ID   MRCKG_HUMAN             Reviewed;        1551 AA.
AC   Q6DT37; O00565;
DT   08-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT   02-MAR-2010, sequence version 2.
DT   27-MAR-2024, entry version 172.
DE   RecName: Full=Serine/threonine-protein kinase MRCK gamma;
DE            EC=2.7.11.1;
DE   AltName: Full=CDC42-binding protein kinase gamma;
DE   AltName: Full=DMPK-like gamma;
DE   AltName: Full=Myotonic dystrophy kinase-related CDC42-binding kinase gamma;
DE            Short=MRCK gamma;
DE            Short=MRCKG;
DE            Short=Myotonic dystrophy protein kinase-like gamma;
DE   AltName: Full=Myotonic dystrophy protein kinase-like alpha;
GN   Name=CDC42BPG {ECO:0000312|HGNC:HGNC:29829}; Synonyms=DMPK2;
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] {ECO:0000305, ECO:0000312|EMBL:AAT67172.1}
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, AND TISSUE
RP   SPECIFICITY.
RC   TISSUE=Colon {ECO:0000269|PubMed:15194684};
RX   PubMed=15194684; DOI=10.1074/jbc.m405252200;
RA   Ng Y., Tan I., Lim L., Leung T.;
RT   "Expression of the human myotonic dystrophy kinase-related Cdc42-binding
RT   kinase gamma is regulated by promoter DNA methylation and Sp1 binding.";
RL   J. Biol. Chem. 279:34156-34164(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16554811; DOI=10.1038/nature04632;
RA   Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K.,
RA   Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F., Bloom T.,
RA   Bruford E., Chang J.L., Cuomo C.A., Eichler E., FitzGerald M.G.,
RA   Jaffe D.B., LaButti K., Nicol R., Park H.-S., Seaman C., Sougnez C.,
RA   Yang X., Zimmer A.R., Zody M.C., Birren B.W., Nusbaum C., Fujiyama A.,
RA   Hattori M., Rogers J., Lander E.S., Sakaki Y.;
RT   "Human chromosome 11 DNA sequence and analysis including novel gene
RT   identification.";
RL   Nature 440:497-500(2006).
RN   [3] {ECO:0000305, ECO:0000312|EMBL:CAA73006.1}
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 113-401.
RX   PubMed=9341881; DOI=10.1007/s004390050562;
RA   Kedra D., Seroussi E., Fransson I., Trifunovic J., Clark M.,
RA   Lagercrantz J., Blennow E., Mehlin H., Dumanski J.;
RT   "The germinal centre kinase gene and a novel CDC25-like gene are located in
RT   the vicinity of the PYGM gene on 11q13.";
RL   Hum. Genet. 100:611-619(1997).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1482, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=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   [5]
RP   VARIANTS [LARGE SCALE ANALYSIS] LEU-168; PHE-280; PRO-362 AND ASP-537.
RX   PubMed=17344846; DOI=10.1038/nature05610;
RA   Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C., Bignell G.,
RA   Davies H., Teague J., Butler A., Stevens C., Edkins S., O'Meara S.,
RA   Vastrik I., Schmidt E.E., Avis T., Barthorpe S., Bhamra G., Buck G.,
RA   Choudhury B., Clements J., Cole J., Dicks E., Forbes S., Gray K.,
RA   Halliday K., Harrison R., Hills K., Hinton J., Jenkinson A., Jones D.,
RA   Menzies A., Mironenko T., Perry J., Raine K., Richardson D., Shepherd R.,
RA   Small A., Tofts C., Varian J., Webb T., West S., Widaa S., Yates A.,
RA   Cahill D.P., Louis D.N., Goldstraw P., Nicholson A.G., Brasseur F.,
RA   Looijenga L., Weber B.L., Chiew Y.-E., DeFazio A., Greaves M.F.,
RA   Green A.R., Campbell P., Birney E., Easton D.F., Chenevix-Trench G.,
RA   Tan M.-H., Khoo S.K., Teh B.T., Yuen S.T., Leung S.Y., Wooster R.,
RA   Futreal P.A., Stratton M.R.;
RT   "Patterns of somatic mutation in human cancer genomes.";
RL   Nature 446:153-158(2007).
CC   -!- FUNCTION: May act as a downstream effector of CDC42 in cytoskeletal
CC       reorganization. Contributes to the actomyosin contractility required
CC       for cell invasion, through the regulation of MYPT1 and thus MLC2
CC       phosphorylation (By similarity). {ECO:0000250|UniProtKB:Q5VT25,
CC       ECO:0000269|PubMed:15194684}.
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         Evidence={ECO:0000269|PubMed:15194684};
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; Evidence={ECO:0000269|PubMed:15194684};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000269|PubMed:15194684};
CC   -!- ACTIVITY REGULATION: Maintained in an inactive, closed conformation by
CC       an interaction between the kinase domain and the negative
CC       autoregulatory C-terminal coiled-coil region. Agonist binding to the
CC       phorbol ester binding site disrupts this, releasing the kinase domain
CC       to allow N-terminus-mediated dimerization and kinase activation by
CC       transautophosphorylation (By similarity).
CC       {ECO:0000250|UniProtKB:Q5VT25}.
CC   -!- SUBUNIT: Homodimer and homotetramer via the coiled coil regions.
CC       Interacts tightly with GTP-bound but not GDP-bound CDC42 (By
CC       similarity). {ECO:0000250}.
CC   -!- INTERACTION:
CC       Q6DT37; Q9UHD2: TBK1; NbExp=3; IntAct=EBI-689124, EBI-356402;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:15194684}.
CC       Note=Concentrates at the leading edge of cells.
CC   -!- TISSUE SPECIFICITY: Expressed in heart and skeletal muscle.
CC       {ECO:0000269|PubMed:15194684}.
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. AGC Ser/Thr
CC       protein kinase family. DMPK subfamily. {ECO:0000305}.
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DR   EMBL; AY648038; AAT67172.1; -; mRNA.
DR   EMBL; AP001187; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; Y12337; CAA73006.1; -; mRNA.
DR   CCDS; CCDS31601.1; -.
DR   RefSeq; NP_059995.2; NM_017525.2.
DR   AlphaFoldDB; Q6DT37; -.
DR   SMR; Q6DT37; -.
DR   BioGRID; 120719; 53.
DR   IntAct; Q6DT37; 7.
DR   MINT; Q6DT37; -.
DR   STRING; 9606.ENSP00000345133; -.
DR   BindingDB; Q6DT37; -.
DR   ChEMBL; CHEMBL5615; -.
DR   DrugBank; DB12010; Fostamatinib.
DR   DrugCentral; Q6DT37; -.
DR   iPTMnet; Q6DT37; -.
DR   PhosphoSitePlus; Q6DT37; -.
DR   BioMuta; CDC42BPG; -.
DR   DMDM; 290457650; -.
DR   CPTAC; non-CPTAC-5991; -.
DR   CPTAC; non-CPTAC-5992; -.
DR   EPD; Q6DT37; -.
DR   jPOST; Q6DT37; -.
DR   MassIVE; Q6DT37; -.
DR   MaxQB; Q6DT37; -.
DR   PaxDb; 9606-ENSP00000345133; -.
DR   PeptideAtlas; Q6DT37; -.
DR   ProteomicsDB; 66255; -.
DR   Pumba; Q6DT37; -.
DR   Antibodypedia; 15651; 41 antibodies from 16 providers.
DR   DNASU; 55561; -.
DR   Ensembl; ENST00000342711.6; ENSP00000345133.5; ENSG00000171219.9.
DR   GeneID; 55561; -.
DR   KEGG; hsa:55561; -.
DR   MANE-Select; ENST00000342711.6; ENSP00000345133.5; NM_017525.3; NP_059995.2.
DR   UCSC; uc001obs.5; human.
DR   AGR; HGNC:29829; -.
DR   CTD; 55561; -.
DR   DisGeNET; 55561; -.
DR   GeneCards; CDC42BPG; -.
DR   HGNC; HGNC:29829; CDC42BPG.
DR   HPA; ENSG00000171219; Tissue enhanced (brain, skin).
DR   MIM; 613991; gene.
DR   neXtProt; NX_Q6DT37; -.
DR   OpenTargets; ENSG00000171219; -.
DR   PharmGKB; PA134901493; -.
DR   VEuPathDB; HostDB:ENSG00000171219; -.
DR   eggNOG; KOG0612; Eukaryota.
DR   GeneTree; ENSGT01030000234517; -.
DR   HOGENOM; CLU_000288_140_3_1; -.
DR   InParanoid; Q6DT37; -.
DR   OMA; PWQHRIR; -.
DR   OrthoDB; 988261at2759; -.
DR   PhylomeDB; Q6DT37; -.
DR   TreeFam; TF313551; -.
DR   PathwayCommons; Q6DT37; -.
DR   SignaLink; Q6DT37; -.
DR   BioGRID-ORCS; 55561; 11 hits in 1183 CRISPR screens.
DR   ChiTaRS; CDC42BPG; human.
DR   GenomeRNAi; 55561; -.
DR   Pharos; Q6DT37; Tchem.
DR   PRO; PR:Q6DT37; -.
DR   Proteomes; UP000005640; Chromosome 11.
DR   RNAct; Q6DT37; Protein.
DR   Bgee; ENSG00000171219; Expressed in skin of abdomen and 97 other cell types or tissues.
DR   GO; GO:0031252; C:cell leading edge; IDA:UniProtKB.
DR   GO; GO:0034451; C:centriolar satellite; IDA:HPA.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005856; C:cytoskeleton; IBA:GO_Central.
DR   GO; GO:0005829; C:cytosol; IDA:HPA.
DR   GO; GO:0005524; F:ATP binding; IDA:UniProtKB.
DR   GO; GO:0000287; F:magnesium ion binding; IDA:UniProtKB.
DR   GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; IDA:UniProtKB.
DR   GO; GO:0030036; P:actin cytoskeleton organization; ISS:UniProtKB.
DR   GO; GO:0031032; P:actomyosin structure organization; IBA:GO_Central.
DR   GO; GO:0006468; P:protein phosphorylation; IDA:UniProtKB.
DR   CDD; cd20866; C1_MRCKgamma; 1.
DR   CDD; cd01243; PH_MRCK; 1.
DR   CDD; cd05597; STKc_DMPK_like; 1.
DR   Gene3D; 1.20.5.340; -; 1.
DR   Gene3D; 3.30.60.20; -; 1.
DR   Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR   InterPro; IPR000961; AGC-kinase_C.
DR   InterPro; IPR046349; C1-like_sf.
DR   InterPro; IPR001180; CNH_dom.
DR   InterPro; IPR000095; CRIB_dom.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR014930; Myotonic_dystrophy_kinase_coil.
DR   InterPro; IPR002219; PE/DAG-bd.
DR   InterPro; IPR011993; PH-like_dom_sf.
DR   InterPro; IPR001849; PH_domain.
DR   InterPro; IPR017892; Pkinase_C.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR008271; Ser/Thr_kinase_AS.
DR   PANTHER; PTHR22988; MYOTONIC DYSTROPHY S/T KINASE-RELATED; 1.
DR   PANTHER; PTHR22988:SF22; SERINE_THREONINE-PROTEIN KINASE MRCK GAMMA; 1.
DR   Pfam; PF00130; C1_1; 1.
DR   Pfam; PF00780; CNH; 1.
DR   Pfam; PF08826; DMPK_coil; 1.
DR   Pfam; PF00069; Pkinase; 1.
DR   Pfam; PF00433; Pkinase_C; 1.
DR   SMART; SM00109; C1; 1.
DR   SMART; SM00036; CNH; 1.
DR   SMART; SM00233; PH; 1.
DR   SMART; SM00133; S_TK_X; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF57889; Cysteine-rich domain; 1.
DR   SUPFAM; SSF50729; PH domain-like; 1.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   PROSITE; PS51285; AGC_KINASE_CTER; 1.
DR   PROSITE; PS50219; CNH; 1.
DR   PROSITE; PS50108; CRIB; 1.
DR   PROSITE; PS50003; PH_DOMAIN; 1.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
DR   PROSITE; PS00479; ZF_DAG_PE_1; 1.
DR   PROSITE; PS50081; ZF_DAG_PE_2; 1.
DR   Genevisible; Q6DT37; HS.
PE   1: Evidence at protein level;
KW   ATP-binding; Coiled coil; Cytoplasm; Kinase; Magnesium; Metal-binding;
KW   Nucleotide-binding; Phosphoprotein; Reference proteome;
KW   Serine/threonine-protein kinase; Transferase; Zinc; Zinc-finger.
FT   CHAIN           1..1551
FT                   /note="Serine/threonine-protein kinase MRCK gamma"
FT                   /id="PRO_0000086397"
FT   DOMAIN          71..337
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT                   ECO:0000269|PubMed:15194684"
FT   DOMAIN          338..408
FT                   /note="AGC-kinase C-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00618"
FT   DOMAIN          947..1066
FT                   /note="PH"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT   DOMAIN          1092..1366
FT                   /note="CNH"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00795"
FT   DOMAIN          1437..1450
FT                   /note="CRIB"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00057"
FT   ZN_FING         878..927
FT                   /note="Phorbol-ester/DAG-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00226"
FT   REGION          467..486
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          655..675
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          801..849
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          863..886
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1442..1551
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          406..678
FT                   /evidence="ECO:0000255"
FT   COILED          730..802
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        1460..1474
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1510..1537
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        195
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:P54265,
FT                   ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-
FT                   ProRule:PRU10027"
FT   BINDING         77..85
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:P54265,
FT                   ECO:0000255|PROSITE-ProRule:PRU00159"
FT   BINDING         100
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT                   ECO:0000269|PubMed:15194684"
FT   MOD_RES         216
FT                   /note="Phosphoserine; by autocatalysis"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         228
FT                   /note="Phosphoserine; by autocatalysis"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         234
FT                   /note="Phosphothreonine; by autocatalysis"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         1482
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   VARIANT         168
FT                   /note="P -> L (in dbSNP:rs34454471)"
FT                   /evidence="ECO:0000269|PubMed:17344846"
FT                   /id="VAR_040840"
FT   VARIANT         280
FT                   /note="S -> F (in a glioblastoma multiforme sample; somatic
FT                   mutation; dbSNP:rs770462360)"
FT                   /evidence="ECO:0000269|PubMed:17344846"
FT                   /id="VAR_040841"
FT   VARIANT         362
FT                   /note="T -> P (in dbSNP:rs55688429)"
FT                   /evidence="ECO:0000269|PubMed:17344846"
FT                   /id="VAR_040842"
FT   VARIANT         537
FT                   /note="A -> D (in dbSNP:rs34241745)"
FT                   /evidence="ECO:0000269|PubMed:17344846"
FT                   /id="VAR_040843"
FT   VARIANT         1135
FT                   /note="Q -> R (in dbSNP:rs3741395)"
FT                   /id="VAR_057105"
FT   CONFLICT        628
FT                   /note="P -> R (in Ref. 1; AAT67172)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   1551 AA;  172459 MW;  A6D042D5D11318D7 CRC64;
     MERRLRALEQ LARGEAGGCP GLDGLLDLLL ALHHELSSGP LRRERSVAQF LSWASPFVSK
     VKELRLQRDD FEILKVIGRG AFGEVTVVRQ RDTGQIFAMK MLHKWEMLKR AETACFREER
     DVLVKGDSRW VTTLHYAFQD EEYLYLVMDY YAGGDLLTLL SRFEDRLPPE LAQFYLAEMV
     LAIHSLHQLG YVHRDVKPDN VLLDVNGHIR LADFGSCLRL NTNGMVDSSV AVGTPDYISP
     EILQAMEEGK GHYGPQCDWW SLGVCAYELL FGETPFYAES LVETYGKIMN HEDHLQFPPD
     VPDVPASAQD LIRQLLCRQE ERLGRGGLDD FRNHPFFEGV DWERLASSTA PYIPELRGPM
     DTSNFDVDDD TLNHPGTLPP PSHGAFSGHH LPFVGFTYTS GSHSPESSSE AWAALERKLQ
     CLEQEKVELS RKHQEALHAP TDHRELEQLR KEVQTLRDRL PEMLRDKASL SQTDGPPAGS
     PGQDSDLRQE LDRLHRELAE GRAGLQAQEQ ELCRAQGQQE ELLQRLQEAQ EREAATASQT
     RALSSQLEEA RAAQRELEAQ VSSLSRQVTQ LQGQWEQRLE ESSQAKTIHT ASETNGMGPP
     EGGPQEAQLR KEVAALREQL EQAHSHRPSG KEEALCQLQE ENRRLSREQE RLEAELAQEQ
     ESKQRLEGER RETESNWEAQ LADILSWVND EKVSRGYLQA LATKMAEELE SLRNVGTQTL
     PARPLDHQWK ARRLQKMEAS ARLELQSALE AEIRAKQGLQ ERLTQVQEAQ LQAERRLQEA
     EKQSQALQQE LAMLREELRA RGPVDTKPSN SLIPFLSFRS SEKDSAKDPG ISGEATRHGG
     EPDLRPEGRR SLRMGAVFPR APTANTASTE GLPAKPGSHT LRPRSFPSPT KCLRCTSLML
     GLGRQGLGCD ACGYFCHTTC APQAPPCPVP PDLLRTALGV HPETGTGTAY EGFLSVPRPS
     GVRRGWQRVF AALSDSRLLL FDAPDLRLSP PSGALLQVLD LRDPQFSATP VLASDVIHAQ
     SRDLPRIFRV TTSQLAVPPT TCTVLLLAES EGERERWLQV LGELQRLLLD ARPRPRPVYT
     LKEAYDNGLP LLPHTLCAAI LDQDRLALGT EEGLFVIHLR SNDIFQVGEC RRVQQLTLSP
     SAGLLVVLCG RGPSVRLFAL AELENIEVAG AKIPESRGCQ VLAAGSILQA RTPVLCVAVK
     RQVLCYQLGP GPGPWQRRIR ELQAPATVQS LGLLGDRLCV GAAGGFALYP LLNEAAPLAL
     GAGLVPEELP PSRGGLGEAL GAVELSLSEF LLLFTTAGIY VDGAGRKSRG HELLWPAAPM
     GWGYAAPYLT VFSENSIDVF DVRRAEWVQT VPLKKVRPLN PEGSLFLYGT EKVRLTYLRN
     QLAEKDEFDI PDLTDNSRRQ LFRTKSKRRF FFRVSEEQQK QQRREMLKDP FVRSKLISPP
     TNFNHLVHVG PANGRPGARD KSPAPEEKGR VARGSGPQRP HSFSEALRRP ASMGSEGLGG
     DADPMKRKPW TSLSSESVSC PQGSLSPATS LMQVSERPRS LPLSPELESS P
//