI QKLPAQAPDQ ADAQKALDMI FSAAQHSNAA ITEMERLQDL WEVYQRLGLE DDIVDPSNTL LREGPVLKIS FRRNDPMERY LFLFNNMLLY CVPRVIQVGA QFQVRTRIDV AGMKVRELMD AEFPHSFLVS GKQRTLELQA RSQEEMISWM QAFQAAIDQI EKRNETFKAA AQGPEGDIQE QELQSEELGL RAPQWVRDKM VTMCMRCQEP FNALTRRRHH CRACGYVVCA RCSDYRAELK YDDNRPNRVC LHCYAFLTGN VLPEAKEDKR RGILEKGSSA TPDQSLMCSF LQLIGDKWGK SGPRGWCVIP RDDPLVLYVY AAPQDMRAHT SIPLLGYQVT VGPQGDPRVF QLQQSGQLYT FKAETEELKG RWVKAMERAA SGWSPSWPND GDLSD //