BCAR1_HUMAN
ID BCAR1_HUMAN Reviewed; 870 AA.
AC P56945; B3KWD7; B4DEV4; B4DGB5; B4DIW5; B7Z7X7; E9PCL5; E9PCV2; F5GXA2;
AC F5GXV6; F5H7Z0; F8WA69; Q6QEF7;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 09-FEB-2010, sequence version 2.
DT 03-AUG-2022, entry version 210.
DE RecName: Full=Breast cancer anti-estrogen resistance protein 1;
DE AltName: Full=CRK-associated substrate;
DE AltName: Full=Cas scaffolding protein family member 1;
DE AltName: Full=p130cas;
GN Name=BCAR1; Synonyms=CAS, CASS1, CRKAS;
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 [MRNA] (ISOFORM 1), AND VARIANT SER-76.
RC TISSUE=Mammary cancer;
RX PubMed=10639512; DOI=10.1093/jnci/92.2.112;
RA Brinkman A., van der Flier S., Kok E.M., Dorssers L.C.J.;
RT "BCAR1, a human homologue of the adapter protein p130Cas, induces anti-
RT estrogen resistance in breast cancer cells.";
RL J. Natl. Cancer Inst. 92:112-120(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANT SER-76.
RC TISSUE=Testis;
RA Otto E., Birnbaum S., Verbeek M., Hildebrandt F.;
RT "Interaction between human Crk-associated substrate (p130Cas) and
RT nephrocystin.";
RL Submitted (DEC-1999) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANT SER-76.
RC TISSUE=Cornea;
RA Imoto Y., Ohguro N., Yoshida A., Tsujikawa M., Inoue Y., Tano Y.;
RT "The effects of growth factors on tyrosine phosphorylation of p130Cas in
RT corneal epithelial cell.";
RL Submitted (MAR-2000) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
RA Lin L., Li H., Zhou G., Shen C., Ke R., Zhong G., Yang S.;
RL Submitted (FEB-2004) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2; 4; 5; 6; 7 AND 8),
RP AND VARIANT SER-76.
RC TISSUE=Amygdala, Caudate nucleus, Cerebellum, Hippocampus, Teratocarcinoma,
RC 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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15616553; DOI=10.1038/nature03187;
RA Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X., Xie G.,
RA Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., Bajorek E.,
RA Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J., Buckingham J.M.,
RA Callen D.F., Campbell C.S., Campbell M.L., Campbell E.W., Caoile C.,
RA Challacombe J.F., Chasteen L.A., Chertkov O., Chi H.C., Christensen M.,
RA Clark L.M., Cohn J.D., Denys M., Detter J.C., Dickson M.,
RA Dimitrijevic-Bussod M., Escobar J., Fawcett J.J., Flowers D., Fotopulos D.,
RA Glavina T., Gomez M., Gonzales E., Goodstein D., Goodwin L.A., Grady D.L.,
RA Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E.,
RA Huang W., Israni S., Jett J., Jewett P.B., Kadner K., Kimball H.,
RA Kobayashi A., Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y.,
RA Lowry S., Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J.,
RA Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D.,
RA Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L., Rash S.,
RA Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., Salamov A.,
RA Saunders E.H., Scott D., Shough T., Stallings R.L., Stalvey M.,
RA Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H.,
RA Torney D.C., Tran-Gyamfi M., Tsai M., Ulanovsky L.E., Ustaszewska A.,
RA Vo N., White P.S., Williams A.L., Wills P.L., Wu J.-R., Wu K., Yang J.,
RA DeJong P., Bruce D., Doggett N.A., Deaven L., Schmutz J., Grimwood J.,
RA Richardson P., Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M.,
RA Myers R.M., Rubin E.M., Pennacchio L.A.;
RT "The sequence and analysis of duplication-rich human chromosome 16.";
RL Nature 432:988-994(2004).
RN [7]
RP PROTEIN SEQUENCE OF 1-9; 380-391 AND 792-801, ACETYLATION AT MET-1, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Ovarian carcinoma;
RA Bienvenut W.V., Lempens A., Norman J.C.;
RL Submitted (OCT-2009) to UniProtKB.
RN [8]
RP INTERACTION WITH CSPG4.
RX PubMed=10587647; DOI=10.1038/70302;
RA Eisenmann K.M., McCarthy J.B., Simpson M.A., Keely P.J., Guan J.-L.,
RA Tachibana K., Lim L., Manser E., Furcht L.T., Iida J.;
RT "Melanoma chondroitin sulphate proteoglycan regulates cell spreading
RT through Cdc42, Ack-1 and p130cas.";
RL Nat. Cell Biol. 1:507-513(1999).
RN [9]
RP INTERACTION WITH INPPL1.
RX PubMed=11158326; DOI=10.1128/mcb.21.4.1416-1428.2001;
RA Prasad N., Topping R.S., Decker S.J.;
RT "SH2-containing inositol 5'-phosphatase SHIP2 associates with the p130(Cas)
RT adapter protein and regulates cellular adhesion and spreading.";
RL Mol. Cell. Biol. 21:1416-1428(2001).
RN [10]
RP FUNCTION, AND IDENTIFICATION IN A COMPLEX WITH SH2D3C AND CRK.
RX PubMed=12432078; DOI=10.1242/jcs.00207;
RA Sakakibara A., Ohba Y., Kurokawa K., Matsuda M., Hattori S.;
RT "Novel function of Chat in controlling cell adhesion via Cas-Crk-C3G-
RT pathway-mediated Rap1 activation.";
RL J. Cell Sci. 115:4915-4924(2002).
RN [11]
RP FUNCTION, SUBCELLULAR LOCATION, PHOSPHORYLATION, AND INTERACTION WITH BMX.
RX PubMed=12832404; DOI=10.1074/jbc.m306438200;
RA Abassi Y.A., Rehn M., Ekman N., Alitalo K., Vuori K.;
RT "p130Cas Couples the tyrosine kinase Bmx/Etk with regulation of the actin
RT cytoskeleton and cell migration.";
RL J. Biol. Chem. 278:35636-35643(2003).
RN [12]
RP INTERACTION WITH SH2D3C.
RX PubMed=17174122; DOI=10.1016/j.immuni.2006.09.014;
RA Regelmann A.G., Danzl N.M., Wanjalla C., Alexandropoulos K.;
RT "The hematopoietic isoform of Cas-Hef1-associated signal transducer
RT regulates chemokine-induced inside-out signaling and T cell trafficking.";
RL Immunity 25:907-918(2006).
RN [13]
RP FUNCTION IN CELL MIGRATION, AND INTERACTION WITH BCAR1; CDC42 AND CRK.
RX PubMed=17038317; DOI=10.1074/jbc.m604342200;
RA Modzelewska K., Newman L.P., Desai R., Keely P.J.;
RT "Ack1 mediates Cdc42-dependent cell migration and signaling to p130Cas.";
RL J. Biol. Chem. 281:37527-37535(2006).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-134; SER-139; THR-269 AND
RP SER-292, AND 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 [15]
RP PHOSPHORYLATION AT SER-139; SER-437 AND SER-639, AND INTERACTION WITH
RP BCAR3.
RX PubMed=19454314; DOI=10.1016/j.cellsig.2009.05.006;
RA Makkinje A., Near R.I., Infusini G., Vanden Borre P., Bloom A., Cai D.,
RA Costello C.E., Lerner A.;
RT "AND-34/BCAR3 regulates adhesion-dependent p130Cas serine phosphorylation
RT and breast cancer cell growth pattern.";
RL Cell. Signal. 21:1423-1435(2009).
RN [16]
RP INTERACTION WITH PTK2B/PYK2, AND PHOSPHORYLATION.
RX PubMed=19086031; DOI=10.1002/jcp.21649;
RA Rufanova V.A., Alexanian A., Wakatsuki T., Lerner A., Sorokin A.;
RT "Pyk2 mediates endothelin-1 signaling via p130Cas/BCAR3 cascade and
RT regulates human glomerular mesangial cell adhesion and spreading.";
RL J. Cell. Physiol. 219:45-56(2009).
RN [17]
RP PHOSPHORYLATION BY SRC UPON ACTIVATION OF PTK2/FAK1.
RX PubMed=19147981; DOI=10.1172/jci37160;
RA Pylayeva Y., Gillen K.M., Gerald W., Beggs H.E., Reichardt L.F.,
RA Giancotti F.G.;
RT "Ras- and PI3K-dependent breast tumorigenesis in mice and humans requires
RT focal adhesion kinase signaling.";
RL J. Clin. Invest. 119:252-266(2009).
RN [18]
RP INTERACTION WITH PEAK1.
RX PubMed=20534451; DOI=10.1073/pnas.0914776107;
RA Wang Y., Kelber J.A., Tran Cao H.S., Cantin G.T., Lin R., Wang W.,
RA Kaushal S., Bristow J.M., Edgington T.S., Hoffman R.M., Bouvet M.,
RA Yates J.R. III, Klemke R.L.;
RT "Pseudopodium-enriched atypical kinase 1 regulates the cytoskeleton and
RT cancer progression.";
RL Proc. Natl. Acad. Sci. U.S.A. 107:10920-10925(2010).
RN [19]
RP ERRATUM OF PUBMED:20534451.
RA Wang Y., Kelber J.A., Tran Cao H.S., Cantin G.T., Lin R., Wang W.,
RA Kaushal S., Bristow J.M., Edgington T.S., Hoffman R.M., Bouvet M.,
RA Yates J.R. III, Klemke R.L.;
RL Proc. Natl. Acad. Sci. U.S.A. 107:13556-13556(2010).
RN [20]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-134 AND SER-139, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [21]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-428, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [22]
RP IDENTIFICATION IN A COMPLEX WITH PTPRA; BCAR3 AND SRC.
RX PubMed=22801373; DOI=10.1128/mcb.00214-12;
RA Sun G., Cheng S.Y., Chen M., Lim C.J., Pallen C.J.;
RT "Protein tyrosine phosphatase alpha phosphotyrosyl-789 binds BCAR3 to
RT position Cas for activation at integrin-mediated focal adhesions.";
RL Mol. Cell. Biol. 32:3776-3789(2012).
RN [23]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-139 AND SER-639, AND
RP IDENTIFICATION BY 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).
RN [24]
RP DEPHOSPHORYLATION AT TYR-128 BY PTPN14, AND PHOSPHORYLATION AT TYR-128 BY
RP SRC.
RX PubMed=22710723; DOI=10.1038/onc.2012.220;
RA Zhang P., Guo A., Possemato A., Wang C., Beard L., Carlin C.,
RA Markowitz S.D., Polakiewicz R.D., Wang Z.;
RT "Identification and functional characterization of p130Cas as a substrate
RT of protein tyrosine phosphatase nonreceptor 14.";
RL Oncogene 32:2087-2095(2013).
RN [25]
RP X-RAY CRYSTALLOGRAPHY (1.14 ANGSTROMS) OF 3-71.
RX PubMed=15784259; DOI=10.1016/j.jmb.2005.02.017;
RA Wisniewska M., Bossenmaier B., Georges G., Hesse F., Dangl M.,
RA Kunkele K.P., Ioannidis I., Huber R., Engh R.A.;
RT "The 1.1 A resolution crystal structure of the p130cas SH3 domain and
RT ramifications for ligand selectivity.";
RL J. Mol. Biol. 347:1005-1014(2005).
RN [26]
RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 645-870 IN COMPLEX WITH SH2D3C AND
RP BCAR3, AND MUTAGENESIS OF LEU-787; PHE-794 AND ASP-797.
RX PubMed=22081014; DOI=10.1038/nsmb.2152;
RA Mace P.D., Wallez Y., Dobaczewska M.K., Lee J.J., Robinson H.,
RA Pasquale E.B., Riedl S.J.;
RT "NSP-Cas protein structures reveal a promiscuous interaction module in cell
RT signaling.";
RL Nat. Struct. Mol. Biol. 18:1381-1387(2011).
RN [27]
RP VARIANT [LARGE SCALE ANALYSIS] THR-407.
RX PubMed=16959974; DOI=10.1126/science.1133427;
RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P.,
RA Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V.,
RA Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H.,
RA Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W.,
RA Velculescu V.E.;
RT "The consensus coding sequences of human breast and colorectal cancers.";
RL Science 314:268-274(2006).
CC -!- FUNCTION: Docking protein which plays a central coordinating role for
CC tyrosine kinase-based signaling related to cell adhesion
CC (PubMed:12832404, PubMed:12432078). Implicated in induction of cell
CC migration and cell branching (PubMed:12432078, PubMed:12832404,
CC PubMed:17038317). Involved in the BCAR3-mediated inhibition of TGFB
CC signaling (By similarity). {ECO:0000250|UniProtKB:Q61140,
CC ECO:0000269|PubMed:12432078, ECO:0000269|PubMed:12832404,
CC ECO:0000269|PubMed:17038317}.
CC -!- SUBUNIT: Forms complexes in vivo with PTK2/FAK1, adapter protein CRKL
CC and LYN kinase. Can heterodimerize with NEDD9. Component of a complex
CC comprised of SH2D3C, BCAR1/CAS, and CRK (PubMed:12432078). Within the
CC complex, interacts with SH2D3C (via C-terminus), and CRK
CC (PubMed:12432078, PubMed:17174122). Part of a complex comprised of
CC PTPRA, BCAR1, BCAR3 (via SH2 domain) and SRC; the formation of the
CC complex is dependent on intergrin mediated-tyrosine phosphorylation of
CC PTPRA (PubMed:22801373). Interacts with BCAR3 (via Ras-GEF domain); the
CC interaction regulates adhesion-dependent serine phosphorylation
CC (PubMed:22081014). Interacts with SMAD2 and SMAD3 (By similarity).
CC Interacts with NPHP1 (By similarity). Interacts with PTK2B/PYK2
CC (PubMed:19086031). Interacts (via C-terminus) with SH2D3C/CHAT isoform
CC 2 (via C-terminus) (PubMed:17174122, PubMed:22081014). Interacts with
CC activated CSPG4. Interacts with BMX, INPPL1/SHIP2 and PEAK1. Part of a
CC collagen-stimulated complex involved in cell migration made of CDC42,
CC CRK, TNK2 and BCAR1/p130cas. Interacts with TNK2 via SH3 domains.
CC {ECO:0000250|UniProtKB:Q61140, ECO:0000269|PubMed:10587647,
CC ECO:0000269|PubMed:11158326, ECO:0000269|PubMed:12432078,
CC ECO:0000269|PubMed:12832404, ECO:0000269|PubMed:17038317,
CC ECO:0000269|PubMed:17174122, ECO:0000269|PubMed:19086031,
CC ECO:0000269|PubMed:19454314, ECO:0000269|PubMed:20534451,
CC ECO:0000269|PubMed:22081014, ECO:0000269|PubMed:22801373}.
CC -!- INTERACTION:
CC P56945; Q49AR9: ANKS1A; NbExp=3; IntAct=EBI-702093, EBI-11954519;
CC P56945; O75815-1: BCAR3; NbExp=3; IntAct=EBI-702093, EBI-15953103;
CC P56945; P53618: COPB1; NbExp=3; IntAct=EBI-702093, EBI-359063;
CC P56945; P46108: CRK; NbExp=7; IntAct=EBI-702093, EBI-886;
CC P56945; Q5T9C2-3: FAM102A; NbExp=3; IntAct=EBI-702093, EBI-11980989;
CC P56945; Q86YD7: FAM90A1; NbExp=3; IntAct=EBI-702093, EBI-6658203;
CC P56945; P06241: FYN; NbExp=4; IntAct=EBI-702093, EBI-515315;
CC P56945; P06241-3: FYN; NbExp=3; IntAct=EBI-702093, EBI-10691738;
CC P56945; Q9BZE0: GLIS2; NbExp=3; IntAct=EBI-702093, EBI-7251368;
CC P56945; O15357: INPPL1; NbExp=2; IntAct=EBI-702093, EBI-1384248;
CC P56945; P46940: IQGAP1; NbExp=4; IntAct=EBI-702093, EBI-297509;
CC P56945; P50281: MMP14; NbExp=3; IntAct=EBI-702093, EBI-992788;
CC P56945; O43639: NCK2; NbExp=3; IntAct=EBI-702093, EBI-713635;
CC P56945; Q9H792: PEAK1; NbExp=3; IntAct=EBI-702093, EBI-2609701;
CC P56945; Q96QH2: PRAM1; NbExp=3; IntAct=EBI-702093, EBI-2860740;
CC P56945; Q05397: PTK2; NbExp=2; IntAct=EBI-702093, EBI-702142;
CC P56945; P18031: PTPN1; NbExp=5; IntAct=EBI-702093, EBI-968788;
CC P56945; Q05209: PTPN12; NbExp=5; IntAct=EBI-702093, EBI-2266035;
CC P56945; Q8N5H7-2: SH2D3C; NbExp=8; IntAct=EBI-702093, EBI-15952996;
CC P56945; P12931: SRC; NbExp=3; IntAct=EBI-702093, EBI-621482;
CC P56945; Q9C0H9: SRCIN1; NbExp=3; IntAct=EBI-702093, EBI-1393949;
CC P56945; Q07912: TNK2; NbExp=5; IntAct=EBI-702093, EBI-603457;
CC P56945; Q68CZ2: TNS3; NbExp=8; IntAct=EBI-702093, EBI-1220488;
CC P56945; O75604: USP2; NbExp=3; IntAct=EBI-702093, EBI-743272;
CC P56945; P18206-2: VCL; NbExp=3; IntAct=EBI-702093, EBI-11027067;
CC P56945; P07947: YES1; NbExp=4; IntAct=EBI-702093, EBI-515331;
CC P56945; Q9QWI6: Srcin1; Xeno; NbExp=3; IntAct=EBI-702093, EBI-775592;
CC P56945; Q04205: TNS; Xeno; NbExp=2; IntAct=EBI-702093, EBI-2607590;
CC -!- SUBCELLULAR LOCATION: Cell junction, focal adhesion
CC {ECO:0000269|PubMed:12832404}. Cytoplasm {ECO:0000269|PubMed:12832404}.
CC Cell projection, axon {ECO:0000250|UniProtKB:Q61140}.
CC Note=Unphosphorylated form localizes in the cytoplasm (By similarity).
CC Localizes to focal adhesion sites following integrin engagement (By
CC similarity). {ECO:0000250|UniProtKB:Q61140}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=8;
CC Name=1;
CC IsoId=P56945-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P56945-2; Sequence=VSP_043559;
CC Name=3;
CC IsoId=P56945-3; Sequence=VSP_045355;
CC Name=4;
CC IsoId=P56945-4; Sequence=VSP_046127, VSP_046128;
CC Name=5;
CC IsoId=P56945-5; Sequence=VSP_046748;
CC Name=6;
CC IsoId=P56945-6; Sequence=VSP_046749;
CC Name=7;
CC IsoId=P56945-7; Sequence=VSP_046750;
CC Name=8;
CC IsoId=P56945-8; Sequence=VSP_046751;
CC -!- TISSUE SPECIFICITY: Widely expressed with an abundant expression in the
CC testis. Low level of expression seen in the liver, thymus, and
CC peripheral blood leukocytes. The protein has been detected in a B-cell
CC line.
CC -!- DOMAIN: Contains a central domain (substrate domain) containing
CC multiple potential SH2-binding sites and a C-terminal domain containing
CC a divergent helix-loop-helix (HLH) motif. The SH2-binding sites
CC putatively bind CRK, NCK and ABL1 SH2 domains. The HLH motif is
CC absolutely required for the induction of pseudohyphal growth in yeast
CC and mediates heterodimerization with NEDD9 (By similarity).
CC {ECO:0000250}.
CC -!- DOMAIN: A serine-rich region promotes activation of the serum response
CC element (SRE).
CC -!- DOMAIN: The SH3 domain is necessary for the localization of the protein
CC to focal adhesions and interacts with one proline-rich region of
CC PTK2/FAK11.
CC -!- PTM: PTK2/FAK1 activation mediates phosphorylation at the YDYVHL motif;
CC phosphorylation is most likely catalyzed by SRC family members. SRC-
CC family kinases are recruited to the phosphorylated sites and can
CC phosphorylate other tyrosine residues. Tyrosine phosphorylation is
CC triggered by integrin-mediated adhesion of cells to the extracellular
CC matrix. {ECO:0000269|PubMed:12832404, ECO:0000269|PubMed:19147981,
CC ECO:0000269|PubMed:19454314, ECO:0000269|PubMed:22710723}.
CC -!- PTM: Dephosphorylated by PTPN14 at Tyr-128.
CC -!- PTM: Phosphorylated by SRC kinase in a EDN1- and PTK2B-mediated manner;
CC phosphorylation strengthens its interaction with BCAR3 as part of the
CC PTK2B/BCAR1/BCAR3/RAP1 signaling pathway.
CC {ECO:0000269|PubMed:19086031}.
CC -!- SIMILARITY: Belongs to the CAS family. {ECO:0000305}.
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/BCAR1ID761ch16q23.html";
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; AJ242987; CAB75875.2; -; mRNA.
DR EMBL; AF218451; AAF27527.1; -; mRNA.
DR EMBL; AB040024; BAA92711.1; -; mRNA.
DR EMBL; AY545071; AAS48631.1; -; mRNA.
DR EMBL; AK027608; BAB55230.1; -; mRNA.
DR EMBL; AK124815; BAG54099.1; -; mRNA.
DR EMBL; AK293808; BAG57215.1; -; mRNA.
DR EMBL; AK294513; BAG57726.1; -; mRNA.
DR EMBL; AK295809; BAG58627.1; -; mRNA.
DR EMBL; AK302617; BAH13763.1; -; mRNA.
DR EMBL; AC009078; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS10915.1; -. [P56945-1]
DR CCDS; CCDS54037.1; -. [P56945-5]
DR CCDS; CCDS54038.1; -. [P56945-3]
DR CCDS; CCDS54039.1; -. [P56945-4]
DR CCDS; CCDS54040.1; -. [P56945-6]
DR CCDS; CCDS54041.1; -. [P56945-8]
DR CCDS; CCDS54042.1; -. [P56945-2]
DR CCDS; CCDS54043.1; -. [P56945-7]
DR RefSeq; NP_001164185.1; NM_001170714.1. [P56945-6]
DR RefSeq; NP_001164186.1; NM_001170715.1. [P56945-7]
DR RefSeq; NP_001164187.1; NM_001170716.1. [P56945-2]
DR RefSeq; NP_001164188.1; NM_001170717.1. [P56945-3]
DR RefSeq; NP_001164189.1; NM_001170718.1. [P56945-8]
DR RefSeq; NP_001164190.1; NM_001170719.1. [P56945-5]
DR RefSeq; NP_001164191.1; NM_001170720.1. [P56945-4]
DR RefSeq; NP_055382.2; NM_014567.3. [P56945-1]
DR RefSeq; XP_016879386.1; XM_017023897.1.
DR PDB; 1WYX; X-ray; 1.14 A; A/B=3-71.
DR PDB; 3T6G; X-ray; 2.50 A; B/D=645-870.
DR PDB; 5O2M; NMR; -; A=4-73.
DR PDB; 5O2P; NMR; -; A=4-73.
DR PDB; 5O2Q; NMR; -; A=4-73.
DR PDBsum; 1WYX; -.
DR PDBsum; 3T6G; -.
DR PDBsum; 5O2M; -.
DR PDBsum; 5O2P; -.
DR PDBsum; 5O2Q; -.
DR AlphaFoldDB; P56945; -.
DR SMR; P56945; -.
DR BioGRID; 114934; 526.
DR CORUM; P56945; -.
DR DIP; DIP-33855N; -.
DR ELM; P56945; -.
DR IntAct; P56945; 262.
DR MINT; P56945; -.
DR STRING; 9606.ENSP00000391669; -.
DR iPTMnet; P56945; -.
DR PhosphoSitePlus; P56945; -.
DR BioMuta; BCAR1; -.
DR DMDM; 288558806; -.
DR EPD; P56945; -.
DR jPOST; P56945; -.
DR MassIVE; P56945; -.
DR MaxQB; P56945; -.
DR PaxDb; P56945; -.
DR PeptideAtlas; P56945; -.
DR PRIDE; P56945; -.
DR ProteomicsDB; 19466; -.
DR ProteomicsDB; 19521; -.
DR ProteomicsDB; 24360; -.
DR ProteomicsDB; 24539; -.
DR ProteomicsDB; 27632; -.
DR ProteomicsDB; 30445; -.
DR ProteomicsDB; 56960; -. [P56945-1]
DR ProteomicsDB; 56961; -. [P56945-2]
DR ABCD; P56945; 2 sequenced antibodies.
DR Antibodypedia; 3607; 847 antibodies from 41 providers.
DR DNASU; 9564; -.
DR Ensembl; ENST00000162330.10; ENSP00000162330.5; ENSG00000050820.17. [P56945-1]
DR Ensembl; ENST00000393420.10; ENSP00000377072.6; ENSG00000050820.17. [P56945-3]
DR Ensembl; ENST00000393422.6; ENSP00000377074.2; ENSG00000050820.17. [P56945-7]
DR Ensembl; ENST00000418647.7; ENSP00000391669.3; ENSG00000050820.17. [P56945-6]
DR Ensembl; ENST00000420641.7; ENSP00000392708.3; ENSG00000050820.17. [P56945-2]
DR Ensembl; ENST00000535626.6; ENSP00000440370.2; ENSG00000050820.17. [P56945-4]
DR Ensembl; ENST00000538440.6; ENSP00000443841.2; ENSG00000050820.17. [P56945-8]
DR Ensembl; ENST00000542031.6; ENSP00000440415.2; ENSG00000050820.17. [P56945-5]
DR GeneID; 9564; -.
DR KEGG; hsa:9564; -.
DR MANE-Select; ENST00000162330.10; ENSP00000162330.5; NM_014567.5; NP_055382.2.
DR UCSC; uc002fdv.4; human. [P56945-1]
DR CTD; 9564; -.
DR DisGeNET; 9564; -.
DR GeneCards; BCAR1; -.
DR HGNC; HGNC:971; BCAR1.
DR HPA; ENSG00000050820; Low tissue specificity.
DR MIM; 602941; gene.
DR neXtProt; NX_P56945; -.
DR OpenTargets; ENSG00000050820; -.
DR PharmGKB; PA25281; -.
DR VEuPathDB; HostDB:ENSG00000050820; -.
DR eggNOG; ENOG502QQHE; Eukaryota.
DR GeneTree; ENSGT00950000183008; -.
DR HOGENOM; CLU_017000_1_0_1; -.
DR InParanoid; P56945; -.
DR OMA; AQDVRHK; -.
DR OrthoDB; 1086228at2759; -.
DR PhylomeDB; P56945; -.
DR TreeFam; TF328782; -.
DR PathwayCommons; P56945; -.
DR Reactome; R-HSA-186763; Downstream signal transduction.
DR Reactome; R-HSA-372708; p130Cas linkage to MAPK signaling for integrins.
DR Reactome; R-HSA-4420097; VEGFA-VEGFR2 Pathway.
DR Reactome; R-HSA-8849471; PTK6 Regulates RHO GTPases, RAS GTPase and MAP kinases.
DR SignaLink; P56945; -.
DR SIGNOR; P56945; -.
DR BioGRID-ORCS; 9564; 298 hits in 1082 CRISPR screens.
DR ChiTaRS; BCAR1; human.
DR EvolutionaryTrace; P56945; -.
DR GeneWiki; BCAR1; -.
DR GenomeRNAi; 9564; -.
DR Pharos; P56945; Tbio.
DR PRO; PR:P56945; -.
DR Proteomes; UP000005640; Chromosome 16.
DR RNAct; P56945; protein.
DR Bgee; ENSG00000050820; Expressed in right hemisphere of cerebellum and 95 other tissues.
DR ExpressionAtlas; P56945; baseline and differential.
DR Genevisible; P56945; HS.
DR GO; GO:0015629; C:actin cytoskeleton; IEA:Ensembl.
DR GO; GO:0030424; C:axon; IEA:UniProtKB-SubCell.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005925; C:focal adhesion; IDA:BHF-UCL.
DR GO; GO:0030027; C:lamellipodium; IEA:Ensembl.
DR GO; GO:0016020; C:membrane; IEA:Ensembl.
DR GO; GO:0001726; C:ruffle; IDA:UniProtKB.
DR GO; GO:0019901; F:protein kinase binding; IPI:UniProtKB.
DR GO; GO:0017124; F:SH3 domain binding; IEA:UniProtKB-KW.
DR GO; GO:0007015; P:actin filament organization; IDA:UniProtKB.
DR GO; GO:0090527; P:actin filament reorganization; IBA:GO_Central.
DR GO; GO:0050851; P:antigen receptor-mediated signaling pathway; IDA:UniProtKB.
DR GO; GO:0050853; P:B cell receptor signaling pathway; IDA:UniProtKB.
DR GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR GO; GO:0060326; P:cell chemotaxis; IMP:BHF-UCL.
DR GO; GO:0051301; P:cell division; NAS:UniProtKB.
DR GO; GO:0016477; P:cell migration; IDA:UniProtKB.
DR GO; GO:0035729; P:cellular response to hepatocyte growth factor stimulus; IMP:BHF-UCL.
DR GO; GO:0086100; P:endothelin receptor signaling pathway; IDA:UniProtKB.
DR GO; GO:0007173; P:epidermal growth factor receptor signaling pathway; ISS:UniProtKB.
DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; ISS:UniProtKB.
DR GO; GO:0048012; P:hepatocyte growth factor receptor signaling pathway; IMP:BHF-UCL.
DR GO; GO:0008286; P:insulin receptor signaling pathway; ISS:UniProtKB.
DR GO; GO:0007229; P:integrin-mediated signaling pathway; IDA:UniProtKB.
DR GO; GO:0048011; P:neurotrophin TRK receptor signaling pathway; ISS:UniProtKB.
DR GO; GO:0048008; P:platelet-derived growth factor receptor signaling pathway; ISS:UniProtKB.
DR GO; GO:0030335; P:positive regulation of cell migration; IDA:UniProtKB.
DR GO; GO:0010595; P:positive regulation of endothelial cell migration; IDA:BHF-UCL.
DR GO; GO:0042981; P:regulation of apoptotic process; TAS:UniProtKB.
DR GO; GO:0001558; P:regulation of cell growth; TAS:UniProtKB.
DR GO; GO:0050852; P:T cell receptor signaling pathway; NAS:UniProtKB.
DR GO; GO:0007169; P:transmembrane receptor protein tyrosine kinase signaling pathway; IBA:GO_Central.
DR GO; GO:0048010; P:vascular endothelial growth factor receptor signaling pathway; IMP:BHF-UCL.
DR CDD; cd12001; SH3_BCAR1; 1.
DR Gene3D; 1.20.120.830; -; 1.
DR InterPro; IPR028848; BCAR1.
DR InterPro; IPR035745; BCAR1_SH3.
DR InterPro; IPR021901; CAS_C.
DR InterPro; IPR037362; CAS_fam.
DR InterPro; IPR014928; Serine_rich_dom.
DR InterPro; IPR038319; Serine_rich_sf.
DR InterPro; IPR036028; SH3-like_dom_sf.
DR InterPro; IPR001452; SH3_domain.
DR PANTHER; PTHR10654; PTHR10654; 1.
DR PANTHER; PTHR10654:SF15; PTHR10654:SF15; 1.
DR Pfam; PF12026; CAS_C; 1.
DR Pfam; PF08824; Serine_rich; 1.
DR Pfam; PF00018; SH3_1; 1.
DR PRINTS; PR00452; SH3DOMAIN.
DR SMART; SM00326; SH3; 1.
DR SUPFAM; SSF50044; SSF50044; 1.
DR PROSITE; PS50002; SH3; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Cell adhesion;
KW Cell junction; Cell projection; Cytoplasm; Diabetes mellitus;
KW Direct protein sequencing; Phosphoprotein; Reference proteome; SH3 domain;
KW SH3-binding.
FT CHAIN 1..870
FT /note="Breast cancer anti-estrogen resistance protein 1"
FT /id="PRO_0000064854"
FT DOMAIN 3..65
FT /note="SH3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT REGION 70..156
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 115..416
FT /note="Substrate for kinases"
FT /evidence="ECO:0000250"
FT REGION 411..449
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 609..658
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 715..734
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 746..796
FT /note="Divergent helix-loop-helix motif"
FT MOTIF 635..643
FT /note="SH3-binding"
FT /evidence="ECO:0000255"
FT COMPBIAS 72..99
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 100..156
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 427..445
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 623..653
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000269|Ref.7"
FT MOD_RES 128
FT /note="Phosphotyrosine; by SRC"
FT /evidence="ECO:0000269|PubMed:22710723"
FT MOD_RES 134
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231"
FT MOD_RES 139
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:19454314,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 234
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q61140"
FT MOD_RES 249
FT /note="Phosphotyrosine; by ABL1"
FT /evidence="ECO:0000250|UniProtKB:Q63767"
FT MOD_RES 269
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 292
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 362
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q61140"
FT MOD_RES 372
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q61140"
FT MOD_RES 410
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q61140"
FT MOD_RES 428
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692"
FT MOD_RES 437
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:19454314"
FT MOD_RES 639
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:19454314,
FT ECO:0007744|PubMed:23186163"
FT VAR_SEQ 1..4
FT /note="MNHL -> MLTHRPQEAEQRGRTPGPSFEW (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_043559"
FT VAR_SEQ 1..4
FT /note="MNHL -> MQGK (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_046127"
FT VAR_SEQ 1..4
FT /note="MNHL -> ME (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_046748"
FT VAR_SEQ 1..4
FT /note="MNHL -> MPAKPFLSSVLLSWKVLDFSGPGPQGTGQPCSCGHWAEGQGGPP
FT EPAGGP (in isoform 6)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_046749"
FT VAR_SEQ 1..4
FT /note="MNHL -> MHCPGEAPLAAPRPTPKDPCLR (in isoform 7)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_046750"
FT VAR_SEQ 1..4
FT /note="MNHL -> MSVP (in isoform 8)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_046751"
FT VAR_SEQ 64..211
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_046128"
FT VAR_SEQ 304
FT /note="A -> AVSKCQGNARARLRLWGVW (in isoform 3)"
FT /evidence="ECO:0000303|Ref.4"
FT /id="VSP_045355"
FT VARIANT 76
FT /note="P -> S (in dbSNP:rs1035539)"
FT /evidence="ECO:0000269|PubMed:10639512,
FT ECO:0000269|PubMed:14702039, ECO:0000269|Ref.2,
FT ECO:0000269|Ref.3"
FT /id="VAR_058970"
FT VARIANT 407
FT /note="S -> T (in a breast cancer sample; somatic mutation;
FT dbSNP:rs144989936)"
FT /evidence="ECO:0000269|PubMed:16959974"
FT /id="VAR_035798"
FT VARIANT 491
FT /note="R -> L (in dbSNP:rs16957558)"
FT /id="VAR_057820"
FT VARIANT 558
FT /note="H -> R (in dbSNP:rs16957552)"
FT /id="VAR_057821"
FT MUTAGEN 787
FT /note="L->E: Weakens interaction with SH2D3C."
FT /evidence="ECO:0000269|PubMed:22081014"
FT MUTAGEN 794
FT /note="F->R: Weakens interaction with SH2D3C."
FT /evidence="ECO:0000269|PubMed:22081014"
FT MUTAGEN 797
FT /note="D->R: Weakens interaction with SH2D3C."
FT /evidence="ECO:0000269|PubMed:22081014"
FT CONFLICT 63
FT /note="L -> S (in Ref. 5; BAB55230)"
FT /evidence="ECO:0000305"
FT CONFLICT 236
FT /note="I -> T (in Ref. 2; AAF27527)"
FT /evidence="ECO:0000305"
FT CONFLICT 254
FT /note="V -> I (in Ref. 5; BAG54099)"
FT /evidence="ECO:0000305"
FT CONFLICT 349
FT /note="A -> G (in Ref. 2; AAF27527)"
FT /evidence="ECO:0000305"
FT CONFLICT 363
FT /note="D -> Y (in Ref. 2; AAF27527)"
FT /evidence="ECO:0000305"
FT CONFLICT 385
FT /note="T -> A (in Ref. 4; AAS48631)"
FT /evidence="ECO:0000305"
FT CONFLICT 428
FT /note="S -> P (in Ref. 5; BAB55230)"
FT /evidence="ECO:0000305"
FT CONFLICT 471
FT /note="S -> G (in Ref. 5; BAB55230)"
FT /evidence="ECO:0000305"
FT CONFLICT 600
FT /note="N -> S (in Ref. 4; AAS48631)"
FT /evidence="ECO:0000305"
FT CONFLICT 700
FT /note="Q -> R (in Ref. 5; BAH13763)"
FT /evidence="ECO:0000305"
FT CONFLICT 714
FT /note="P -> L (in Ref. 5; BAG54099)"
FT /evidence="ECO:0000305"
FT CONFLICT 740
FT /note="D -> G (in Ref. 4; AAS48631)"
FT /evidence="ECO:0000305"
FT STRAND 5..12
FT /evidence="ECO:0007829|PDB:1WYX"
FT STRAND 29..34
FT /evidence="ECO:0007829|PDB:1WYX"
FT HELIX 37..39
FT /evidence="ECO:0007829|PDB:1WYX"
FT STRAND 43..48
FT /evidence="ECO:0007829|PDB:1WYX"
FT STRAND 51..56
FT /evidence="ECO:0007829|PDB:1WYX"
FT HELIX 57..59
FT /evidence="ECO:0007829|PDB:1WYX"
FT STRAND 60..68
FT /evidence="ECO:0007829|PDB:1WYX"
FT HELIX 740..770
FT /evidence="ECO:0007829|PDB:3T6G"
FT HELIX 775..801
FT /evidence="ECO:0007829|PDB:3T6G"
FT HELIX 806..835
FT /evidence="ECO:0007829|PDB:3T6G"
FT HELIX 840..870
FT /evidence="ECO:0007829|PDB:3T6G"
SQ SEQUENCE 870 AA; 93372 MW; B81EC3430049E795 CRC64;
MNHLNVLAKA LYDNVAESPD ELSFRKGDIM TVLEQDTQGL DGWWLCSLHG RQGIVPGNRL
KILVGMYDKK PAGPGPGPPA TPAQPQPGLH APAPPASQYT PMLPNTYQPQ PDSVYLVPTP
SKAQQGLYQV PGPSPQFQSP PAKQTSTFSK QTPHHPFPSP ATDLYQVPPG PGGPAQDIYQ
VPPSAGMGHD IYQVPPSMDT RSWEGTKPPA KVVVPTRVGQ GYVYEAAQPE QDEYDIPRHL
LAPGPQDIYD VPPVRGLLPS QYGQEVYDTP PMAVKGPNGR DPLLEVYDVP PSVEKGLPPS
NHHAVYDVPP SVSKDVPDGP LLREETYDVP PAFAKAKPFD PARTPLVLAA PPPDSPPAED
VYDVPPPAPD LYDVPPGLRR PGPGTLYDVP RERVLPPEVA DGGVVDSGVY AVPPPAEREA
PAEGKRLSAS STGSTRSSQS ASSLEVAGPG REPLELEVAV EALARLQQGV SATVAHLLDL
AGSAGATGSW RSPSEPQEPL VQDLQAAVAA VQSAVHELLE FARSAVGNAA HTSDRALHAK
LSRQLQKMED VHQTLVAHGQ ALDAGRGGSG ATLEDLDRLV ACSRAVPEDA KQLASFLHGN
ASLLFRRTKA TAPGPEGGGT LHPNPTDKTS SIQSRPLPSP PKFTSQDSPD GQYENSEGGW
MEDYDYVHLQ GKEEFEKTQK ELLEKGSITR QGKSQLELQQ LKQFERLEQE VSRPIDHDLA
NWTPAQPLAP GRTGGLGPSD RQLLLFYLEQ CEANLTTLTN AVDAFFTAVA TNQPPKIFVA
HSKFVILSAH KLVFIGDTLS RQAKAADVRS QVTHYSNLLC DLLRGIVATT KAAALQYPSP
SAAQDMVERV KELGHSTQQF RRVLGQLAAA
