ID   SRGP1_HUMAN             Reviewed;        1085 AA.
AC   Q7Z6B7; Q9H8A3; Q9P2P2;
DT   07-JUN-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2003, sequence version 1.
DT   24-JAN-2024, entry version 177.
DE   RecName: Full=SLIT-ROBO Rho GTPase-activating protein 1;
DE            Short=srGAP1;
DE   AltName: Full=Rho GTPase-activating protein 13;
GN   Name=SRGAP1; Synonyms=ARHGAP13, KIAA1304;
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 1).
RC   TISSUE=Uterus;
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   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 23-1085 (ISOFORM 2).
RC   TISSUE=Brain;
RX   PubMed=10718198; DOI=10.1093/dnares/7.1.65;
RA   Nagase T., Kikuno R., Ishikawa K., Hirosawa M., Ohara O.;
RT   "Prediction of the coding sequences of unidentified human genes. XVI. The
RT   complete sequences of 150 new cDNA clones from brain which code for large
RT   proteins in vitro.";
RL   DNA Res. 7:65-73(2000).
RN   [3]
RP   FUNCTION, TISSUE SPECIFICITY, AND INTERACTION WITH ROBO1; CDC42 AND RHOA.
RX   PubMed=11672528; DOI=10.1016/s0092-8674(01)00530-x;
RA   Wong K., Ren X.R., Huang Y.Z., Xie Y., Liu G., Saito H., Tang H., Wen L.,
RA   Brady-Kalnay S.M., Mei L., Wu J.Y., Xiong W.C., Rao Y.;
RT   "Signal transduction in neuronal migration: roles of GTPase activating
RT   proteins and the small GTPase Cdc42 in the Slit-Robo pathway.";
RL   Cell 107:209-221(2001).
RN   [4]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA   Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT   "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT   networks.";
RL   Cell 127:635-648(2006).
RN   [5]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=18220336; DOI=10.1021/pr0705441;
RA   Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III;
RT   "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient
RT   phosphoproteomic analysis.";
RL   J. Proteome Res. 7:1346-1351(2008).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-999; THR-1001 AND SER-1032,
RP   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   [7]
RP   INTERACTION WITH FASLG.
RX   PubMed=19807924; DOI=10.1186/1471-2172-10-53;
RA   Voss M., Lettau M., Janssen O.;
RT   "Identification of SH3 domain interaction partners of human FasL (CD178) by
RT   phage display screening.";
RL   BMC Immunol. 10:53-53(2009).
RN   [8]
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   [9]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA   Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA   Bennett K.L., Superti-Furga G., Colinge J.;
RT   "Initial characterization of the human central proteome.";
RL   BMC Syst. Biol. 5:17-17(2011).
RN   [10]
RP   HETEROOLIGOMERIZATION, AND DOMAIN F-BAR.
RX   PubMed=22467852; DOI=10.1242/jcs.098962;
RA   Coutinho-Budd J., Ghukasyan V., Zylka M.J., Polleux F.;
RT   "The F-BAR domains from srGAP1, srGAP2, and srGAP3 differentially regulate
RT   membrane deformation.";
RL   J. Cell Sci. 125:3390-3401(2012).
RN   [11]
RP   INVOLVEMENT IN NMTC2, VARIANTS NMTC2 HIS-149; THR-275; CYS-617 AND ARG-875,
RP   AND CHARACTERIZATION OF VARIANTS NMTC2 HIS-149; THR-275; CYS-617 AND
RP   ARG-875.
RX   PubMed=23539728; DOI=10.1210/jc.2012-3823;
RA   He H., Bronisz A., Liyanarachchi S., Nagy R., Li W., Huang Y., Akagi K.,
RA   Saji M., Kula D., Wojcicka A., Sebastian N., Wen B., Puch Z., Kalemba M.,
RA   Stachlewska E., Czetwertynska M., Dlugosinska J., Dymecka K., Ploski R.,
RA   Krawczyk M., Morrison P.J., Ringel M.D., Kloos R.T., Jazdzewski K.,
RA   Symer D.E., Vieland V.J., Ostrowski M., Jarzab B., de la Chapelle A.;
RT   "SRGAP1 is a candidate gene for papillary thyroid carcinoma
RT   susceptibility.";
RL   J. Clin. Endocrinol. Metab. 98:E973-E980(2013).
RN   [12]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-416; SER-835; SER-917;
RP   SER-932 AND SER-1032, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP   ANALYSIS].
RC   TISSUE=Cervix carcinoma;
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: GTPase-activating protein for RhoA and Cdc42 small GTPases.
CC       Together with CDC42 seems to be involved in the pathway mediating the
CC       repulsive signaling of Robo and Slit proteins in neuronal migration.
CC       SLIT2, probably through interaction with ROBO1, increases the
CC       interaction of SRGAP1 with ROBO1 and inactivates CDC42.
CC       {ECO:0000269|PubMed:11672528}.
CC   -!- SUBUNIT: Homodimer (Probable). Forms a heterooligomer with SRGAP2 and
CC       SRGAP3 through its F-BAR domain. Interacts with ROBO1, CDC42 and RHOA.
CC       Interacts with FASLG. {ECO:0000269|PubMed:11672528,
CC       ECO:0000269|PubMed:19807924, ECO:0000305}.
CC   -!- INTERACTION:
CC       Q7Z6B7; Q14155: ARHGEF7; NbExp=4; IntAct=EBI-2481729, EBI-717515;
CC       Q7Z6B7; P42858: HTT; NbExp=4; IntAct=EBI-2481729, EBI-466029;
CC       Q7Z6B7; P63104: YWHAZ; NbExp=2; IntAct=EBI-2481729, EBI-347088;
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q7Z6B7-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q7Z6B7-2; Sequence=VSP_010580;
CC   -!- TISSUE SPECIFICITY: Expressed in brain, lung, kidney, and testis.
CC       {ECO:0000269|PubMed:11672528}.
CC   -!- DOMAIN: The F-BAR domain mediates oligomerization, binds membranes, and
CC       constrains plasma membrane protrusions. {ECO:0000269|PubMed:22467852}.
CC   -!- DISEASE: Thyroid cancer, non-medullary, 2 (NMTC2) [MIM:188470]: A form
CC       of non-medullary thyroid cancer (NMTC), a cancer characterized by
CC       tumors originating from the thyroid follicular cells. NMTCs represent
CC       approximately 95% of all cases of thyroid cancer and are classified
CC       into papillary, follicular, Hurthle cell, and anaplastic neoplasms.
CC       {ECO:0000269|PubMed:23539728}. Note=Disease susceptibility is
CC       associated with variants affecting the gene represented in this entry.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAA92542.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC       Sequence=BAA92542.1; Type=Miscellaneous discrepancy; Note=Intron retention.; Evidence={ECO:0000305};
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DR   EMBL; BC053903; AAH53903.1; -; mRNA.
DR   EMBL; AB037725; BAA92542.1; ALT_INIT; mRNA.
DR   CCDS; CCDS8967.1; -. [Q7Z6B7-1]
DR   CCDS; CCDS91718.1; -. [Q7Z6B7-2]
DR   PIR; G59436; G59436.
DR   RefSeq; NP_001333130.1; NM_001346201.1. [Q7Z6B7-2]
DR   RefSeq; NP_065813.1; NM_020762.3. [Q7Z6B7-1]
DR   AlphaFoldDB; Q7Z6B7; -.
DR   SMR; Q7Z6B7; -.
DR   BioGRID; 121583; 37.
DR   DIP; DIP-53826N; -.
DR   IntAct; Q7Z6B7; 24.
DR   MINT; Q7Z6B7; -.
DR   STRING; 9606.ENSP00000347198; -.
DR   GlyConnect; 2077; 1 N-Linked glycan (1 site).
DR   GlyCosmos; Q7Z6B7; 3 sites, 4 glycans.
DR   GlyGen; Q7Z6B7; 7 sites, 2 N-linked glycans (1 site), 2 O-linked glycans (6 sites).
DR   iPTMnet; Q7Z6B7; -.
DR   PhosphoSitePlus; Q7Z6B7; -.
DR   SwissPalm; Q7Z6B7; -.
DR   BioMuta; SRGAP1; -.
DR   DMDM; 48428624; -.
DR   EPD; Q7Z6B7; -.
DR   jPOST; Q7Z6B7; -.
DR   MassIVE; Q7Z6B7; -.
DR   MaxQB; Q7Z6B7; -.
DR   PaxDb; 9606-ENSP00000347198; -.
DR   PeptideAtlas; Q7Z6B7; -.
DR   ProteomicsDB; 69392; -. [Q7Z6B7-1]
DR   ProteomicsDB; 69393; -. [Q7Z6B7-2]
DR   Pumba; Q7Z6B7; -.
DR   ABCD; Q7Z6B7; 7 sequenced antibodies.
DR   Antibodypedia; 29129; 280 antibodies from 28 providers.
DR   DNASU; 57522; -.
DR   Ensembl; ENST00000355086.8; ENSP00000347198.3; ENSG00000196935.10. [Q7Z6B7-1]
DR   Ensembl; ENST00000631006.3; ENSP00000485752.2; ENSG00000196935.10. [Q7Z6B7-2]
DR   GeneID; 57522; -.
DR   KEGG; hsa:57522; -.
DR   MANE-Select; ENST00000355086.8; ENSP00000347198.3; NM_020762.4; NP_065813.1.
DR   UCSC; uc010ssp.2; human. [Q7Z6B7-1]
DR   AGR; HGNC:17382; -.
DR   CTD; 57522; -.
DR   DisGeNET; 57522; -.
DR   GeneCards; SRGAP1; -.
DR   HGNC; HGNC:17382; SRGAP1.
DR   HPA; ENSG00000196935; Low tissue specificity.
DR   MalaCards; SRGAP1; -.
DR   MIM; 188470; phenotype.
DR   MIM; 606523; gene.
DR   neXtProt; NX_Q7Z6B7; -.
DR   OpenTargets; ENSG00000196935; -.
DR   PharmGKB; PA134887956; -.
DR   VEuPathDB; HostDB:ENSG00000196935; -.
DR   eggNOG; KOG3565; Eukaryota.
DR   GeneTree; ENSGT00950000182824; -.
DR   HOGENOM; CLU_005715_0_0_1; -.
DR   InParanoid; Q7Z6B7; -.
DR   OMA; LIVESCV; -.
DR   OrthoDB; 2904755at2759; -.
DR   PhylomeDB; Q7Z6B7; -.
DR   TreeFam; TF315892; -.
DR   PathwayCommons; Q7Z6B7; -.
DR   Reactome; R-HSA-428543; Inactivation of CDC42 and RAC1.
DR   Reactome; R-HSA-8980692; RHOA GTPase cycle.
DR   Reactome; R-HSA-9013148; CDC42 GTPase cycle.
DR   Reactome; R-HSA-9013149; RAC1 GTPase cycle.
DR   SignaLink; Q7Z6B7; -.
DR   SIGNOR; Q7Z6B7; -.
DR   BioGRID-ORCS; 57522; 10 hits in 1140 CRISPR screens.
DR   ChiTaRS; SRGAP1; human.
DR   GeneWiki; SRGAP1; -.
DR   GenomeRNAi; 57522; -.
DR   Pharos; Q7Z6B7; Tbio.
DR   PRO; PR:Q7Z6B7; -.
DR   Proteomes; UP000005640; Chromosome 12.
DR   RNAct; Q7Z6B7; Protein.
DR   Bgee; ENSG00000196935; Expressed in buccal mucosa cell and 188 other cell types or tissues.
DR   ExpressionAtlas; Q7Z6B7; baseline and differential.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005829; C:cytosol; TAS:Reactome.
DR   GO; GO:0005096; F:GTPase activator activity; TAS:Reactome.
DR   GO; GO:0030336; P:negative regulation of cell migration; IBA:GO_Central.
DR   GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR   CDD; cd07683; F-BAR_srGAP1; 1.
DR   CDD; cd04383; RhoGAP_srGAP; 1.
DR   CDD; cd11955; SH3_srGAP1-3; 1.
DR   Gene3D; 1.20.1270.60; Arfaptin homology (AH) domain/BAR domain; 1.
DR   Gene3D; 1.10.555.10; Rho GTPase activation protein; 1.
DR   Gene3D; 2.30.30.40; SH3 Domains; 1.
DR   InterPro; IPR027267; AH/BAR_dom_sf.
DR   InterPro; IPR031160; F_BAR.
DR   InterPro; IPR001060; FCH_dom.
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   InterPro; IPR035648; srGAP1/2/3_SH3.
DR   InterPro; IPR037451; srGAP1_F-BAR.
DR   PANTHER; PTHR14166; SLIT-ROBO RHO GTPASE ACTIVATING PROTEIN; 1.
DR   PANTHER; PTHR14166:SF15; SLIT-ROBO RHO GTPASE-ACTIVATING PROTEIN 1; 1.
DR   Pfam; PF00611; FCH; 1.
DR   Pfam; PF00620; RhoGAP; 1.
DR   Pfam; PF00018; SH3_1; 1.
DR   SMART; SM00055; FCH; 1.
DR   SMART; SM00324; RhoGAP; 1.
DR   SMART; SM00326; SH3; 1.
DR   SUPFAM; SSF103657; BAR/IMD domain-like; 1.
DR   SUPFAM; SSF48350; GTPase activation domain, GAP; 1.
DR   SUPFAM; SSF50044; SH3-domain; 1.
DR   PROSITE; PS51741; F_BAR; 1.
DR   PROSITE; PS50238; RHOGAP; 1.
DR   PROSITE; PS50002; SH3; 1.
DR   Genevisible; Q7Z6B7; HS.
PE   1: Evidence at protein level;
KW   Alternative splicing; Coiled coil; Disease variant; GTPase activation;
KW   Phosphoprotein; Reference proteome; SH3 domain.
FT   CHAIN           1..1085
FT                   /note="SLIT-ROBO Rho GTPase-activating protein 1"
FT                   /id="PRO_0000056765"
FT   DOMAIN          19..314
FT                   /note="F-BAR"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01077"
FT   DOMAIN          506..694
FT                   /note="Rho-GAP"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00172"
FT   DOMAIN          743..802
FT                   /note="SH3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT   REGION          475..496
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          808..954
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          997..1038
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1051..1085
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          351..390
FT                   /evidence="ECO:0000255"
FT   COILED          956..985
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        808..830
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        831..857
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        933..947
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1056..1078
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         416
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   MOD_RES         835
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   MOD_RES         917
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   MOD_RES         932
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   MOD_RES         999
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18669648"
FT   MOD_RES         1001
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:18669648"
FT   MOD_RES         1032
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18669648,
FT                   ECO:0007744|PubMed:23186163"
FT   VAR_SEQ         479..513
FT                   /note="RPPNVPPKPQKHRKSRPRSQYNTKLFNGDLETFVK -> SRGRRNSHTRHQ
FT                   (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:10718198"
FT                   /id="VSP_010580"
FT   VARIANT         149
FT                   /note="Q -> H (in NMTC2; does not affect the interaction
FT                   with ROBO1; decreased GTPase activator activity; in SLIT2
FT                   and ROBO1-mediated inhibition of CDC42; dbSNP:rs781626187)"
FT                   /evidence="ECO:0000269|PubMed:23539728"
FT                   /id="VAR_075879"
FT   VARIANT         275
FT                   /note="A -> T (in NMTC2; does not affect the interaction
FT                   with ROBO1; slightly increased GTPase activator activity;
FT                   in SLIT2 and ROBO1-mediated inhibition of CDC42;
FT                   dbSNP:rs797044990)"
FT                   /evidence="ECO:0000269|PubMed:23539728"
FT                   /id="VAR_075880"
FT   VARIANT         512
FT                   /note="V -> I (in dbSNP:rs74691643)"
FT                   /evidence="ECO:0000269|PubMed:23539728"
FT                   /id="VAR_075881"
FT   VARIANT         617
FT                   /note="R -> C (in NMTC2; does not affect the interaction
FT                   with ROBO1; decreased GTPase activator activity; in SLIT2
FT                   and ROBO1-mediated inhibition of CDC42; dbSNP:rs114817817)"
FT                   /evidence="ECO:0000269|PubMed:23539728"
FT                   /id="VAR_075882"
FT   VARIANT         875
FT                   /note="H -> R (in NMTC2; does not affect the interaction
FT                   with ROBO1; slightly increased GTPase activator activity;
FT                   in SLIT2 and ROBO1-mediated inhibition of CDC42;
FT                   dbSNP:rs61754221)"
FT                   /evidence="ECO:0000269|PubMed:23539728"
FT                   /id="VAR_075883"
SQ   SEQUENCE   1085 AA;  124264 MW;  D7ED1F651344F0D9 CRC64;
     MSTPSRFKKD KEIIAEYESQ VKEIRAQLVE QQKCLEQQTE MRVQLLQDLQ DFFRKKAEIE
     TEYSRNLEKL AERFMAKTRS TKDHQQYKKD QNLLSPVNCW YLLLNQVRRE SKDHATLSDI
     YLNNVIMRFM QISEDSTRMF KKSKEIAFQL HEDLMKVLNE LYTVMKTYHM YHAESISAES
     KLKEAEKQEE KQIGRSGDPV FHIRLEERHQ RRSSVKKIEK MKEKRQAKYS ENKLKSIKAR
     NEYLLTLEAT NASVFKYYIH DLSDLIDCCD LGYHASLNRA LRTYLSAEYN LETSRHEGLD
     IIENAVDNLE PRSDKQRFME MYPAAFCPPM KFEFQSHMGD EVCQVSAQQP VQAELMLRYQ
     QLQSRLATLK IENEEVKKTT EATLQTIQDM VTIEDYDVSE CFQHSRSTES VKSTVSETYL
     SKPSIAKRRA NQQETEQFYF MKLREYLEGS NLITKLQAKH DLLQRTLGEG HRAEYMTTRP
     PNVPPKPQKH RKSRPRSQYN TKLFNGDLET FVKDSGQVIP LIVESCIRFI NLYGLQHQGI
     FRVSGSQVEV NDIKNSFERG ENPLADDQSN HDINSVAGVL KLYFRGLENP LFPKERFNDL
     ISCIRIDNLY ERALHIRKLL LTLPRSVLIV MRYLFAFLNH LSQYSDENMM DPYNLAICFG
     PTLMPVPEIQ DQVSCQAHVN EIIKTIIIHH ETIFPDAKEL DGPVYEKCMA GDDYCDSPYS
     EHGTLEEVDQ DAGTEPHTSE DECEPIEAIA KFDYVGRSAR ELSFKKGASL LLYHRASEDW
     WEGRHNGIDG LVPHQYIVVQ DMDDTFSDTL SQKADSEASS GPVTEDKSSS KDMNSPTDRH
     PDGYLARQRK RGEPPPPVRR PGRTSDGHCP LHPPHALSNS SVDLGSPSLA SHPRGLLQNR
     GLNNDSPERR RRPGHGSLTN ISRHDSLKKI DSPPIRRSTS SGQYTGFNDH KPLDPETIAQ
     DIEETMNTAL NELRELERQS TAKHAPDVVL DTLEQVKNSP TPATSTESLS PLHNVALRSS
     EPQIRRSTSS SSDTMSTFKP MVAPRMGVQL KPPALRPKPA VLPKTNPTIG PAPPPQGPTD
     KSCTM
//