GBPC_DICDI
ID GBPC_DICDI Reviewed; 2631 AA.
AC Q8MVR1; Q54F62;
DT 25-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 120.
DE RecName: Full=Cyclic GMP-binding protein C;
DE EC=2.7.11.1;
DE AltName: Full=Ras guanine nucleotide exchange factor T;
DE AltName: Full=RasGEF domain-containing protein T;
GN Name=gbpC; Synonyms=gefT, rasGEFT; ORFNames=DDB_G0291079;
OS Dictyostelium discoideum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=44689;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND DEVELOPMENTAL STAGE.
RX PubMed=12011437; DOI=10.1073/pnas.102167299;
RA Goldberg J.M., Bosgraaf L., Van Haastert P.J.M., Smith J.L.;
RT "Identification of four candidate cGMP targets in Dictyostelium.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:6749-6754(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4;
RX PubMed=15875012; DOI=10.1038/nature03481;
RA Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT "The genome of the social amoeba Dictyostelium discoideum.";
RL Nature 435:43-57(2005).
RN [3]
RP FUNCTION.
RX PubMed=12198158; DOI=10.1093/emboj/cdf438;
RA Bosgraaf L., Russcher H., Smith J.L., Wessels D., Soll D.R.,
RA Van Haastert P.J.M.;
RT "A novel cGMP signalling pathway mediating myosin phosphorylation and
RT chemotaxis in Dictyostelium.";
RL EMBO J. 21:4560-4570(2002).
RN [4]
RP DEVELOPMENTAL STAGE.
RX PubMed=16086850; DOI=10.1186/gb-2005-6-8-r68;
RA Wilkins A., Szafranski K., Fraser D.J., Bakthavatsalam D., Mueller R.,
RA Fisher P.R., Gloeckner G., Eichinger L., Noegel A.A., Insall R.H.;
RT "The Dictyostelium genome encodes numerous RasGEFs with multiple biological
RT roles.";
RL Genome Biol. 6:R68.1-R68.12(2005).
RN [5]
RP FUNCTION.
RX PubMed=15827084; DOI=10.1242/jcs.02317;
RA Bosgraaf L., Waijer A., Engel R., Visser A.J.W.G., Wessels D., Soll D.,
RA van Haastert P.J.M.;
RT "RasGEF-containing proteins GbpC and GbpD have differential effects on cell
RT polarity and chemotaxis in Dictyostelium.";
RL J. Cell Sci. 118:1899-1910(2005).
RN [6]
RP FUNCTION.
RX PubMed=16546177; DOI=10.1016/j.febslet.2006.03.008;
RA Goldberg J.M., Wolpin E.S., Bosgraaf L., Clarkson B.K.,
RA Van Haastert P.J.M., Smith J.L.;
RT "Myosin light chain kinase A is activated by cGMP-dependent and cGMP-
RT independent pathways.";
RL FEBS Lett. 580:2059-2064(2006).
RN [7]
RP FUNCTION, AND MUTAGENESIS OF LYS-342 AND LYS-905.
RX PubMed=18703517; DOI=10.1074/jbc.m804265200;
RA van Egmond W.N., Kortholt A., Plak K., Bosgraaf L., Bosgraaf S.,
RA Keizer-Gunnink I., van Haastert P.J.M.;
RT "Intramolecular activation mechanism of the dictyostelium LRRK2-homolog
RT Roco protein GbpC.";
RL J. Biol. Chem. 283:30412-30420(2008).
RN [8]
RP FUNCTION.
RX PubMed=18299345; DOI=10.1083/jcb.200709180;
RA Veltman D.M., Keizer-Gunnik I., Van Haastert P.J.M.;
RT "Four key signaling pathways mediating chemotaxis in Dictyostelium
RT discoideum.";
RL J. Cell Biol. 180:747-753(2008).
CC -!- FUNCTION: Promotes the exchange of Ras-bound GDP by GTP (By
CC similarity). Required for cyclic GMP-mediated chemotaxis, polarity.
CC Plays a key role in cyclic AMP-induced myosin II translocation to the
CC cortex. Also involved in the phosphorylation of mlkA and mlcR, either
CC directly or via an intermediate kinase. {ECO:0000250,
CC ECO:0000269|PubMed:12198158, ECO:0000269|PubMed:15827084,
CC ECO:0000269|PubMed:16546177, ECO:0000269|PubMed:18299345,
CC ECO:0000269|PubMed:18703517}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
CC [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
CC threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
CC Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC EC=2.7.11.1;
CC -!- DEVELOPMENTAL STAGE: Increases dramatically after starvation is
CC initiated with a peak between 4-12 hours. {ECO:0000269|PubMed:12011437,
CC ECO:0000269|PubMed:16086850}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. TKL Ser/Thr
CC protein kinase family. ROCO subfamily. {ECO:0000305}.
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; AF481923; AAM34041.1; -; Genomic_DNA.
DR EMBL; AAFI02000175; EAL61887.1; -; Genomic_DNA.
DR RefSeq; XP_635392.1; XM_630300.1.
DR AlphaFoldDB; Q8MVR1; -.
DR SMR; Q8MVR1; -.
DR STRING; 44689.DDB0191359; -.
DR PaxDb; Q8MVR1; -.
DR EnsemblProtists; EAL61887; EAL61887; DDB_G0291079.
DR GeneID; 8627976; -.
DR KEGG; ddi:DDB_G0291079; -.
DR dictyBase; DDB_G0291079; gbpC.
DR eggNOG; KOG0192; Eukaryota.
DR eggNOG; KOG0619; Eukaryota.
DR eggNOG; KOG3417; Eukaryota.
DR HOGENOM; CLU_227708_0_0_1; -.
DR InParanoid; Q8MVR1; -.
DR OMA; KEYKEMP; -.
DR PRO; PR:Q8MVR1; -.
DR Proteomes; UP000002195; Chromosome 5.
DR GO; GO:0005938; C:cell cortex; IDA:dictyBase.
DR GO; GO:0031252; C:cell leading edge; IDA:dictyBase.
DR GO; GO:0005737; C:cytoplasm; IDA:dictyBase.
DR GO; GO:0005886; C:plasma membrane; IMP:dictyBase.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0030553; F:cGMP binding; IDA:dictyBase.
DR GO; GO:0005525; F:GTP binding; IDA:dictyBase.
DR GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; IDA:dictyBase.
DR GO; GO:0005543; F:phospholipid binding; IDA:dictyBase.
DR GO; GO:0004672; F:protein kinase activity; IBA:GO_Central.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0032060; P:bleb assembly; IGI:dictyBase.
DR GO; GO:0031589; P:cell-substrate adhesion; IMP:dictyBase.
DR GO; GO:0019934; P:cGMP-mediated signaling; IDA:dictyBase.
DR GO; GO:0007163; P:establishment or maintenance of cell polarity; IMP:dictyBase.
DR GO; GO:0045860; P:positive regulation of protein kinase activity; IMP:dictyBase.
DR GO; GO:0046579; P:positive regulation of Ras protein signal transduction; IDA:dictyBase.
DR GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR GO; GO:0050920; P:regulation of chemotaxis; IMP:dictyBase.
DR GO; GO:0051602; P:response to electrical stimulus; IMP:dictyBase.
DR GO; GO:0007165; P:signal transduction; IBA:GO_Central.
DR GO; GO:0007264; P:small GTPase mediated signal transduction; IEA:InterPro.
DR CDD; cd00038; CAP_ED; 2.
DR CDD; cd06224; REM; 1.
DR Gene3D; 1.10.10.10; -; 2.
DR Gene3D; 1.10.840.10; -; 1.
DR Gene3D; 2.30.29.30; -; 1.
DR Gene3D; 2.60.120.10; -; 2.
DR Gene3D; 3.40.50.300; -; 1.
DR Gene3D; 3.80.10.10; -; 1.
DR InterPro; IPR018490; cNMP-bd-like.
DR InterPro; IPR000595; cNMP-bd_dom.
DR InterPro; IPR032171; COR.
DR InterPro; IPR000591; DEP_dom.
DR InterPro; IPR004182; GRAM.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR001611; Leu-rich_rpt.
DR InterPro; IPR003591; Leu-rich_rpt_typical-subtyp.
DR InterPro; IPR032675; LRR_dom_sf.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR000651; Ras-like_Gua-exchang_fac_N.
DR InterPro; IPR023578; Ras_GEF_dom_sf.
DR InterPro; IPR001895; RASGEF_cat_dom.
DR InterPro; IPR036964; RASGEF_cat_dom_sf.
DR InterPro; IPR014710; RmlC-like_jellyroll.
DR InterPro; IPR020859; ROC_dom.
DR InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR Pfam; PF00027; cNMP_binding; 2.
DR Pfam; PF16095; COR; 1.
DR Pfam; PF00610; DEP; 1.
DR Pfam; PF02893; GRAM; 1.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR Pfam; PF00617; RasGEF; 1.
DR Pfam; PF00618; RasGEF_N; 1.
DR PRINTS; PR00109; TYRKINASE.
DR SMART; SM00049; DEP; 1.
DR SMART; SM00568; GRAM; 1.
DR SMART; SM00369; LRR_TYP; 2.
DR SMART; SM00147; RasGEF; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF46785; SSF46785; 1.
DR SUPFAM; SSF48366; SSF48366; 1.
DR SUPFAM; SSF51206; SSF51206; 2.
DR SUPFAM; SSF52540; SSF52540; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS50042; CNMP_BINDING_3; 2.
DR PROSITE; PS50186; DEP; 1.
DR PROSITE; PS51450; LRR; 4.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
DR PROSITE; PS50009; RASGEF_CAT; 1.
DR PROSITE; PS50212; RASGEF_NTER; 1.
DR PROSITE; PS51424; ROC; 1.
PE 1: Evidence at protein level;
KW ATP-binding; cGMP; cGMP-binding; GTP-binding;
KW Guanine-nucleotide releasing factor; Kinase; Leucine-rich repeat;
KW Nucleotide-binding; Reference proteome; Repeat;
KW Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..2631
FT /note="Cyclic GMP-binding protein C"
FT /id="PRO_0000353103"
FT REPEAT 170..194
FT /note="LRR 1"
FT REPEAT 196..217
FT /note="LRR 2"
FT REPEAT 218..240
FT /note="LRR 3"
FT REPEAT 242..262
FT /note="LRR 4"
FT REPEAT 263..285
FT /note="LRR 5"
FT REPEAT 287..308
FT /note="LRR 6"
FT DOMAIN 323..515
FT /note="Roc"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00758"
FT DOMAIN 878..1172
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT DOMAIN 1366..1539
FT /note="N-terminal Ras-GEF"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00135"
FT DOMAIN 1620..1706
FT /note="DEP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00066"
FT DOMAIN 1708..1971
FT /note="Ras-GEF"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00168"
FT DOMAIN 2354..2414
FT /note="GRAM"
FT REGION 1225..1263
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1387..1418
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1989..2013
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2142..2180
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2192..2239
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2263..2346
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2143..2180
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2206..2223
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2224..2239
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2263..2283
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2323..2346
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 1023
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 336..343
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00758"
FT BINDING 402..406
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00758"
FT BINDING 458..461
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00758"
FT BINDING 884..892
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 905
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 2014..2133
FT /ligand="a nucleoside 3',5'-cyclic phosphate"
FT /ligand_id="ChEBI:CHEBI:58464"
FT /ligand_label="1"
FT BINDING 2490..2616
FT /ligand="a nucleoside 3',5'-cyclic phosphate"
FT /ligand_id="ChEBI:CHEBI:58464"
FT /ligand_label="2"
FT MUTAGEN 342
FT /note="K->N: Loss of nucleotide binding activity."
FT /evidence="ECO:0000269|PubMed:18703517"
FT MUTAGEN 905
FT /note="K->N: Loss of chemotax."
FT /evidence="ECO:0000269|PubMed:18703517"
SQ SEQUENCE 2631 AA; 294127 MW; 5BB7AABD0A637701 CRC64;
MSQKQKPIRF QDYQFTATKD EAYGRSDRYV KQFLNKNLLK KKDGTLGTAE ELLTLIQQSN
INVVTASTGG AAMGAMLNHT VSTINLTGSG SVPTYNPSDN RNSGSHVITS TNSVISNSSI
SSTGVINNNI NNNSNINSNT GTTTTTISLP NNTEIKTALV STGSQNASDT AQIDIEFHLS
YTQLVTLPPS IFSLIWIQKL VLTHHNIKTL SEDIGKLQQL QVLVLENNRL INLPQSIGDL
VNLKRLEVDN NHLVSLCSLE RLSKLEVLSV NNNKLTLLPT SIASLSSLKT LNIKSNPIIT
PPSTVVSKGL KDIVSFLREL ETGARPCLRS KLVVLGDPGV GKTSVVQCMK GKKKKTNVTS
SSINIGGSSG SEVGIEIDQY DFDVVFDEDD KKRRVITLST WDIANQDVYF ASSQLFDSER
SVYIVVFNLN NDDFSAIEYW LHCIMSTSPN SPIVLVGTHI DAFENLNVVN AVLESVASRF
QKRFTNIQAI ISVSCTTGYD VDKLRQLIED IIKTQPYLKE KVPSSFFTLE EALIEVKKKR
IPPVMMWQEY INLANICNLK DSVQIQRATE FLHNIGSIVY FNDLNSSTVG KMVILDQQWI
INCMSSLITS KLLINNCNGI VRQSDLELVW KAPTYPEHLH PALLSIMQAF EICRSLSPSD
LVRPEEVNEK EVMGDRNLVP NLLSDNTNIV AQWDDFIDPD TILLNRQYHL PFLPEKFFGK
LIIHLMNFTK VESCQKRAVI LRNQDNHEAL IELKTIKDNK DGTFKKILTV DVRGLVSPVS
LLRIVTDTIE SLFSQWYKLD IKRYISCYEC AILYDRNPTL FTIEECELAV IDGKTVLTCN
QKSDSDRVST SHRLKLDILA PDISMVDIPI PRFNLSEVKI NKEVGRGAFG IVYEAEWMSE
WIALKKLLLP SSTDTTNLNG NGEVMVYDDP DQLIEDRLRV FREFRHEVYY MSGLNHPNVM
KISGFCIQPL CMALEYVRYG SLYSLLSNSS IEISWGLRLQ IASEIAKGMQ HLHSHNPPVI
HRDLKSPNIL LNGITEGQNS VATIIDFGTS TALYGGAALI RCVDQPLWLG PEVLAGTAYS
EPSDVYSFGI ILWELYTRAH PFDEFQFGQW MSKLEDEIIR GLRPTIPPTC PPEYVELIQS
CWTHEPNSRP TFTSIVEILG QIKKKFAPLP FTHPPHIRNM MRKSRSSSIS EAMLPSNLLH
LNLNGINNNN NNSNNNNNSI PVTTISLTSS GTSPTNSPVG GLLSQSLTQP ITSGGSTSGI
LSTSVNRDNS SLVSASSLGN NTSTSSLASL VSNNSGLHHS PSASDGLNDY YGADNNNNNN
DSTMDFFQDI FTEEENEQPY PFADDDQQKG ILFGFDEEQT NPSASSVSII IAATMAKMIE
MMTKGESSAT LKSEHISTRR RSDTAGKNGV PPHWRNSVPL STNSSTTLDE TFIDDFIYVY
RSFTTPRNIF KLLVRRFFGP RHTDKVDTFT IKKFEQKKAA IRQGIAVFLR KWVADITELE
FRQEEFWLYH NTVAFTKQFI ASEFPTIATQ IYGTLTTHED EVNLTNQRFL QIAFSESEIQ
IDRAMSSMQL TTPKPFRSQK NLANSYNSQS GGGDSSFYYQ PSSNDVSRVF LNLATGMRDP
LLGITVKEKK FKKDKVSTLC CSGSEIIDWI TKCMPIKREE ASILVLDMLM KQFFIQISDD
GIPISNQKGT NPTFSDSPTS FYMFLEDDPE LIARQYTFLE LKYLQNIHPR ELLGFSVGLV
MPNENEKDPE KWRQSNFPHI YDYFRWFNKM TMLVSTEILR QRDIKQRASI IEKYISIALE
YLSLWNFNGI MQVLSSLHSE PISRLSATWA KVSQRSMDCF YELSRLMLPE SNYLPLRTAL
ASQKPNTIIQ ASPLYPNISA YMVHTVCPTI PFLGALIADL SQTCTENPTF ISSGGEKMIN
ILRVKRLSKK MKMFKEYKEM PTQYLPALTT IPLQYYEHYV NDLKALDSLQ IDRLSDIERK
LEIICEKNGT TNDDKEKGDE NGGGLTSSNF FGNGSDELTE RDWTILLTNA SVIAYNRGDV
VMEENAINTH LYRIKSGAIS VEKKDKEGIN CKVATMFAPK MFGEMSFLGN KTTARLTVDE
ESDLYVMDIP FLNNLFNGHP RLGAKFYKIM ANQLAIRLKN LPWSKPKNTT GGSSSSNQSA
GPDNILGTTP TGISSSGGGL TSLLNQNLSS IMSLSNSNTP PASPRVMTTP TLPSPPAPLQ
SPPTSGISSP TTTTSTTTDQ QKINNTIFQN VHPTINVHRT SSSANLVSPH GRPSNSGFGH
SSGGERTINK DPHQRDSGSM DKPILSLGSG GTPRGDGARS GSISYLGRTQ TSTSPLNEGL
SGGQQPVMKK NDQEFCQRFA LVDEIVIKDY PCSLNRSGRL YISQQHVCFY SKFFGYKTKK
VIPFKNIDKL ICINVNQIEL TRLKNTVPSN YRLTFQTGKD REDAFSMIHI LWDSSKVSNS
SSDEIKNKLA AERKKVNNLT LKTRSNKNKG DELTKEDWEL IGCEGSRSST FKKDEVIIRE
GERMQKIFQI GKGVCRIEKS VPVAPGSSEM KKVVLGTMKQ DDTFGEITYL LNGETTADVI
ADTDQTEVYT IEGQFVNILF DLNPALASKW FKYLATALNK TLIERESQLY A
