FGD5_HUMAN
ID FGD5_HUMAN Reviewed; 1462 AA.
AC Q6ZNL6; B3KVQ3; Q6MZY1; Q7Z303; Q8IYP3; Q8N861; Q8N8G4;
DT 15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 18-MAY-2010, sequence version 3.
DT 03-AUG-2022, entry version 161.
DE RecName: Full=FYVE, RhoGEF and PH domain-containing protein 5;
DE AltName: Full=Zinc finger FYVE domain-containing protein 23;
GN Name=FGD5; Synonyms=ZFYVE23;
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 2), AND NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 77-1462 (ISOFORM 1).
RC TISSUE=Spleen, and Testis;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16641997; DOI=10.1038/nature04728;
RA Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J.,
RA Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P.,
RA Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A.,
RA Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L.,
RA Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G.,
RA Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W.,
RA Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M.,
RA Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P.,
RA Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H.,
RA Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J.,
RA Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W.,
RA Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B.,
RA Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O.,
RA Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B.,
RA Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H.,
RA Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J.,
RA Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X.,
RA Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R.,
RA Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.;
RT "The DNA sequence, annotation and analysis of human chromosome 3.";
RL Nature 440:1194-1198(2006).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-215 (ISOFORM 1).
RC TISSUE=Placenta;
RX PubMed=10737800; DOI=10.1073/pnas.97.7.3491;
RA Dias Neto E., Correa R.G., Verjovski-Almeida S., Briones M.R.S.,
RA Nagai M.A., da Silva W. Jr., Zago M.A., Bordin S., Costa F.F.,
RA Goldman G.H., Carvalho A.F., Matsukuma A., Baia G.S., Simpson D.H.,
RA Brunstein A., de Oliveira P.S.L., Bucher P., Jongeneel C.V., O'Hare M.J.,
RA Soares F., Brentani R.R., Reis L.F.L., de Souza S.J., Simpson A.J.G.;
RT "Shotgun sequencing of the human transcriptome with ORF expressed sequence
RT tags.";
RL Proc. Natl. Acad. Sci. U.S.A. 97:3491-3496(2000).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 318-1462 (ISOFORM 1).
RC TISSUE=Esophageal carcinoma, and Uterus;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [6]
RP FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
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).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 889-1304.
RG Structural genomics consortium (SGC);
RT "Crystal structure of the DH and PH-1 domains of human FGD5.";
RL Submitted (JUN-2010) to the PDB data bank.
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. {ECO:0000269|PubMed:22328776}.
CC -!- INTERACTION:
CC Q6ZNL6; P55212: CASP6; NbExp=3; IntAct=EBI-7962481, EBI-718729;
CC Q6ZNL6; Q8NI60: COQ8A; NbExp=3; IntAct=EBI-7962481, EBI-745535;
CC Q6ZNL6; P13473-2: LAMP2; NbExp=3; IntAct=EBI-7962481, EBI-21591415;
CC Q6ZNL6; O75400-2: PRPF40A; NbExp=3; IntAct=EBI-7962481, EBI-5280197;
CC Q6ZNL6; P62826: RAN; NbExp=3; IntAct=EBI-7962481, EBI-286642;
CC Q6ZNL6; O43463: SUV39H1; NbExp=2; IntAct=EBI-7962481, EBI-349968;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000269|PubMed:22328776}. Cell projection, ruffle membrane
CC {ECO:0000269|PubMed:22328776}. Endoplasmic reticulum
CC {ECO:0000269|PubMed:22328776}. Golgi apparatus
CC {ECO:0000269|PubMed:22328776}. Early endosome
CC {ECO:0000269|PubMed:22328776}. Note=In peripheral membrane ruffles,
CC colocolizes with F-actin. In confluent HUVECs, detected at cell-cell-
CC contact sites where it colocalizes with vascular endothelial
CC cadherin/CDH5.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q6ZNL6-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q6ZNL6-2; Sequence=VSP_013088;
CC -!- TISSUE SPECIFICITY: Expressed in endothelial cells (at protein level).
CC {ECO:0000269|PubMed:22328776}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC04878.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAC04989.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAC85128.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=CAD98090.1; Type=Erroneous termination; Note=Truncated C-terminus.; Evidence={ECO:0000305};
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DR EMBL; AK096856; BAC04878.1; ALT_INIT; mRNA.
DR EMBL; AK097276; BAC04989.1; ALT_INIT; mRNA.
DR EMBL; AK131078; BAC85128.1; ALT_FRAME; mRNA.
DR EMBL; AK123054; BAG53865.1; -; mRNA.
DR EMBL; AC087591; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC090954; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC035364; AAH35364.1; -; mRNA.
DR EMBL; BF989107; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; BX640820; CAE45896.2; -; Transcribed_RNA.
DR EMBL; BX538312; CAD98090.1; ALT_SEQ; mRNA.
DR CCDS; CCDS46767.1; -. [Q6ZNL6-1]
DR RefSeq; NP_689749.3; NM_152536.3. [Q6ZNL6-1]
DR PDB; 3MPX; X-ray; 2.80 A; A=889-1304.
DR PDBsum; 3MPX; -.
DR AlphaFoldDB; Q6ZNL6; -.
DR SMR; Q6ZNL6; -.
DR BioGRID; 127439; 211.
DR IntAct; Q6ZNL6; 18.
DR MINT; Q6ZNL6; -.
DR STRING; 9606.ENSP00000285046; -.
DR iPTMnet; Q6ZNL6; -.
DR PhosphoSitePlus; Q6ZNL6; -.
DR BioMuta; FGD5; -.
DR DMDM; 296439343; -.
DR EPD; Q6ZNL6; -.
DR jPOST; Q6ZNL6; -.
DR MassIVE; Q6ZNL6; -.
DR PaxDb; Q6ZNL6; -.
DR PeptideAtlas; Q6ZNL6; -.
DR PRIDE; Q6ZNL6; -.
DR ProteomicsDB; 68034; -. [Q6ZNL6-1]
DR ProteomicsDB; 68035; -. [Q6ZNL6-2]
DR Antibodypedia; 5976; 121 antibodies from 20 providers.
DR DNASU; 152273; -.
DR Ensembl; ENST00000285046.10; ENSP00000285046.5; ENSG00000154783.12. [Q6ZNL6-1]
DR GeneID; 152273; -.
DR KEGG; hsa:152273; -.
DR MANE-Select; ENST00000285046.10; ENSP00000285046.5; NM_152536.4; NP_689749.3.
DR UCSC; uc003bzc.4; human. [Q6ZNL6-1]
DR CTD; 152273; -.
DR DisGeNET; 152273; -.
DR GeneCards; FGD5; -.
DR HGNC; HGNC:19117; FGD5.
DR HPA; ENSG00000154783; Low tissue specificity.
DR MIM; 614788; gene.
DR neXtProt; NX_Q6ZNL6; -.
DR OpenTargets; ENSG00000154783; -.
DR PharmGKB; PA134874843; -.
DR VEuPathDB; HostDB:ENSG00000154783; -.
DR eggNOG; KOG1729; Eukaryota.
DR eggNOG; KOG3531; Eukaryota.
DR GeneTree; ENSGT00940000157922; -.
DR InParanoid; Q6ZNL6; -.
DR OMA; GTADPEW; -.
DR OrthoDB; 652460at2759; -.
DR PhylomeDB; Q6ZNL6; -.
DR TreeFam; TF343077; -.
DR PathwayCommons; Q6ZNL6; -.
DR Reactome; R-HSA-9013149; RAC1 GTPase cycle.
DR SignaLink; Q6ZNL6; -.
DR SIGNOR; Q6ZNL6; -.
DR BioGRID-ORCS; 152273; 17 hits in 1066 CRISPR screens.
DR ChiTaRS; FGD5; human.
DR EvolutionaryTrace; Q6ZNL6; -.
DR GenomeRNAi; 152273; -.
DR Pharos; Q6ZNL6; Tbio.
DR PRO; PR:Q6ZNL6; -.
DR Proteomes; UP000005640; Chromosome 3.
DR RNAct; Q6ZNL6; protein.
DR Bgee; ENSG00000154783; Expressed in synovial joint and 153 other tissues.
DR ExpressionAtlas; Q6ZNL6; baseline and differential.
DR Genevisible; Q6ZNL6; 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:0005769; C:early endosome; IEA:UniProtKB-SubCell.
DR GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-SubCell.
DR GO; GO:0005794; C:Golgi apparatus; ISS:UniProtKB.
DR GO; GO:0030027; C:lamellipodium; ISS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IDA:HPA.
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: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; 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 3D-structure; Alternative splicing; Cell membrane; Cell projection;
KW Cytoplasm; Cytoskeleton; Endoplasmic reticulum; Endosome; Golgi apparatus;
KW Guanine-nucleotide releasing factor; Membrane; Metal-binding;
KW Reference proteome; Repeat; Zinc; Zinc-finger.
FT CHAIN 1..1462
FT /note="FYVE, RhoGEF and PH domain-containing protein 5"
FT /id="PRO_0000080950"
FT DOMAIN 892..1084
FT /note="DH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00062"
FT DOMAIN 1113..1207
FT /note="PH 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT DOMAIN 1363..1461
FT /note="PH 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT ZN_FING 1242..1301
FT /note="FYVE-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT REGION 37..323
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 492..512
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 592..613
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 670..718
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 746..777
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 851..887
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 44..83
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 158..175
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 208..224
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 293..321
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 671..688
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 696..717
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 860..886
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 1248
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 1251
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 1264
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 1267
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 1272
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 1275
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 1293
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 1296
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT VAR_SEQ 1..922
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_013088"
FT VARIANT 403
FT /note="G -> R (in dbSNP:rs7636593)"
FT /id="VAR_059799"
FT VARIANT 828
FT /note="A -> T (in dbSNP:rs17038795)"
FT /id="VAR_059800"
FT VARIANT 941
FT /note="E -> K (in dbSNP:rs2307092)"
FT /id="VAR_059801"
FT CONFLICT 124
FT /note="A -> T (in Ref. 1; BAC85128)"
FT /evidence="ECO:0000305"
FT CONFLICT 213
FT /note="A -> G (in Ref. 1; BAC85128)"
FT /evidence="ECO:0000305"
FT CONFLICT 354
FT /note="S -> G (in Ref. 5; CAE45896)"
FT /evidence="ECO:0000305"
FT CONFLICT 574
FT /note="H -> Y (in Ref. 1; BAC04989)"
FT /evidence="ECO:0000305"
FT CONFLICT 1112
FT /note="R -> M (in Ref. 5; CAE45896)"
FT /evidence="ECO:0000305"
FT CONFLICT 1196
FT /note="D -> N (in Ref. 5; CAE45896)"
FT /evidence="ECO:0000305"
FT CONFLICT 1289
FT /note="M -> T (in Ref. 5; CAE45896)"
FT /evidence="ECO:0000305"
FT CONFLICT 1382
FT /note="K -> E (in Ref. 1; BAC04989)"
FT /evidence="ECO:0000305"
FT CONFLICT 1400
FT /note="D -> G (in Ref. 5; CAD98090)"
FT /evidence="ECO:0000305"
FT HELIX 891..917
FT /evidence="ECO:0007829|PDB:3MPX"
FT HELIX 919..929
FT /evidence="ECO:0007829|PDB:3MPX"
FT HELIX 936..968
FT /evidence="ECO:0007829|PDB:3MPX"
FT TURN 969..972
FT /evidence="ECO:0007829|PDB:3MPX"
FT HELIX 978..981
FT /evidence="ECO:0007829|PDB:3MPX"
FT TURN 982..986
FT /evidence="ECO:0007829|PDB:3MPX"
FT HELIX 987..1008
FT /evidence="ECO:0007829|PDB:3MPX"
FT HELIX 1012..1022
FT /evidence="ECO:0007829|PDB:3MPX"
FT HELIX 1032..1054
FT /evidence="ECO:0007829|PDB:3MPX"
FT HELIX 1062..1084
FT /evidence="ECO:0007829|PDB:3MPX"
FT HELIX 1088..1100
FT /evidence="ECO:0007829|PDB:3MPX"
FT STRAND 1114..1116
FT /evidence="ECO:0007829|PDB:3MPX"
FT STRAND 1119..1124
FT /evidence="ECO:0007829|PDB:3MPX"
FT STRAND 1127..1145
FT /evidence="ECO:0007829|PDB:3MPX"
FT STRAND 1151..1158
FT /evidence="ECO:0007829|PDB:3MPX"
FT STRAND 1174..1179
FT /evidence="ECO:0007829|PDB:3MPX"
FT STRAND 1184..1188
FT /evidence="ECO:0007829|PDB:3MPX"
FT HELIX 1192..1204
FT /evidence="ECO:0007829|PDB:3MPX"
SQ SEQUENCE 1462 AA; 159891 MW; 3012049C00F7384B CRC64;
MFRGPKPPIA PKPRLTAPNE WRASVYLNDS LNKCSNGRLP CVDRGLDEGP RSIPKCSESE
TDEDYIVVPR VPLREDEPKD EGSVGNKALV SPESSAEEEE EREEGGEACG LEGTGAGEDS
VAPAAPGAGA LSREGEEGTD LALEDEGEGC ADEPGTLEQV SRSEEEEKLV QPHRECSLED
SGPWAGEGVF QSDLLLPHIH GEDQEPPDTP GEAEEDDEEG CASTDPAGAD EGSGPDRPTE
DMGQDAEDTS EEPPEKEELA GVQEAETATD CPEVLEEGCE EATGVTGGEQ VDLSEPPDHE
KKTNQEVAAA TLEDHAQDES AEESCQIVPF ENDCMEDFVT SLTGSPYEFF PTESTSFCSE
SCSPLSESAK GLESEQAPKL GLRAEENPMV GALCGQCGSL QGGAAEGPAA PDVVVVLEEE
ALDDALANPY VMGVGLPGQA APGEGGQAAS DALGGYGSKE ELNCEAEGGL VPADRKNTST
RVRPHSGKVA GYVPETVPEE TGPEAGSSAP GIGGAAEEVG KTLLSLEGKP LEASRALPAK
PRAFTLYPRS FSVEGREIPV SVYQEPEGSG LDDHRIKRKE DNLSLSCVIG SSGSFSQRNH
LPSSGTSTPS SMVDIPPPFD LACITKKPIT KSSPSLLIES DSPDKYKKKK SSFKRFLALT
FKKKTENKLH VDVNVSSSRS SSESSYHGPS RILEVDRRSL SNSPQLKSRT GKLRASESPS
SLIFYRDGKR KGVPFSRTVS RVESFEDRSR PPFLPLPLTK PRSISFPSAD TSDYENIPAM
NSDYENIQIP PRRPARAGAF TKLFEDQSRA LSTANENDGY VDMSSFNAFE SKQQSADQDA
ESAYTEPYKV CPISSAAPKE DLTSDEEQRS SEEEDSASRD PSVTHKVEGQ SRALVIAQEL
LSSEKAYVEM LQHLNLDFHG AVMRALDDMD HEGRDTLARE ELRQGLSELP AIHDLHQGIL
EELEERLSNW ESQQKVADVF LAREQGFDHH ATHILQFDRY LGLLSENCLH SPRLAAAVRE
FEQSVQGGSQ TAKHRLLRVV QRLFQYQVLL TDYLNNLCPD SAEYDNTQGA LSLISKVTDR
ANDSMEQGEN LQKLVHIEHS VRGQGDLLQP GREFLKEGTL MKVTGKNRRP RHLFLMNDVL
LYTYPQKDGK YRLKNTLAVA NMKVSRPVME KVPYALKIET SESCLMLSAS SCAERDEWYG
CLSRALPEDY KAQALAAFHH SVEIRERLGV SLGERPPTLV PVTHVMMCMN CGCDFSLTLR
RHHCHACGKI VCRNCSRNKY PLKYLKDRMA KVCDGCFGEL KKRGRAVPGL MRERPVSMSF
PLSSPRFSGS AFSSVFQSIN PSTFKKQKKV PSALTEVAAS GEGSAISGYL SRCKRGKRHW
KKLWFVIKGK VLYTYMASED KVALESMPLL GFTIAPEKEE GSSEVGPIFH LYHKKTLFYS
FKAEDTNSAQ RWIEAMEDAS VL
