FGD2_HUMAN
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 03-AUG-2022, entry version 167.
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};
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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 EPD; Q7Z6J4; -.
DR jPOST; Q7Z6J4; -.
DR MassIVE; Q7Z6J4; -.
DR MaxQB; Q7Z6J4; -.
DR PaxDb; Q7Z6J4; -.
DR PeptideAtlas; Q7Z6J4; -.
DR PRIDE; Q7Z6J4; -.
DR ProteomicsDB; 69421; -. [Q7Z6J4-1]
DR ProteomicsDB; 69422; -. [Q7Z6J4-2]
DR ProteomicsDB; 69423; -. [Q7Z6J4-4]
DR ProteomicsDB; 69424; -. [Q7Z6J4-5]
DR Antibodypedia; 29766; 66 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 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; IMNSERS; -.
DR OrthoDB; 652460at2759; -.
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 1068 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 178 other tissues.
DR ExpressionAtlas; Q7Z6J4; baseline and differential.
DR Genevisible; Q7Z6J4; HS.
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:0043507; P:positive regulation of JUN kinase activity; IEA:Ensembl.
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; cd13386; PH1_FGD2; 1.
DR CDD; cd13236; PH2_FGD1-4; 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; IPR035941; FGD1-4_PH2.
DR InterPro; IPR037797; FGD2_PH1.
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 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 SUPFAM; SSF57903; SSF57903; 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; 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
