GMIP_HUMAN
ID GMIP_HUMAN Reviewed; 970 AA.
AC Q9P107; A0AVN9; B7ZLZ0;
DT 29-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 22-JUL-2008, sequence version 2.
DT 03-AUG-2022, entry version 159.
DE RecName: Full=GEM-interacting protein;
DE Short=GMIP;
GN Name=GMIP;
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), FUNCTION, AND INTERACTION WITH GEM.
RC TISSUE=Leukemia;
RX PubMed=12093360; DOI=10.1042/bj20020829;
RA Aresta S., de Tand-Heim M.-F., Beranger F., de Gunzburg J.;
RT "A novel Rho GTPase-activating-protein interacts with Gem, a member of the
RT Ras superfamily of GTPases.";
RL Biochem. J. 367:57-65(2002).
RN [2]
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Brain;
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 [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=16964243; DOI=10.1038/nbt1240;
RA Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
RT "A probability-based approach for high-throughput protein phosphorylation
RT analysis and site localization.";
RL Nat. Biotechnol. 24:1285-1292(2006).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Platelet;
RX PubMed=18088087; DOI=10.1021/pr0704130;
RA Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J.,
RA Schuetz C., Walter U., Gambaryan S., Sickmann A.;
RT "Phosphoproteome of resting human platelets.";
RL J. Proteome Res. 7:526-534(2008).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-234 AND SER-243, AND
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 [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-234, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19369195; DOI=10.1074/mcp.m800588-mcp200;
RA Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,
RA Mann M., Daub H.;
RT "Large-scale proteomics analysis of the human kinome.";
RL Mol. Cell. Proteomics 8:1751-1764(2009).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-234, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [11]
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 [12]
RP IDENTIFICATION BY 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 [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-19; SER-234; SER-437;
RP SER-441; THR-660; SER-885; SER-907; SER-914; SER-919 AND SER-923, 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 [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-231, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [15]
RP X-RAY CRYSTALLOGRAPHY (2.40 ANGSTROMS) OF 80-357.
RG Structural genomics consortium (SGC);
RT "Crystal structure of the N-terminal domain of the GEM interacting
RT protein.";
RL Submitted (MAR-2011) to the PDB data bank.
CC -!- FUNCTION: Stimulates, in vitro and in vivo, the GTPase activity of
CC RhoA. {ECO:0000269|PubMed:12093360}.
CC -!- SUBUNIT: Interacts with GEM through its N-terminal.
CC {ECO:0000269|PubMed:12093360}.
CC -!- INTERACTION:
CC Q9P107; Q92619: ARHGAP45; NbExp=3; IntAct=EBI-11603420, EBI-2825900;
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9P107-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9P107-2; Sequence=VSP_056142;
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DR EMBL; AF132541; AAF61330.1; -; mRNA.
DR EMBL; AC011458; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471106; EAW84839.1; -; Genomic_DNA.
DR EMBL; BC126436; AAI26437.1; -; mRNA.
DR EMBL; BC144142; AAI44143.1; -; mRNA.
DR CCDS; CCDS12408.1; -. [Q9P107-1]
DR CCDS; CCDS74318.1; -. [Q9P107-2]
DR PIR; D59435; D59435.
DR RefSeq; NP_001275927.1; NM_001288998.1.
DR RefSeq; NP_001275928.1; NM_001288999.1. [Q9P107-2]
DR RefSeq; NP_057657.2; NM_016573.3. [Q9P107-1]
DR PDB; 3QWE; X-ray; 2.40 A; A=80-357.
DR PDBsum; 3QWE; -.
DR AlphaFoldDB; Q9P107; -.
DR SMR; Q9P107; -.
DR BioGRID; 119442; 29.
DR IntAct; Q9P107; 9.
DR STRING; 9606.ENSP00000203556; -.
DR iPTMnet; Q9P107; -.
DR PhosphoSitePlus; Q9P107; -.
DR BioMuta; GMIP; -.
DR DMDM; 212286192; -.
DR EPD; Q9P107; -.
DR jPOST; Q9P107; -.
DR MassIVE; Q9P107; -.
DR MaxQB; Q9P107; -.
DR PaxDb; Q9P107; -.
DR PeptideAtlas; Q9P107; -.
DR PRIDE; Q9P107; -.
DR ProteomicsDB; 83629; -. [Q9P107-1]
DR Antibodypedia; 61622; 82 antibodies from 17 providers.
DR DNASU; 51291; -.
DR Ensembl; ENST00000203556.9; ENSP00000203556.3; ENSG00000089639.11. [Q9P107-1]
DR Ensembl; ENST00000587238.5; ENSP00000467054.1; ENSG00000089639.11. [Q9P107-2]
DR GeneID; 51291; -.
DR KEGG; hsa:51291; -.
DR MANE-Select; ENST00000203556.9; ENSP00000203556.3; NM_016573.4; NP_057657.2.
DR UCSC; uc002nnd.5; human. [Q9P107-1]
DR CTD; 51291; -.
DR DisGeNET; 51291; -.
DR GeneCards; GMIP; -.
DR HGNC; HGNC:24852; GMIP.
DR HPA; ENSG00000089639; Tissue enhanced (bone marrow, lymphoid tissue).
DR MIM; 609694; gene.
DR neXtProt; NX_Q9P107; -.
DR OpenTargets; ENSG00000089639; -.
DR PharmGKB; PA134963566; -.
DR VEuPathDB; HostDB:ENSG00000089639; -.
DR eggNOG; KOG1453; Eukaryota.
DR GeneTree; ENSGT00950000183110; -.
DR HOGENOM; CLU_006236_1_0_1; -.
DR InParanoid; Q9P107; -.
DR OMA; QYMLGLD; -.
DR PhylomeDB; Q9P107; -.
DR TreeFam; TF351450; -.
DR PathwayCommons; Q9P107; -.
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; Q9P107; -.
DR SIGNOR; Q9P107; -.
DR BioGRID-ORCS; 51291; 23 hits in 1083 CRISPR screens.
DR ChiTaRS; GMIP; human.
DR EvolutionaryTrace; Q9P107; -.
DR GenomeRNAi; 51291; -.
DR Pharos; Q9P107; Tbio.
DR PRO; PR:Q9P107; -.
DR Proteomes; UP000005640; Chromosome 19.
DR RNAct; Q9P107; protein.
DR Bgee; ENSG00000089639; Expressed in granulocyte and 139 other tissues.
DR ExpressionAtlas; Q9P107; baseline and differential.
DR Genevisible; Q9P107; HS.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005886; C:plasma membrane; IDA:HPA.
DR GO; GO:0005096; F:GTPase activator activity; IDA:HGNC-UCL.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0090630; P:activation of GTPase activity; IBA:GO_Central.
DR GO; GO:0035556; P:intracellular signal transduction; IDA:HGNC-UCL.
DR GO; GO:0034260; P:negative regulation of GTPase activity; IDA:BHF-UCL.
DR GO; GO:0051056; P:regulation of small GTPase mediated signal transduction; TAS:Reactome.
DR Gene3D; 1.10.555.10; -; 1.
DR Gene3D; 1.20.1270.60; -; 1.
DR InterPro; IPR027267; AH/BAR_dom_sf.
DR InterPro; IPR046349; C1-like_sf.
DR InterPro; IPR031160; F_BAR.
DR InterPro; IPR002219; PE/DAG-bd.
DR InterPro; IPR008936; Rho_GTPase_activation_prot.
DR InterPro; IPR000198; RhoGAP_dom.
DR Pfam; PF00620; RhoGAP; 1.
DR SMART; SM00109; C1; 1.
DR SMART; SM00324; RhoGAP; 1.
DR SUPFAM; SSF103657; SSF103657; 1.
DR SUPFAM; SSF48350; SSF48350; 1.
DR SUPFAM; SSF57889; SSF57889; 1.
DR PROSITE; PS51741; F_BAR; 1.
DR PROSITE; PS50238; RHOGAP; 1.
DR PROSITE; PS00479; ZF_DAG_PE_1; 1.
DR PROSITE; PS50081; ZF_DAG_PE_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Coiled coil; GTPase activation;
KW Metal-binding; Phosphoprotein; Reference proteome; Zinc; Zinc-finger.
FT CHAIN 1..970
FT /note="GEM-interacting protein"
FT /id="PRO_0000056725"
FT DOMAIN 81..344
FT /note="F-BAR"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01077"
FT DOMAIN 554..757
FT /note="Rho-GAP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00172"
FT ZN_FING 493..537
FT /note="Phorbol-ester/DAG-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00226"
FT REGION 44..76
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 224..263
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 377..478
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 762..878
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 897..932
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 54..68
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 224..247
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 248..263
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 425..457
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 768..804
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 812..830
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 852..866
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 19
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 71
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6PGG2"
FT MOD_RES 231
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 234
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19369195, ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 243
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 437
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 441
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 660
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 885
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 907
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 914
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 919
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 923
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT VAR_SEQ 442..467
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_056142"
FT VARIANT 641
FT /note="D -> N (in dbSNP:rs12003)"
FT /id="VAR_044518"
FT CONFLICT 666
FT /note="E -> D (in Ref. 1; AAF61330)"
FT /evidence="ECO:0000305"
FT CONFLICT 773
FT /note="S -> F (in Ref. 1; AAF61330)"
FT /evidence="ECO:0000305"
FT CONFLICT 870
FT /note="V -> C (in Ref. 1; AAF61330)"
FT /evidence="ECO:0000305"
FT HELIX 81..89
FT /evidence="ECO:0007829|PDB:3QWE"
FT HELIX 93..140
FT /evidence="ECO:0007829|PDB:3QWE"
FT HELIX 149..176
FT /evidence="ECO:0007829|PDB:3QWE"
FT HELIX 178..229
FT /evidence="ECO:0007829|PDB:3QWE"
FT HELIX 248..322
FT /evidence="ECO:0007829|PDB:3QWE"
FT HELIX 324..335
FT /evidence="ECO:0007829|PDB:3QWE"
FT TURN 336..338
FT /evidence="ECO:0007829|PDB:3QWE"
FT HELIX 343..351
FT /evidence="ECO:0007829|PDB:3QWE"
SQ SEQUENCE 970 AA; 106683 MW; 8163EF62F85EB2EE CRC64;
MDAAEPGLPP GPEGRKRYSD IFRSLDNLEI SLGNVTLEML AGDPLLSEDP EPDKTPTATV
TNEASCWSGP SPEGPVPLTG EELDLRLIRT KGGVDAALEY AKTWSRYAKE LLAWTEKRAS
YELEFAKSTM KIAEAGKVSI QQQSHMPLQY IYTLFLEHDL SLGTLAMETV AQQKRDYYQP
LAAKRTEIEK WRKEFKEQWM KEQKRMNEAV QALRRAQLQY VQRSEDLRAR SQGSPEDSAP
QASPGPSKQQ ERRRRSREEA QAKAQEAEAL YQACVREANA RQQDLEIAKQ RIVSHVRKLV
FQGDEVLRRV TLSLFGLRGA QAERGPRAFA ALAECCAPFE PGQRYQEFVR ALRPEAPPPP
PPAFSFQEFL PSLNSSPLDI RKKLSGPLPP RLDENSAEPG PWEDPGTGWR WQGTPGPTPG
SDVDSVGGGS ESRSLDSPTS SPGAGTRQLV KASSTGTESS DDFEERDPDL GDGLENGLGS
PFGKWTLSSA AQTHQLRRLR GPAKCRECEA FMVSGTECEE CFLTCHKRCL ETLLILCGHR
RLPARTPLFG VDFLQLPRDF PEEVPFVVTK CTAEIEHRAL DVQGIYRVSG SRVRVERLCQ
AFENGRALVE LSGNSPHDVS SVLKRFLQEL TEPVIPFHLY DAFISLAKTL HADPGDDPGT
PSPSPEVIRS LKTLLVQLPD SNYNTLRHLV AHLFRVAARF MENKMSANNL GIVFGPTLLR
PPDGPRAASA IPVTCLLDSG HQAQLVEFLI VHYEQIFGMD ELPQATEPPP QDSSPAPGPL
TTSSQPPPPH LDPDSQPPVL ASDPGPDPQH HSTLEQHPTA TPTEIPTPQS DQREDVAEDT
KDGGGEVSSQ GPEDSLLGTQ SRGHFSRQPV KYPRGGVRPV THQLSSLALV ASKLCEETPI
TSVPRGSLRG RGPSPAAASP EGSPLRRTPL PKHFEITQET ARLLSKLDSE AVPRATCCPD
VQPEEAEDHL
