ID   CDGAP_DROME             Reviewed;        1843 AA.
AC   Q9VIS1; Q6AWI4; Q8MSV9; Q9NCL1;
DT   26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 2.
DT   27-MAR-2024, entry version 172.
DE   RecName: Full=GTPase-activating protein CdGAPr;
DE   AltName: Full=d-CdGAPr;
GN   Name=CdGAPr; ORFNames=CG10538;
OS   Drosophila melanogaster (Fruit fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC   Drosophilidae; Drosophila; Sophophora.
OX   NCBI_TaxID=7227;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX   PubMed=10842085; DOI=10.1016/s0925-4773(00)00291-4;
RA   Sagnier T., Grienenberger A., Mariol M.-C., Berenger H., Pradel J.,
RA   Graba Y.;
RT   "Dynamic expression of d-CdGAPr, a novel Drosophila melanogaster gene
RT   encoding a GTPase activating protein.";
RL   Mech. Dev. 94:267-270(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Berkeley;
RX   PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA   Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA   Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA   George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA   Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA   Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA   Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA   An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA   Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA   Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA   Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA   Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA   Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA   Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA   Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA   Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA   Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA   Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA   Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA   Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA   Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA   Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA   McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA   Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA   Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA   Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA   Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA   Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA   Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA   Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA   Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA   Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA   Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA   Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA   Venter J.C.;
RT   "The genome sequence of Drosophila melanogaster.";
RL   Science 287:2185-2195(2000).
RN   [3]
RP   GENOME REANNOTATION.
RC   STRAIN=Berkeley;
RX   PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA   Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA   Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA   Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA   Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA   Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA   Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT   "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT   review.";
RL   Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Berkeley; TISSUE=Embryo;
RA   Stapleton M., Carlson J.W., Chavez C., Frise E., George R.A., Pacleb J.M.,
RA   Park S., Wan K.H., Yu C., Rubin G.M., Celniker S.E.;
RL   Submitted (AUG-2004) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1062-1843.
RC   STRAIN=Berkeley; TISSUE=Embryo;
RX   PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA   Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A.,
RA   Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA   Celniker S.E.;
RT   "A Drosophila full-length cDNA resource.";
RL   Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
RN   [6]
RP   FUNCTION.
RX   PubMed=17360775; DOI=10.1242/dev.001529;
RA   Murakami S., Umetsu D., Maeyama Y., Sato M., Yoshida S., Tabata T.;
RT   "Focal adhesion kinase controls morphogenesis of the Drosophila optic
RT   stalk.";
RL   Development 134:1539-1548(2007).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1216, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY.
RX   PubMed=17372656; DOI=10.1039/b617545g;
RA   Bodenmiller B., Mueller L.N., Pedrioli P.G.A., Pflieger D., Juenger M.A.,
RA   Eng J.K., Aebersold R., Tao W.A.;
RT   "An integrated chemical, mass spectrometric and computational strategy for
RT   (quantitative) phosphoproteomics: application to Drosophila melanogaster
RT   Kc167 cells.";
RL   Mol. Biosyst. 3:275-286(2007).
RN   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-166; SER-168; SER-180;
RP   SER-837; SER-840; THR-843; SER-851; SER-861; SER-872; SER-876; SER-1029;
RP   THR-1118; THR-1121; SER-1125; SER-1281; SER-1284; SER-1453; SER-1456 AND
RP   THR-1679, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC   TISSUE=Embryo;
RX   PubMed=18327897; DOI=10.1021/pr700696a;
RA   Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P.;
RT   "Phosphoproteome analysis of Drosophila melanogaster embryos.";
RL   J. Proteome Res. 7:1675-1682(2008).
CC   -!- FUNCTION: Probably functions as a GTPase-activating protein (GAP) for
CC       RAC1 and/or CDC42. Required for optic stalk formation.
CC       {ECO:0000269|PubMed:17360775}.
CC   -!- TISSUE SPECIFICITY: Ubiquitously expressed.
CC       {ECO:0000269|PubMed:10842085}.
CC   -!- DEVELOPMENTAL STAGE: Expressed at all developmental stages, with
CC       highest expression at the posterior pole of the early cellular
CC       blastoderm, the neuro-ectoderm prior to neuroblast delamination, rows
CC       of epidermal cells in the most posterior part of thoracic and first
CC       abdominal segments and a ring of epidermal cells at the posterior end
CC       of the embryo. {ECO:0000269|PubMed:10842085}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAM49910.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC       Sequence=AAT94493.1; Type=Frameshift; Evidence={ECO:0000305};
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DR   EMBL; AF218776; AAF44627.1; -; mRNA.
DR   EMBL; AE014134; AAF53844.2; -; Genomic_DNA.
DR   EMBL; BT015264; AAT94493.1; ALT_FRAME; mRNA.
DR   EMBL; AY118541; AAM49910.1; ALT_INIT; mRNA.
DR   RefSeq; NP_001260600.1; NM_001273671.2.
DR   RefSeq; NP_610002.1; NM_136158.5.
DR   AlphaFoldDB; Q9VIS1; -.
DR   SMR; Q9VIS1; -.
DR   BioGRID; 61243; 3.
DR   IntAct; Q9VIS1; 3.
DR   STRING; 7227.FBpp0304488; -.
DR   iPTMnet; Q9VIS1; -.
DR   PaxDb; 7227-FBpp0304488; -.
DR   DNASU; 35267; -.
DR   EnsemblMetazoa; FBtr0081318; FBpp0080851; FBgn0032821.
DR   EnsemblMetazoa; FBtr0332179; FBpp0304488; FBgn0032821.
DR   GeneID; 35267; -.
DR   KEGG; dme:Dmel_CG10538; -.
DR   UCSC; CG10538-RA; d. melanogaster.
DR   AGR; FB:FBgn0032821; -.
DR   CTD; 35267; -.
DR   FlyBase; FBgn0032821; CdGAPr.
DR   VEuPathDB; VectorBase:FBgn0032821; -.
DR   eggNOG; KOG1449; Eukaryota.
DR   GeneTree; ENSGT00940000168991; -.
DR   InParanoid; Q9VIS1; -.
DR   OMA; HALQKDM; -.
DR   OrthoDB; 2913909at2759; -.
DR   PhylomeDB; Q9VIS1; -.
DR   Reactome; R-DME-8980692; RHOA GTPase cycle.
DR   Reactome; R-DME-9013148; CDC42 GTPase cycle.
DR   Reactome; R-DME-9013149; RAC1 GTPase cycle.
DR   Reactome; R-DME-9013405; RHOD GTPase cycle.
DR   Reactome; R-DME-9013406; RHOQ GTPase cycle.
DR   Reactome; R-DME-9013409; RHOJ GTPase cycle.
DR   Reactome; R-DME-9013420; RHOU GTPase cycle.
DR   Reactome; R-DME-9013423; RAC3 GTPase cycle.
DR   Reactome; R-DME-9035034; RHOF GTPase cycle.
DR   SignaLink; Q9VIS1; -.
DR   BioGRID-ORCS; 35267; 0 hits in 3 CRISPR screens.
DR   GenomeRNAi; 35267; -.
DR   PRO; PR:Q9VIS1; -.
DR   Proteomes; UP000000803; Chromosome 2L.
DR   Bgee; FBgn0032821; Expressed in parasegment (Drosophila) and 33 other cell types or tissues.
DR   ExpressionAtlas; Q9VIS1; baseline and differential.
DR   GO; GO:0005096; F:GTPase activator activity; ISS:FlyBase.
DR   GO; GO:0031290; P:retinal ganglion cell axon guidance; IMP:UniProtKB.
DR   GO; GO:0007264; P:small GTPase mediated signal transduction; IBA:GO_Central.
DR   CDD; cd04384; RhoGAP_CdGAP; 1.
DR   CDD; cd11835; SH3_ARHGAP32_33; 1.
DR   Gene3D; 1.10.555.10; Rho GTPase activation protein; 1.
DR   Gene3D; 2.30.30.40; SH3 Domains; 1.
DR   InterPro; IPR008936; Rho_GTPase_activation_prot.
DR   InterPro; IPR000198; RhoGAP_dom.
DR   InterPro; IPR036028; SH3-like_dom_sf.
DR   InterPro; IPR001452; SH3_domain.
DR   PANTHER; PTHR15729; CDC42 GTPASE-ACTIVATING PROTEIN; 1.
DR   PANTHER; PTHR15729:SF10; GTPASE-ACTIVATING PROTEIN CDGAPR; 1.
DR   Pfam; PF00620; RhoGAP; 1.
DR   SMART; SM00324; RhoGAP; 1.
DR   SMART; SM00326; SH3; 1.
DR   SUPFAM; SSF48350; GTPase activation domain, GAP; 1.
DR   SUPFAM; SSF50044; SH3-domain; 1.
DR   PROSITE; PS50238; RHOGAP; 1.
DR   PROSITE; PS50002; SH3; 1.
DR   Genevisible; Q9VIS1; DM.
PE   1: Evidence at protein level;
KW   Coiled coil; Developmental protein; GTPase activation; Phosphoprotein;
KW   Reference proteome; SH3 domain.
FT   CHAIN           1..1843
FT                   /note="GTPase-activating protein CdGAPr"
FT                   /id="PRO_0000320117"
FT   DOMAIN          295..363
FT                   /note="SH3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT   DOMAIN          424..618
FT                   /note="Rho-GAP"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00172"
FT   REGION          94..117
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          746..780
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          894..975
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1013..1106
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1721..1745
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1779..1829
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          1378..1404
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        760..780
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        926..952
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1027..1052
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1068..1099
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1721..1744
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1779..1794
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1803..1829
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         166
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:18327897"
FT   MOD_RES         168
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:18327897"
FT   MOD_RES         180
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:18327897"
FT   MOD_RES         837
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:18327897"
FT   MOD_RES         840
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:18327897"
FT   MOD_RES         843
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000269|PubMed:18327897"
FT   MOD_RES         851
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:18327897"
FT   MOD_RES         861
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:18327897"
FT   MOD_RES         872
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:18327897"
FT   MOD_RES         876
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:18327897"
FT   MOD_RES         1029
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:18327897"
FT   MOD_RES         1118
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000269|PubMed:18327897"
FT   MOD_RES         1121
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000269|PubMed:18327897"
FT   MOD_RES         1125
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:18327897"
FT   MOD_RES         1216
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:17372656"
FT   MOD_RES         1281
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:18327897"
FT   MOD_RES         1284
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:18327897"
FT   MOD_RES         1453
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:18327897"
FT   MOD_RES         1456
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:18327897"
FT   MOD_RES         1679
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000269|PubMed:18327897"
FT   CONFLICT        1092
FT                   /note="Missing (in Ref. 4; AAT94493 and 5; AAM49910)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1818..1820
FT                   /note="NNR -> K (in Ref. 5; AAM49910)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   1843 AA;  204217 MW;  4D5C65C637765D57 CRC64;
     MSDKVSTSLA AQLHSHALAS AEAGGIGGVN GGPIACHAST DKDAQAPPLQ FEMDAPAAAI
     SAQLNFKIVP ADSLPGLSYQ DMFASMNTSQ ISNASTESSC SPPIQGAVPP PKPSRHMAVQ
     PLNSKSCRFP KLEECAHFHY ERVQLGPLSV QLLDDKSEHM GSSIASQSLG GDLPHSSLRS
     FSPESCWFII RVCPQRCEPF LIKRSFENMQ LLDEMLHRCV YDRKISGLRN MEELAAELPS
     ESDVEYAVAK YLERFSKIAS DSLTCGTILT WLQLDNKGRR LPLADGETQR TINTPAVGAA
     YGVRRYQAQA PDEINIEVGD MISVIDMPSP AESIWWRGKK SHLQKSLYEV GFFPQSCVAT
     IGDKVPRNFP MPAPLVGHLD ASPTKPVLRK HGKLIAFFRS FILSRPSRRR LKQSGIYRER
     VFNCDLSEHL LNSGQDIPMV LRSCAEFIEN YGVIDGIYRL SGITSNIQRL RRAFDEERVP
     DLGNPEMKQD IHAVSSLLKM YFRELPNPLC TYQLYDNFVE AIQVKADEAD ERLRLMKETV
     LKLPPPHYRT LKYLAEHLYK VSQHHGRTGM TDKNLAIVWA PNLLRSPALE SGGVAALRGV
     GVQAVVTEYL IRNCHNIFDA LDDHPARHSM VASATAAAAN AAGGELRLES LTDCESLLVE
     QREQDQSLGV VERPKSLSTG GAKLISLEEA QERHSRVEGA DLKQSLPISM LTSASSNAAS
     NIGSYIEVGG GPSSLPDKYH TVLSAPRSWQ KRKPDKTPSW KSIFSRSQRQ GNPDPGQKIT
     TDVKDSVASR VSFVQASHAH ASKELTKHDK PKSIELLETT SNERDPKPMD LCIRSNSIDS
     LRTVGHSRSV SHDSYFDLLQ SPQRGHMTTC PSRELSELGL NFDREEPEMR IFSESESLVS
     SPRVGKENVP PASGSATRRI MRARPEDFSS QTNSVNPSPK KQPRLNLLSP SSARTMPPPP
     LSAPGTASSS CGHESGGAEN CCKRYKLEDQ LCDIQFIDCG TPENVPTTQQ QFASVEVHPP
     PKPARANQSP ISSSNGASVG SSSSSTRYSY PSVQLGAKRK EQQDAKERFS YQGTFTQPGQ
     KQESSAPRPV HSTNNGATLR KPRVEPVEDG QIKLHVPTPT TPARSPRYSL LLCDTESSDN
     SSAVNTPQYD MEPLMLTSAM SGVSGVSSNV QQQQLLLGVD ASSSYLGSSH ESLGQNINNH
     HDAEQRDMNA LKRELSLDLN PLQPRLPQPA NRAATLPVKD QLQAAAAAMC SSPNNSNFTD
     NTSQSVTPSE YGYQHLQRQL SMHSLLATDE SSPVYEDFEQ TPVKMVPSPI KSTISITYKS
     PEKEKKPSAI LETNFDENTV YEQVKLFRNS VTEVNQMLHE RSSLKQIAEE EQHDGGAYKA
     AEMTQQLLQL EQEHHDHEEQ QEKEPEDEEQ SQLLYENIEL RKPKTVYENL RGEEMKFITE
     EQKPNVDRIE LDSLDSLPDN MEHEQSSPSK SPTFSVKELA NKFESSPVEQ LPNFDFSVRG
     GSMKKPNELS VPKTMPAPVP LKKLNSSAQK ITRSLDENAF VREFGGKQLQ DLSLSNKLPE
     VMSEVNSRRK SFDFTRPKTL NPPKRLPGMS ITEEICQKRV GEMEAITPTT ENRISLIQQN
     NMPKEQQSSA NQFLPPAGRK NVLTGVVLDR ERIDKIKEER RQQLTQKYYG DTLKSRSRTE
     LNSEDNFPAA ESLRIKSKSR GDMHALQKDI DMNLKQLSRV TGGGSECTLH TGLSQGNGQE
     HLGQQRVRRI SDEKNQNCDT SNGGVSGITS TSLLSVKTTA QKYGSTSKTP ANKFERSQPM
     PRDRLQRNSL AESNAGTNNR EKISPQFSIR DVTAMFESRS QNQ
//