BCAR3_MOUSE
ID BCAR3_MOUSE Reviewed; 820 AA.
AC Q9QZK2; Q3TNC9; Q3UP10;
DT 04-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 145.
DE RecName: Full=Breast cancer anti-estrogen resistance protein 3 homolog;
DE AltName: Full=p130Cas-binding protein AND-34;
GN Name=Bcar3; Synonyms=And34;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY,
RP PHOSPHORYLATION, INTERACTION WITH BCAR1, AND INDUCTION BY
RP INTERLEUKIN-1-BETA AND TNF-ALPHA.
RC STRAIN=C57BL/6J;
RX PubMed=10438950;
RA Cai D., Clayton L.K., Smolyar A., Lerner A.;
RT "AND-34, a novel p130Cas-binding thymic stromal cell protein regulated by
RT adhesion and inflammatory cytokines.";
RL J. Immunol. 163:2104-2112(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=C57BL/6J; TISSUE=Kidney;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=FVB/N; TISSUE=Mammary tumor;
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 FUNCTION IN GTPASES ACTIVATION, AND INTERACTION WITH BCAR1; PTK2/FAK1 AND
RP PTPN1.
RX PubMed=10896938; DOI=10.1074/jbc.m003074200;
RA Gotoh T., Cai D., Tian X., Feig L.A., Lerner A.;
RT "p130Cas regulates the activity of AND-34, a novel Ral, Rap1, and R-Ras
RT guanine nucleotide exchange factor.";
RL J. Biol. Chem. 275:30118-30123(2000).
RN [5]
RP TISSUE SPECIFICITY, AND INTERACTION WITH NEDD9 AND BCAR1.
RX PubMed=12517963; DOI=10.4049/jimmunol.170.2.969;
RA Cai D., Felekkis K.N., Near R.I., O'Neill G.M., van Seventer J.M.,
RA Golemis E.A., Lerner A.;
RT "The GDP exchange factor AND-34 is expressed in B cells, associates with
RT HEF1, and activates Cdc42.";
RL J. Immunol. 170:969-978(2003).
RN [6]
RP FUNCTION, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX PubMed=19365570;
RA Near R.I., Smith R.S., Toselli P.A., Freddo T.F., Bloom A.B.,
RA Vanden Borre P., Seldin D.C., Lerner A.;
RT "Loss of AND-34/BCAR3 expression in mice results in rupture of the adult
RT lens.";
RL Mol. Vis. 15:685-699(2009).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-370 AND SER-466, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Kidney, and Lung;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [8]
RP FUNCTION, IDENTIFICATION IN A COMPLEX WITH PTPRA; BCAR1 AND SRC,
RP SUBCELLULAR LOCATION, AND DOMAIN.
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 [9]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=25499443; DOI=10.1186/s13058-014-0476-9;
RA Guo J., Canaff L., Rajadurai C.V., Fils-Aime N., Tian J., Dai M., Korah J.,
RA Villatoro M., Park M., Ali S., Lebrun J.J.;
RT "Breast cancer anti-estrogen resistance 3 inhibits transforming growth
RT factor beta/Smad signaling and associates with favorable breast cancer
RT disease outcomes.";
RL Breast Cancer Res. 16:476-476(2014).
CC -!- FUNCTION: Acts as an adapter protein downstream of several growth
CC factor receptors to promote cell proliferation, migration, and
CC redistribution of actin fibers (PubMed:12517963). Specifically involved
CC in INS/insulin signaling pathway by mediating MAPK1/ERK2-MAPK3/ERK1
CC activation and DNA synthesis (By similarity). Promotes insulin-mediated
CC membrane ruffling (By similarity). In response to vasoconstrictor
CC peptide EDN1, involved in the activation of RAP1 downstream of PTK2B
CC via interaction with phosphorylated BCAR1 (PubMed:10896938). Inhibits
CC cell migration and invasion via regulation of TGFB-mediated matrix
CC digestion, actin filament rearrangement, and inhibition of invadopodia
CC activity (PubMed:25499443). May inhibit TGFB-SMAD signaling, via
CC facilitating BCAR1 and SMAD2 and/or SMAD3 interaction
CC (PubMed:25499443). Regulates EGF-induced DNA synthesis (By similarity).
CC Required for the maintenance of ocular lens morphology and structural
CC integrity, potentially via regulation of focal adhesion complex
CC signaling (PubMed:19365570). Acts upstream of PTPRA to regulate the
CC localization of BCAR1 and PTPRA to focal adhesions, via regulation of
CC SRC-mediated phosphorylation of PTPRA (PubMed:22801373). Positively
CC regulates integrin-induced tyrosine phosphorylation of BCAR1
CC (PubMed:22801373). Acts as a guanine nucleotide exchange factor (GEF)
CC for small GTPases RALA, RAP1A and RRAS (PubMed:10896938). However, in a
CC contrasting study, lacks GEF activity towards RAP1 (By similarity).
CC {ECO:0000250|UniProtKB:D3ZAZ5, ECO:0000250|UniProtKB:O75815,
CC ECO:0000269|PubMed:10896938, ECO:0000269|PubMed:12517963,
CC ECO:0000269|PubMed:19365570, ECO:0000269|PubMed:22801373,
CC ECO:0000269|PubMed:25499443}.
CC -!- SUBUNIT: Part of a complex comprised of PTPRA, BCAR1, BCAR3 (via SH2
CC domain) and SRC; the formation of the complex is dependent on integrin
CC mediated-tyrosine phosphorylation of PTPRA (PubMed:22801373). Within
CC the complex, interacts (via SH2 domain) with PTPRA (when phosphorylated
CC on 'Tyr-825') (PubMed:22801373). Interacts (via Ras-GEF domain) with
CC BCAR1 (PubMed:10438950, PubMed:10896938, PubMed:12517963). Interacts
CC with (via Ras-GEF domain) NEDD9 (PubMed:12517963). Interacts with
CC PTK2B/FAK1 (PubMed:10896938). Interacts with PTPN1. Interacts (via SH2
CC domain) with EGFR (when tyrosine-phosphorylated) (By similarity).
CC {ECO:0000250|UniProtKB:O75815, ECO:0000269|PubMed:10438950,
CC ECO:0000269|PubMed:10896938, ECO:0000269|PubMed:12517963,
CC ECO:0000269|PubMed:22801373}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:25499443}. Cell
CC junction, focal adhesion {ECO:0000269|PubMed:22801373}.
CC Note=Localization to focal adhesions depends on interaction with PTPRA.
CC {ECO:0000269|PubMed:22801373}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9QZK2-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9QZK2-2; Sequence=VSP_017815;
CC -!- TISSUE SPECIFICITY: Abundantly expressed in the lung and brain, with
CC lower expression in splenic lymphocytes and liver (at protein level)
CC (PubMed:19365570). Expressed in splenic lymphocytes (at protein level)
CC (PubMed:19365570). Expressed in the lymph node cortical region,
CC periphery of the splenic white pulp and in alveolar lung fibroblasts
CC (PubMed:19365570). Expressed in epithelial cells in the lens equatorial
CC region and early stage nucleated cortical lens fiber cells
CC (PubMed:19365570). Expressed in the thymus (PubMed:10438950). Expressed
CC in B-cells (PubMed:12517963). {ECO:0000269|PubMed:10438950,
CC ECO:0000269|PubMed:12517963, ECO:0000269|PubMed:19365570}.
CC -!- INDUCTION: Up-regulated by IL1A and LTA, in thymus cortical reticular
CC cell lines. {ECO:0000269|PubMed:10438950}.
CC -!- DOMAIN: The SH2 domain mediates interaction with tyrosine-
CC phosphorylated proteins (PubMed:10896938, PubMed:22801373). However,
CC not involved in the binding to phosphorylated BCAR1 (PubMed:10896938).
CC Required for cell cycle progression in response to INS/insulin (By
CC similarity). Required for regulation of EGF-induced DNA synthesis (By
CC similarity). {ECO:0000250|UniProtKB:O75815,
CC ECO:0000269|PubMed:10896938, ECO:0000269|PubMed:22801373}.
CC -!- DOMAIN: The Ras-GEF domain appears to adopt a closed conformation
CC rendering it incapable of carrying out canonical exchange factor
CC function, this closed conformation is probably required for interaction
CC with BCAR1. {ECO:0000269|PubMed:10896938}.
CC -!- PTM: Phosphorylated on tyrosine residues.
CC {ECO:0000269|PubMed:10438950}.
CC -!- DISRUPTION PHENOTYPE: Knockout mice are generally normal and viable
CC (PubMed:19365570). Retinal white circular lesions in anterior chamber
CC derived from the lens cortex (PubMed:19365570). Retinal lens is
CC partially opaque and irregular in structure, with rupture leading to
CC cortical lens fragments floating in the aqueous humor
CC (PubMed:19365570). Abnormally deep anterior chamber with anterior
CC synechiae, ectropion uveae, mild to moderate retinal ganglion loss, and
CC a small pigmented pre-retinal membrane overlying the optic nerve
CC (PubMed:19365570). Reduced phosphorylation of AKT1 and BCAR1 in lens
CC epithelial cells (PubMed:19365570). Retinal lens abnormalities develop
CC progressively postnatally; at postnatal day 3 (P3) there is anterior
CC lens vacuolization and liquefaction of lens cortical fibers
CC (PubMed:19365570). At P24 there is evidence of extensive lens cortex
CC vacuolation and early lens extrusion, progressing to extrusion of lens
CC cortical material at P33 (PubMed:19365570).
CC {ECO:0000269|PubMed:19365570}.
CC -!- CAUTION: The guanine nucleotide exchange factor (GEF) activity is
CC controversial. One study showed GEF activity towards RALA, RAP1A and
CC RRAS (PubMed:10896938). However, in another study, a construct
CC containing only the Ras-GEF domain lacks GEF activity towards RAP1 (By
CC similarity). {ECO:0000250|UniProtKB:O75815,
CC ECO:0000269|PubMed:10896938}.
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DR EMBL; AF179566; AAD53182.1; -; mRNA.
DR EMBL; AK143894; BAE25587.1; -; mRNA.
DR EMBL; AK165396; BAE38160.1; -; mRNA.
DR EMBL; BC023930; AAH23930.1; -; mRNA.
DR CCDS; CCDS17810.1; -. [Q9QZK2-1]
DR RefSeq; NP_038895.1; NM_013867.2. [Q9QZK2-1]
DR AlphaFoldDB; Q9QZK2; -.
DR SMR; Q9QZK2; -.
DR BioGRID; 205895; 1.
DR STRING; 10090.ENSMUSP00000029766; -.
DR iPTMnet; Q9QZK2; -.
DR PhosphoSitePlus; Q9QZK2; -.
DR MaxQB; Q9QZK2; -.
DR PaxDb; Q9QZK2; -.
DR PeptideAtlas; Q9QZK2; -.
DR PRIDE; Q9QZK2; -.
DR ProteomicsDB; 273443; -. [Q9QZK2-1]
DR ProteomicsDB; 273444; -. [Q9QZK2-2]
DR Antibodypedia; 2973; 170 antibodies from 34 providers.
DR Ensembl; ENSMUST00000029766; ENSMUSP00000029766; ENSMUSG00000028121. [Q9QZK2-1]
DR GeneID; 29815; -.
DR KEGG; mmu:29815; -.
DR UCSC; uc008req.2; mouse. [Q9QZK2-1]
DR CTD; 8412; -.
DR MGI; MGI:1352501; Bcar3.
DR VEuPathDB; HostDB:ENSMUSG00000028121; -.
DR eggNOG; ENOG502QPX3; Eukaryota.
DR GeneTree; ENSGT00940000154130; -.
DR HOGENOM; CLU_015281_0_0_1; -.
DR InParanoid; Q9QZK2; -.
DR OMA; RSDAYQD; -.
DR OrthoDB; 138275at2759; -.
DR PhylomeDB; Q9QZK2; -.
DR TreeFam; TF323756; -.
DR BioGRID-ORCS; 29815; 2 hits in 73 CRISPR screens.
DR ChiTaRS; Bcar3; mouse.
DR PRO; PR:Q9QZK2; -.
DR Proteomes; UP000000589; Chromosome 3.
DR RNAct; Q9QZK2; protein.
DR Bgee; ENSMUSG00000028121; Expressed in primary oocyte and 236 other tissues.
DR ExpressionAtlas; Q9QZK2; baseline and differential.
DR Genevisible; Q9QZK2; MM.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005925; C:focal adhesion; IMP:UniProtKB.
DR GO; GO:0016020; C:membrane; IMP:UniProtKB.
DR GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; IEA:UniProtKB-KW.
DR GO; GO:0019900; F:kinase binding; ISO:MGI.
DR GO; GO:0001784; F:phosphotyrosine residue binding; ISS:UniProtKB.
DR GO; GO:0086100; P:endothelin receptor signaling pathway; ISS:UniProtKB.
DR GO; GO:0008286; P:insulin receptor signaling pathway; ISS:UniProtKB.
DR GO; GO:0002089; P:lens morphogenesis in camera-type eye; IMP:MGI.
DR GO; GO:0045740; P:positive regulation of DNA replication; ISS:UniProtKB.
DR GO; GO:0045742; P:positive regulation of epidermal growth factor receptor signaling pathway; ISS:UniProtKB.
DR GO; GO:0043547; P:positive regulation of GTPase activity; ISS:UniProtKB.
DR GO; GO:0043410; P:positive regulation of MAPK cascade; ISS:UniProtKB.
DR GO; GO:0033138; P:positive regulation of peptidyl-serine phosphorylation; IMP:MGI.
DR GO; GO:0007264; P:small GTPase mediated signal transduction; IEA:InterPro.
DR CDD; cd10337; SH2_BCAR3; 1.
DR Gene3D; 1.10.840.10; -; 1.
DR Gene3D; 3.30.505.10; -; 1.
DR InterPro; IPR028849; BCAR3.
DR InterPro; IPR023578; Ras_GEF_dom_sf.
DR InterPro; IPR001895; RASGEF_cat_dom.
DR InterPro; IPR036964; RASGEF_cat_dom_sf.
DR InterPro; IPR000980; SH2.
DR InterPro; IPR036860; SH2_dom_sf.
DR InterPro; IPR044102; SH2_SHEP1/BCAR3/NSP1.
DR PANTHER; PTHR14247:SF10; PTHR14247:SF10; 1.
DR Pfam; PF00617; RasGEF; 1.
DR Pfam; PF00017; SH2; 1.
DR SMART; SM00147; RasGEF; 1.
DR SMART; SM00252; SH2; 1.
DR SUPFAM; SSF48366; SSF48366; 1.
DR SUPFAM; SSF55550; SSF55550; 1.
DR PROSITE; PS50009; RASGEF_CAT; 1.
DR PROSITE; PS50001; SH2; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Cell junction; Cytoplasm;
KW Guanine-nucleotide releasing factor; Methylation; Phosphoprotein;
KW Reference proteome; SH2 domain.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:O75815"
FT CHAIN 2..820
FT /note="Breast cancer anti-estrogen resistance protein 3
FT homolog"
FT /id="PRO_0000230286"
FT DOMAIN 148..247
FT /note="SH2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00191"
FT DOMAIN 543..813
FT /note="Ras-GEF"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00168"
FT REGION 40..81
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 346..367
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 739..743
FT /note="Mediates the interaction with BCAR1/p130CAS"
FT /evidence="ECO:0000250|UniProtKB:O75815"
FT COMPBIAS 65..81
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:O75815"
FT MOD_RES 32
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O75815"
FT MOD_RES 72
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O75815"
FT MOD_RES 77
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O75815"
FT MOD_RES 176
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O75815"
FT MOD_RES 284
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O75815"
FT MOD_RES 329
FT /note="N6-methyllysine"
FT /evidence="ECO:0000250|UniProtKB:O75815"
FT MOD_RES 353
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O75815"
FT MOD_RES 358
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O75815"
FT MOD_RES 370
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 437
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:O75815"
FT MOD_RES 466
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT VAR_SEQ 1..120
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_017815"
FT CONFLICT 36
FT /note="E -> G (in Ref. 2; BAE25587)"
FT /evidence="ECO:0000305"
FT CONFLICT 525
FT /note="K -> E (in Ref. 2; BAE25587)"
FT /evidence="ECO:0000305"
FT CONFLICT 795
FT /note="R -> G (in Ref. 2; BAE38160)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 820 AA; 92263 MW; 69DDACECDE869F01 CRC64;
MAAGKFASLP RNMPVNHQFP LASSMDLLSS KSPLAERRTD AYQDVSIHGT LPRKKKGPPS
IRSCDNAGHS KSPRQSSPLT QDIIQENPLQ DRKGENFIFR DPYLLDPTLE YVKFSKERHI
MDRTPERLKK ELEEELLLSS EDLRSHAWYH GRIPRQVSEN LVQRDGDFLV RDSLSSPGNF
VLTCQWKNLA QHFKINRTVL RLSEAYSRVQ YQFEMESFDS IPGLVRCYVG NRRPISQQSG
AIIFQPINRT VPLWCLEERY GTSPGRGREG SLAEGRPDVV KRLSLTTGSS IQAREHSLPR
GNLLRNKEKS GSQPACLDHV QDRKALTLKA HQSESHLPIG CKLPPQSPSM DTSPCPSSPV
FRTGSEPTLS PALVRRFSSD ARTGEALRGS DSQLCPKPPP KPCKVPFLKT PPSPSPWLTS
EANYCELNPA FAVGCDRGAK LPMQAHDSHE MLLTAKQNGP SGPRNSGINY MILDGDDQAR
HWDPLAVQTD EGQEDKTKFV PPLMETVSSF RPNDFESKLL PPENKPLETA MLKHAKELFT
NHDARVIAQH MLSVDCKVAR ILEVSEDRKR SMGVSSGLEL ITLPHGRQLR LDIIERHNTM
AIGIAVDILG CTGTLENRAG TLNKIIQVAV ELKDAMGDLY AFSAIMKALE MPQITRLEKT
WTALRHHYTQ TAILYEKQLK PFSKILHEGR ESTYVPASNV SVPLLMPLVT LMERQAVTFE
GTDMWENNDE SCEILLNHLA TARFMAEASE SYRMNAERIL ADFQPDEEMT EILRTEFQMR
LLWGSKGAEV NQNERYDKFN QILTALSRKL EPPSGKQAEL
