ES8L1_HUMAN
ID ES8L1_HUMAN Reviewed; 723 AA.
AC Q8TE68; Q71RE2; Q8NC10; Q96BB7; Q9BSQ2; Q9GZQ2; Q9NXH0;
DT 30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 18-MAY-2010, sequence version 3.
DT 03-AUG-2022, entry version 157.
DE RecName: Full=Epidermal growth factor receptor kinase substrate 8-like protein 1;
DE Short=EPS8-like protein 1;
DE AltName: Full=Epidermal growth factor receptor pathway substrate 8-related protein 1;
DE Short=EPS8-related protein 1;
GN Name=EPS8L1; Synonyms=DRC3, EPS8R1; ORFNames=PP10566;
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 [GENOMIC DNA / MRNA] (ISOFORM 4).
RX PubMed=10514543;
RA Wu K., Xu Z., Wang M., Xu X., Han Y., Cao Y., Wang R., Sun Y., Wu M.;
RT "Cloning and expression analyses of down-regulated cDNA C6-2A in human
RT esophageal cancer.";
RL Zhonghua Yi Xue Yi Chuan Xue Za Zhi 16:325-327(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANTS THR-4; GLU-457 AND
RP ARG-669.
RX PubMed=12620401; DOI=10.1016/s0888-7543(03)00002-8;
RA Tocchetti A., Confalonieri S., Scita G., Di Fiore P.P., Betsholtz C.;
RT "In silico analysis of the EPS8 gene family: genomic organization,
RT expression profile, and protein structure.";
RL Genomics 81:234-244(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANTS THR-4;
RP GLU-457 AND ARG-669.
RX PubMed=15498874; DOI=10.1073/pnas.0404089101;
RA Wan D., Gong Y., Qin W., Zhang P., Li J., Wei L., Zhou X., Li H., Qiu X.,
RA Zhong F., He L., Yu J., Yao G., Jiang H., Qian L., Yu Y., Shu H., Chen X.,
RA Xu H., Guo M., Pan Z., Chen Y., Ge C., Yang S., Gu J.;
RT "Large-scale cDNA transfection screening for genes related to cancer
RT development and progression.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:15724-15729(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2), AND VARIANT
RP ARG-669.
RC TISSUE=Placenta;
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15057824; DOI=10.1038/nature02399;
RA Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E.,
RA Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A.,
RA Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S.,
RA Carrano A.V., Caoile C., Chan Y.M., Christensen M., Cleland C.A.,
RA Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J.,
RA Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M.,
RA Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W.,
RA Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V.,
RA Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D.,
RA McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I.,
RA Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L.,
RA Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A.,
RA She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M.,
RA Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J.,
RA Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E.,
RA Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M.,
RA Rubin E.M., Lucas S.M.;
RT "The DNA sequence and biology of human chromosome 19.";
RL Nature 428:529-535(2004).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3).
RC TISSUE=Muscle, and Skin;
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 [7]
RP FUNCTION, IDENTIFICATION IN A COMPLEX WITH ABI1 AND SOS1, INTERACTION WITH
RP ABI1, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=14565974; DOI=10.1091/mbc.e03-06-0427;
RA Offenhaeuser N., Borgonovo A., Disanza A., Romano P., Ponzanelli I.,
RA Iannolo G., Di Fiore P.P., Scita G.;
RT "The eps8 family of proteins links growth factor stimulation to actin
RT reorganization generating functional redundancy in the Ras/Rac pathway.";
RL Mol. Biol. Cell 15:91-98(2004).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-182, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
CC -!- FUNCTION: Stimulates guanine exchange activity of SOS1. May play a role
CC in membrane ruffling and remodeling of the actin cytoskeleton.
CC {ECO:0000269|PubMed:14565974}.
CC -!- SUBUNIT: Interacts with ABI1. Part of a complex that contains SOS1,
CC ABI1 and EPS8L2. Associates with F-actin.
CC {ECO:0000269|PubMed:14565974}.
CC -!- INTERACTION:
CC Q8TE68; Q9H013: ADAM19; NbExp=2; IntAct=EBI-7487998, EBI-8567699;
CC Q8TE68; P07766: CD3E; NbExp=6; IntAct=EBI-7487998, EBI-1211297;
CC Q8TE68; Q9NYB0: TERF2IP; NbExp=2; IntAct=EBI-7487998, EBI-750109;
CC Q8TE68-2; Q9NYB9-2: ABI2; NbExp=3; IntAct=EBI-12003490, EBI-11096309;
CC Q8TE68-2; A8MQ03: CYSRT1; NbExp=3; IntAct=EBI-12003490, EBI-3867333;
CC Q8TE68-3; P28799: GRN; NbExp=3; IntAct=EBI-21574901, EBI-747754;
CC Q8TE68-3; P42858: HTT; NbExp=3; IntAct=EBI-21574901, EBI-466029;
CC Q8TE68-3; O43933: PEX1; NbExp=3; IntAct=EBI-21574901, EBI-988601;
CC Q8TE68-3; O76024: WFS1; NbExp=3; IntAct=EBI-21574901, EBI-720609;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14565974}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1; Synonyms=A;
CC IsoId=Q8TE68-1; Sequence=Displayed;
CC Name=2; Synonyms=B;
CC IsoId=Q8TE68-2; Sequence=VSP_019083, VSP_019085;
CC Name=3; Synonyms=C;
CC IsoId=Q8TE68-3; Sequence=VSP_019084, VSP_019088, VSP_019089;
CC Name=4;
CC IsoId=Q8TE68-4; Sequence=VSP_019082, VSP_019086, VSP_019087,
CC VSP_019088;
CC -!- TISSUE SPECIFICITY: Detected in placenta.
CC {ECO:0000269|PubMed:14565974}.
CC -!- SIMILARITY: Belongs to the EPS8 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAG03038.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=AAG03039.1; Type=Erroneous gene model prediction; 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; AF282168; AAG03039.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AF282167; AAG03038.1; ALT_FRAME; mRNA.
DR EMBL; AY074928; AAL76117.1; -; mRNA.
DR EMBL; AF370395; AAQ15231.1; -; mRNA.
DR EMBL; AK000265; BAA91041.1; -; mRNA.
DR EMBL; AK075098; BAC11399.1; -; mRNA.
DR EMBL; AC005782; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC011476; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC004907; AAH04907.2; -; mRNA.
DR EMBL; BC015763; AAH15763.1; -; mRNA.
DR CCDS; CCDS12914.1; -. [Q8TE68-1]
DR CCDS; CCDS12915.1; -. [Q8TE68-2]
DR RefSeq; NP_060199.3; NM_017729.3. [Q8TE68-2]
DR RefSeq; NP_573441.2; NM_133180.2. [Q8TE68-1]
DR PDB; 2K2M; NMR; -; A=481-536.
DR PDB; 2ROL; NMR; -; A=478-537.
DR PDBsum; 2K2M; -.
DR PDBsum; 2ROL; -.
DR AlphaFoldDB; Q8TE68; -.
DR BMRB; Q8TE68; -.
DR SMR; Q8TE68; -.
DR BioGRID; 120218; 53.
DR CORUM; Q8TE68; -.
DR IntAct; Q8TE68; 13.
DR MINT; Q8TE68; -.
DR STRING; 9606.ENSP00000201647; -.
DR iPTMnet; Q8TE68; -.
DR PhosphoSitePlus; Q8TE68; -.
DR BioMuta; EPS8L1; -.
DR EPD; Q8TE68; -.
DR jPOST; Q8TE68; -.
DR MassIVE; Q8TE68; -.
DR MaxQB; Q8TE68; -.
DR PaxDb; Q8TE68; -.
DR PeptideAtlas; Q8TE68; -.
DR PRIDE; Q8TE68; -.
DR ProteomicsDB; 74407; -. [Q8TE68-1]
DR ProteomicsDB; 74408; -. [Q8TE68-2]
DR ProteomicsDB; 74409; -. [Q8TE68-3]
DR ProteomicsDB; 74410; -. [Q8TE68-4]
DR Antibodypedia; 19481; 159 antibodies from 24 providers.
DR DNASU; 54869; -.
DR Ensembl; ENST00000201647.11; ENSP00000201647.5; ENSG00000131037.15. [Q8TE68-1]
DR Ensembl; ENST00000245618.5; ENSP00000245618.4; ENSG00000131037.15. [Q8TE68-2]
DR GeneID; 54869; -.
DR KEGG; hsa:54869; -.
DR MANE-Select; ENST00000201647.11; ENSP00000201647.5; NM_133180.3; NP_573441.2.
DR UCSC; uc002qis.5; human. [Q8TE68-1]
DR CTD; 54869; -.
DR DisGeNET; 54869; -.
DR GeneCards; EPS8L1; -.
DR HGNC; HGNC:21295; EPS8L1.
DR HPA; ENSG00000131037; Tissue enhanced (esophagus, skin).
DR MIM; 614987; gene.
DR neXtProt; NX_Q8TE68; -.
DR OpenTargets; ENSG00000131037; -.
DR PharmGKB; PA134990326; -.
DR VEuPathDB; HostDB:ENSG00000131037; -.
DR eggNOG; KOG3557; Eukaryota.
DR GeneTree; ENSGT00940000158125; -.
DR HOGENOM; CLU_014510_0_0_1; -.
DR InParanoid; Q8TE68; -.
DR OMA; SEVRRPH; -.
DR OrthoDB; 218804at2759; -.
DR PhylomeDB; Q8TE68; -.
DR TreeFam; TF313069; -.
DR PathwayCommons; Q8TE68; -.
DR SignaLink; Q8TE68; -.
DR BioGRID-ORCS; 54869; 19 hits in 1081 CRISPR screens.
DR ChiTaRS; EPS8L1; human.
DR EvolutionaryTrace; Q8TE68; -.
DR GeneWiki; EPS8L1; -.
DR GenomeRNAi; 54869; -.
DR Pharos; Q8TE68; Tbio.
DR PRO; PR:Q8TE68; -.
DR Proteomes; UP000005640; Chromosome 19.
DR RNAct; Q8TE68; protein.
DR Bgee; ENSG00000131037; Expressed in lower esophagus mucosa and 164 other tissues.
DR ExpressionAtlas; Q8TE68; baseline and differential.
DR Genevisible; Q8TE68; HS.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0032991; C:protein-containing complex; IDA:UniProtKB.
DR GO; GO:0032587; C:ruffle membrane; IDA:UniProtKB.
DR GO; GO:0003779; F:actin binding; IDA:UniProtKB.
DR GO; GO:0045296; F:cadherin binding; HDA:BHF-UCL.
DR GO; GO:0042608; F:T cell receptor binding; IPI:UniProtKB.
DR GO; GO:1900029; P:positive regulation of ruffle assembly; IGI:UniProtKB.
DR GO; GO:0050790; P:regulation of catalytic activity; IEA:GOC.
DR GO; GO:0035023; P:regulation of Rho protein signal transduction; IDA:UniProtKB.
DR GO; GO:0007266; P:Rho protein signal transduction; IDA:UniProtKB.
DR CDD; cd01210; PTB_EPS8; 1.
DR CDD; cd11764; SH3_Eps8; 1.
DR Gene3D; 1.10.150.50; -; 1.
DR Gene3D; 2.30.29.30; -; 1.
DR InterPro; IPR039801; EPS8-like.
DR InterPro; IPR033928; EPS8_PTB.
DR InterPro; IPR035462; Eps8_SH3.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR013625; PTB.
DR InterPro; IPR006020; PTB/PI_dom.
DR InterPro; IPR013761; SAM/pointed_sf.
DR InterPro; IPR041418; SAM_3.
DR InterPro; IPR036028; SH3-like_dom_sf.
DR InterPro; IPR001452; SH3_domain.
DR PANTHER; PTHR12287; PTHR12287; 1.
DR Pfam; PF08416; PTB; 1.
DR Pfam; PF18016; SAM_3; 1.
DR Pfam; PF00018; SH3_1; 1.
DR SMART; SM00462; PTB; 1.
DR SMART; SM00326; SH3; 1.
DR SUPFAM; SSF50044; SSF50044; 1.
DR PROSITE; PS50002; SH3; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Coiled coil; Cytoplasm; Phosphoprotein;
KW Reference proteome; SH3 domain.
FT CHAIN 1..723
FT /note="Epidermal growth factor receptor kinase substrate 8-
FT like protein 1"
FT /id="PRO_0000239082"
FT DOMAIN 478..537
FT /note="SH3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT REGION 162..247
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 442..477
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 537..589
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 609..636
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 689..719
FT /evidence="ECO:0000255"
FT COMPBIAS 162..182
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 550..571
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 572..589
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 182
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 187
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q8R5F8"
FT VAR_SEQ 1..177
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:10514543"
FT /id="VSP_019082"
FT VAR_SEQ 1..127
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_019083"
FT VAR_SEQ 1..39
FT /note="MSTATGPEAAPKPSAKSIYEQRKRYSTVVMADVSQYPVN -> MGRKAIVLA
FT IANTSLAFPLCQ (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_019084"
FT VAR_SEQ 128..143
FT /note="ERAQPDVHFFQGLRLG -> MNRTWPRRIWGSSQDE (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_019085"
FT VAR_SEQ 178..187
FT /note="QRDRSPAAET -> MSPLSPGSPL (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:10514543"
FT /id="VSP_019086"
FT VAR_SEQ 191..300
FT /note="QRRPSVRAVISTVERGAGRGRPQAKPIPEAEEAQRPEPVGTSSNADSASPDL
FT GPRGPDLAVLQAEREVDILNHVFDDVESFVSRLQKSAEAARVLEHRERGRRSRRRAAG
FT -> ARADLTAILTGCPPLSACLVLAPRPHRRARLLPS (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:10514543"
FT /id="VSP_019087"
FT VAR_SEQ 451
FT /note="R -> RQVTQATQQGRGWEVRGRGRSAWPRLTRLSYFL (in isoform 3
FT and isoform 4)"
FT /evidence="ECO:0000303|PubMed:10514543,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_019088"
FT VAR_SEQ 509..696
FT /note="DDSRKWWKVRDPAGQEGYVPYNILTPYPGPRLHHSQSPARSLNSTPPPPPAP
FT APAPPPALARPRWDRPRWDSCDSLNGLDPSEKEKFSQMLIVNEELQARLAQGRSGPSRA
FT VPGPRAPEPQLSPGSDASEVRAWLQAKGFSSGTVDALGVLTGAQLFSLQKEELRAVSPE
FT EGARVYSQVTVQRSLLED -> ED (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_019089"
FT VARIANT 4
FT /note="A -> T (in dbSNP:rs12609976)"
FT /evidence="ECO:0000269|PubMed:12620401,
FT ECO:0000269|PubMed:15498874"
FT /id="VAR_060375"
FT VARIANT 288
FT /note="R -> G (in dbSNP:rs1620074)"
FT /id="VAR_060376"
FT VARIANT 457
FT /note="Q -> E (in dbSNP:rs1628576)"
FT /evidence="ECO:0000269|PubMed:12620401,
FT ECO:0000269|PubMed:15498874"
FT /id="VAR_056870"
FT VARIANT 669
FT /note="K -> R (in dbSNP:rs1054940)"
FT /evidence="ECO:0000269|PubMed:12620401,
FT ECO:0000269|PubMed:14702039, ECO:0000269|PubMed:15498874"
FT /id="VAR_060377"
FT VARIANT 703
FT /note="L -> P (in dbSNP:rs60073068)"
FT /id="VAR_061647"
FT CONFLICT 30
FT /note="M -> T (in Ref. 4; BAC11399)"
FT /evidence="ECO:0000305"
FT CONFLICT 555
FT /note="P -> S (in Ref. 2; AAL76117)"
FT /evidence="ECO:0000305"
FT CONFLICT 688
FT /note="T -> I (in Ref. 4; BAA91041)"
FT /evidence="ECO:0000305"
FT CONFLICT 695
FT /note="E -> G (in Ref. 4; BAC11399)"
FT /evidence="ECO:0000305"
FT STRAND 482..487
FT /evidence="ECO:0007829|PDB:2K2M"
FT STRAND 493..496
FT /evidence="ECO:0007829|PDB:2K2M"
FT STRAND 504..509
FT /evidence="ECO:0007829|PDB:2K2M"
FT STRAND 511..518
FT /evidence="ECO:0007829|PDB:2K2M"
FT STRAND 525..528
FT /evidence="ECO:0007829|PDB:2K2M"
FT HELIX 529..531
FT /evidence="ECO:0007829|PDB:2K2M"
FT STRAND 532..534
FT /evidence="ECO:0007829|PDB:2K2M"
SQ SEQUENCE 723 AA; 80251 MW; E55F71B6E128151E CRC64;
MSTATGPEAA PKPSAKSIYE QRKRYSTVVM ADVSQYPVNH LVTFCLGEDD GVHTVEDASR
KLAVMDSQGR VWAQEMLLRV SPDHVTLLDP ASKEELESYP LGAIVRCDAV MPPGRSRSLL
LLVCQEPERA QPDVHFFQGL RLGAELIRED IQGALHNYRS GRGERRAAAL RATQEELQRD
RSPAAETPPL QRRPSVRAVI STVERGAGRG RPQAKPIPEA EEAQRPEPVG TSSNADSASP
DLGPRGPDLA VLQAEREVDI LNHVFDDVES FVSRLQKSAE AARVLEHRER GRRSRRRAAG
EGLLTLRAKP PSEAEYTDVL QKIKYAFSLL ARLRGNIADP SSPELLHFLF GPLQMIVNTS
GGPEFASSVR RPHLTSDAVA LLRDNVTPRE NELWTSLGDS WTRPGLELSP EEGPPYRPEF
FSGWEPPVTD PQSRAWEDPV EKQLQHERRR RQQSAPQVAV NGHRDLEPES EPQLESETAG
KWVLCNYDFQ ARNSSELSVK QRDVLEVLDD SRKWWKVRDP AGQEGYVPYN ILTPYPGPRL
HHSQSPARSL NSTPPPPPAP APAPPPALAR PRWDRPRWDS CDSLNGLDPS EKEKFSQMLI
VNEELQARLA QGRSGPSRAV PGPRAPEPQL SPGSDASEVR AWLQAKGFSS GTVDALGVLT
GAQLFSLQKE ELRAVSPEEG ARVYSQVTVQ RSLLEDKEKV SELEAVMEKQ KKKVEGEVEM
EVI
