GNA13_MOUSE
ID GNA13_MOUSE Reviewed; 377 AA.
AC P27601; Q6PF99;
DT 01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1992, sequence version 1.
DT 03-AUG-2022, entry version 191.
DE RecName: Full=Guanine nucleotide-binding protein subunit alpha-13;
DE Short=G alpha-13;
DE Short=G-protein subunit alpha-13;
GN Name=Gna13; Synonyms=Gna-13;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Brain;
RX PubMed=1905812; DOI=10.1073/pnas.88.13.5582;
RA Strathmann M.P., Simon M.I.;
RT "G alpha 12 and G alpha 13 subunits define a fourth class of G protein
RT alpha subunits.";
RL Proc. Natl. Acad. Sci. U.S.A. 88:5582-5586(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=NMRI; TISSUE=Mammary tumor;
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 [3]
RP PROTEIN SEQUENCE OF 51-61 AND 220-227, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC STRAIN=C57BL/6J; TISSUE=Brain;
RA Lubec G., Kang S.U.;
RL Submitted (APR-2007) to UniProtKB.
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 228-288.
RX PubMed=2508088; DOI=10.1073/pnas.86.19.7407;
RA Strathmann M., Wilkie T.M., Simon M.I.;
RT "Diversity of the G-protein family: sequences from five additional alpha
RT subunits in the mouse.";
RL Proc. Natl. Acad. Sci. U.S.A. 86:7407-7409(1989).
RN [5]
RP INTERACTION WITH CTNND1.
RX PubMed=15240885; DOI=10.1073/pnas.0401366101;
RA Krakstad B.F., Ardawatia V.V., Aragay A.M.;
RT "A role for Galpha12/Galpha13 in p120ctn regulation.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:10314-10319(2004).
RN [6]
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RC TISSUE=Testis;
RX PubMed=18703424; DOI=10.1095/biolreprod.107.067504;
RA Hu Y., Xing J., Chen L., Guo X., Du Y., Zhao C., Zhu Y., Lin M., Zhou Z.,
RA Sha J.;
RT "RGS22, a novel testis-specific regulator of G-protein signaling involved
RT in human and mouse spermiogenesis along with GNA12/13 subunits.";
RL Biol. Reprod. 79:1021-1029(2008).
RN [7]
RP FUNCTION.
RX PubMed=19151758; DOI=10.1038/onc.2008.488;
RA Lee S.J., Yang J.W., Cho I.J., Kim W.D., Cho M.K., Lee C.H., Kim S.G.;
RT "The gep oncogenes, Galpha(12) and Galpha(13), upregulate the transforming
RT growth factor-beta1 gene.";
RL Oncogene 28:1230-1240(2009).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [9]
RP FUNCTION.
RX PubMed=21212405; DOI=10.1161/atvbaha.110.218552;
RA Kim Y.M., Lim S.C., Han C.Y., Kay H.Y., Cho I.J., Ki S.H., Lee M.Y.,
RA Kwon H.M., Lee C.H., Kim S.G.;
RT "G(alpha)12/13 induction of CYR61 in association with arteriosclerotic
RT intimal hyperplasia: effect of sphingosine-1-phosphate.";
RL Arterioscler. Thromb. Vasc. Biol. 31:861-869(2011).
RN [10]
RP X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 47-377 IN COMPLEX WITH GTP
RP ANALOG, FUNCTION, SUBUNIT, AND INTERACTION WITH ARHGEF1 AND ARHGEF12.
RX PubMed=16388592; DOI=10.1021/bi051729t;
RA Kreutz B., Yau D.M., Nance M.R., Tanabe S., Tesmer J.J., Kozasa T.;
RT "A new approach to producing functional G alpha subunits yields the
RT activated and deactivated structures of G alpha(12/13) proteins.";
RL Biochemistry 45:167-174(2006).
RN [11]
RP X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 41-377 IN COMPLEX WITH MAGNESIUM,
RP AND INTERACTION WITH ARHGEF11.
RX PubMed=18940608; DOI=10.1016/j.str.2008.07.009;
RA Chen Z., Singer W.D., Danesh S.M., Sternweis P.C., Sprang S.R.;
RT "Recognition of the activated states of Galpha13 by the rgRGS domain of
RT PDZRhoGEF.";
RL Structure 16:1532-1543(2008).
RN [12]
RP INTERACTION WITH GAS2L2.
RX PubMed=23994616; DOI=10.1016/j.bbamcr.2013.08.009;
RA Wu Y.C., Lai H.L., Chang W.C., Lin J.T., Liu Y.J., Chern Y.;
RT "A novel Galphas-binding protein, Gas-2 like 2, facilitates the signaling
RT of the A2A adenosine receptor.";
RL Biochim. Biophys. Acta 1833:3145-3154(2013).
CC -!- FUNCTION: Guanine nucleotide-binding proteins (G proteins) are involved
CC as modulators or transducers in various transmembrane signaling systems
CC (PubMed:21212405, PubMed:19151758, PubMed:16388592). Activates effector
CC molecule RhoA by binding and activating RhoGEFs (ARHGEF1/p115RhoGEF,
CC ARHGEF11/PDZ-RhoGEF and ARHGEF12/LARG) (PubMed:16388592). GNA13-
CC dependent Rho signaling subsequently regulates transcription factor AP-
CC 1 (activating protein-1) (PubMed:19151758, PubMed:21212405). Promotes
CC tumor cell invasion and metastasis by activating Rho/ROCK signaling
CC pathway (By similarity). Inhibits CDH1-mediated cell adhesion in
CC process independent from Rho activation (By similarity).
CC {ECO:0000250|UniProtKB:Q14344, ECO:0000269|PubMed:16388592,
CC ECO:0000269|PubMed:19151758, ECO:0000269|PubMed:21212405}.
CC -!- SUBUNIT: G proteins are composed of 3 units; alpha, beta and gamma
CC (PubMed:16388592). The alpha chain contains the guanine nucleotide
CC binding site (PubMed:16388592). Interacts with UBXD5 (By similarity).
CC Interacts with HAX1 (By similarity). Interacts (in GTP-bound form) with
CC PPP5C (via TPR repeats); activates PPP5C phosphatase activity and
CC translocates PPP5C to the cell membrane (By similarity). Interacts with
CC RGS22 (By similarity). Interacts (in GTP-bound form) with ARHGEF1
CC (PubMed:16388592). Interacts (in GTP-bound form) with ARHGEF11 (via RGS
CC domain) (PubMed:18940608). Interacts (in GTP-bound form) with ARHGEF12
CC (via RGS domain) (PubMed:16388592). Interacts with CTNND1
CC (PubMed:15240885). Interacts with GAS2L2 (PubMed:23994616).
CC {ECO:0000250|UniProtKB:Q14344, ECO:0000269|PubMed:15240885,
CC ECO:0000269|PubMed:16388592, ECO:0000269|PubMed:18940608,
CC ECO:0000269|PubMed:23994616}.
CC -!- INTERACTION:
CC P27601; O08915: Aip; NbExp=3; IntAct=EBI-2255627, EBI-6935014;
CC P27601; Q9ES67: Arhgef11; Xeno; NbExp=3; IntAct=EBI-2255627, EBI-15735216;
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000269|PubMed:18703424}; Lipid-
CC anchor {ECO:0000269|PubMed:18703424}. Melanosome {ECO:0000250}.
CC Cytoplasm {ECO:0000269|PubMed:18703424}. Nucleus
CC {ECO:0000269|PubMed:18703424}. Note=Cytoplasmic in adult somatic cells,
CC but mainly nuclear in spermatids in the testes. Translocates from the
CC cytoplasm to the nucleus during spermatogenesis, hence predominantly
CC observed in the cytoplasm of round spermatids but localized in the
CC nuclei of elongating or elongated spermatids and testicular
CC spermatozoa.
CC -!- TISSUE SPECIFICITY: Expressed in brain and testis, as well as in kidney
CC and sperm (at protein level). {ECO:0000269|PubMed:18703424}.
CC -!- PTM: Phosphorylation on Thr-203 destabilizes the heterotrimer of alpha,
CC beta and gamma, and inhibits Rho activation. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the G-alpha family. G(12) subfamily.
CC {ECO:0000305}.
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DR EMBL; M63660; AAA37649.1; -; mRNA.
DR EMBL; BC057665; AAH57665.1; -; mRNA.
DR EMBL; M57620; AAA63303.1; -; mRNA.
DR CCDS; CCDS25577.1; -.
DR PIR; B41095; B41095.
DR RefSeq; NP_034433.3; NM_010303.3.
DR PDB; 1SHZ; X-ray; 2.85 A; A/D=52-159, A/D=333-376.
DR PDB; 1ZCB; X-ray; 2.00 A; A=47-377.
DR PDB; 3AB3; X-ray; 2.40 A; A/C=47-377.
DR PDB; 3CX6; X-ray; 2.50 A; A=41-377.
DR PDB; 3CX7; X-ray; 2.25 A; A=41-377.
DR PDB; 3CX8; X-ray; 2.00 A; A=41-377.
DR PDBsum; 1SHZ; -.
DR PDBsum; 1ZCB; -.
DR PDBsum; 3AB3; -.
DR PDBsum; 3CX6; -.
DR PDBsum; 3CX7; -.
DR PDBsum; 3CX8; -.
DR AlphaFoldDB; P27601; -.
DR SMR; P27601; -.
DR BioGRID; 199963; 22.
DR DIP; DIP-46241N; -.
DR IntAct; P27601; 6.
DR MINT; P27601; -.
DR STRING; 10090.ENSMUSP00000020930; -.
DR iPTMnet; P27601; -.
DR PhosphoSitePlus; P27601; -.
DR SwissPalm; P27601; -.
DR EPD; P27601; -.
DR jPOST; P27601; -.
DR MaxQB; P27601; -.
DR PaxDb; P27601; -.
DR PeptideAtlas; P27601; -.
DR PRIDE; P27601; -.
DR ProteomicsDB; 267733; -.
DR Antibodypedia; 31626; 271 antibodies from 30 providers.
DR DNASU; 14674; -.
DR Ensembl; ENSMUST00000020930; ENSMUSP00000020930; ENSMUSG00000020611.
DR GeneID; 14674; -.
DR KEGG; mmu:14674; -.
DR UCSC; uc007mce.1; mouse.
DR CTD; 10672; -.
DR MGI; MGI:95768; Gna13.
DR VEuPathDB; HostDB:ENSMUSG00000020611; -.
DR eggNOG; KOG0082; Eukaryota.
DR GeneTree; ENSGT00940000157054; -.
DR HOGENOM; CLU_014184_3_1_1; -.
DR InParanoid; P27601; -.
DR OMA; TSRFACM; -.
DR OrthoDB; 754573at2759; -.
DR PhylomeDB; P27601; -.
DR TreeFam; TF300673; -.
DR Reactome; R-MMU-193648; NRAGE signals death through JNK.
DR Reactome; R-MMU-416482; G alpha (12/13) signalling events.
DR Reactome; R-MMU-428930; Thromboxane signalling through TP receptor.
DR Reactome; R-MMU-456926; Thrombin signalling through proteinase activated receptors (PARs).
DR Reactome; R-MMU-9013148; CDC42 GTPase cycle.
DR Reactome; R-MMU-9013149; RAC1 GTPase cycle.
DR BioGRID-ORCS; 14674; 10 hits in 78 CRISPR screens.
DR ChiTaRS; Gna13; mouse.
DR EvolutionaryTrace; P27601; -.
DR PRO; PR:P27601; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; P27601; protein.
DR Bgee; ENSMUSG00000020611; Expressed in rostral migratory stream and 258 other tissues.
DR ExpressionAtlas; P27601; baseline and differential.
DR Genevisible; P27601; MM.
DR GO; GO:0031526; C:brush border membrane; ISO:MGI.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005834; C:heterotrimeric G-protein complex; ISA:MGI.
DR GO; GO:0042470; C:melanosome; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR GO; GO:0031752; F:D5 dopamine receptor binding; ISO:MGI.
DR GO; GO:0001664; F:G protein-coupled receptor binding; IBA:GO_Central.
DR GO; GO:0031683; F:G-protein beta/gamma-subunit complex binding; IBA:GO_Central.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0003924; F:GTPase activity; ISA:MGI.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0031584; P:activation of phospholipase D activity; ISO:MGI.
DR GO; GO:0007189; P:adenylate cyclase-activating G protein-coupled receptor signaling pathway; IGI:MGI.
DR GO; GO:0007188; P:adenylate cyclase-modulating G protein-coupled receptor signaling pathway; IMP:UniProtKB.
DR GO; GO:0001525; P:angiogenesis; IMP:MGI.
DR GO; GO:0001569; P:branching involved in blood vessel morphogenesis; IMP:MGI.
DR GO; GO:0030154; P:cell differentiation; IDA:MGI.
DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; ISA:MGI.
DR GO; GO:0001701; P:in utero embryonic development; IGI:MGI.
DR GO; GO:0035556; P:intracellular signal transduction; IDA:MGI.
DR GO; GO:0010259; P:multicellular organism aging; IMP:MGI.
DR GO; GO:1904753; P:negative regulation of vascular associated smooth muscle cell migration; ISO:MGI.
DR GO; GO:1904706; P:negative regulation of vascular associated smooth muscle cell proliferation; ISO:MGI.
DR GO; GO:0030168; P:platelet activation; IMP:MGI.
DR GO; GO:0007204; P:positive regulation of cytosolic calcium ion concentration; ISO:MGI.
DR GO; GO:0008217; P:regulation of blood pressure; IGI:MGI.
DR GO; GO:0008360; P:regulation of cell shape; IDA:MGI.
DR GO; GO:0010762; P:regulation of fibroblast migration; IMP:MGI.
DR GO; GO:0007266; P:Rho protein signal transduction; IDA:MGI.
DR CDD; cd00066; G-alpha; 1.
DR Gene3D; 1.10.400.10; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR000469; Gprotein_alpha_12/13.
DR InterPro; IPR001019; Gprotein_alpha_su.
DR InterPro; IPR011025; GproteinA_insert.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR10218; PTHR10218; 1.
DR Pfam; PF00503; G-alpha; 1.
DR PRINTS; PR00318; GPROTEINA.
DR PRINTS; PR00440; GPROTEINA12.
DR SMART; SM00275; G_alpha; 1.
DR SUPFAM; SSF47895; SSF47895; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS51882; G_ALPHA; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Direct protein sequencing; GTP-binding;
KW Lipoprotein; Magnesium; Membrane; Metal-binding; Nucleotide-binding;
KW Nucleus; Palmitate; Phosphoprotein; Reference proteome; Transducer.
FT CHAIN 1..377
FT /note="Guanine nucleotide-binding protein subunit alpha-13"
FT /id="PRO_0000203774"
FT DOMAIN 47..377
FT /note="G-alpha"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01230"
FT REGION 50..63
FT /note="G1 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01230"
FT REGION 195..203
FT /note="G2 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01230"
FT REGION 218..227
FT /note="G3 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01230"
FT REGION 287..294
FT /note="G4 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01230"
FT REGION 347..352
FT /note="G5 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01230"
FT BINDING 58..63
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000269|PubMed:16388592,
FT ECO:0000269|PubMed:18940608, ECO:0007744|PDB:1ZCB,
FT ECO:0007744|PDB:3CX6, ECO:0007744|PDB:3CX7"
FT BINDING 62
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000269|PubMed:18940608,
FT ECO:0007744|PDB:3CX6"
FT BINDING 173
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000269|PubMed:18940608,
FT ECO:0007744|PDB:3CX7"
FT BINDING 197..200
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000269|PubMed:16388592,
FT ECO:0000269|PubMed:18940608, ECO:0007744|PDB:1ZCB,
FT ECO:0007744|PDB:3CX6, ECO:0007744|PDB:3CX7"
FT BINDING 203
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000269|PubMed:18940608,
FT ECO:0007744|PDB:3CX6"
FT BINDING 291..294
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000269|PubMed:16388592,
FT ECO:0000269|PubMed:18940608, ECO:0007744|PDB:1ZCB,
FT ECO:0007744|PDB:3CX6, ECO:0007744|PDB:3CX7"
FT BINDING 349
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000269|PubMed:16388592,
FT ECO:0000269|PubMed:18940608, ECO:0007744|PDB:1ZCB,
FT ECO:0007744|PDB:3CX6, ECO:0007744|PDB:3CX7"
FT MOD_RES 203
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q14344"
FT LIPID 14
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000250|UniProtKB:Q14344"
FT LIPID 18
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000250|UniProtKB:Q14344"
FT CONFLICT 52
FT /note="L -> P (in Ref. 2; AAH57665)"
FT /evidence="ECO:0000305"
FT STRAND 49..54
FT /evidence="ECO:0007829|PDB:1ZCB"
FT HELIX 61..72
FT /evidence="ECO:0007829|PDB:1ZCB"
FT HELIX 78..82
FT /evidence="ECO:0007829|PDB:1ZCB"
FT HELIX 85..105
FT /evidence="ECO:0007829|PDB:1ZCB"
FT HELIX 113..115
FT /evidence="ECO:0007829|PDB:1ZCB"
FT HELIX 116..123
FT /evidence="ECO:0007829|PDB:1ZCB"
FT STRAND 127..129
FT /evidence="ECO:0007829|PDB:1ZCB"
FT HELIX 130..133
FT /evidence="ECO:0007829|PDB:1ZCB"
FT HELIX 139..154
FT /evidence="ECO:0007829|PDB:1ZCB"
FT HELIX 156..163
FT /evidence="ECO:0007829|PDB:1ZCB"
FT HELIX 164..167
FT /evidence="ECO:0007829|PDB:1ZCB"
FT HELIX 174..178
FT /evidence="ECO:0007829|PDB:1ZCB"
FT HELIX 181..184
FT /evidence="ECO:0007829|PDB:1ZCB"
FT STRAND 185..188
FT /evidence="ECO:0007829|PDB:1SHZ"
FT HELIX 193..198
FT /evidence="ECO:0007829|PDB:1ZCB"
FT STRAND 204..213
FT /evidence="ECO:0007829|PDB:1ZCB"
FT STRAND 216..223
FT /evidence="ECO:0007829|PDB:1ZCB"
FT HELIX 227..236
FT /evidence="ECO:0007829|PDB:3CX8"
FT STRAND 242..248
FT /evidence="ECO:0007829|PDB:1ZCB"
FT HELIX 251..253
FT /evidence="ECO:0007829|PDB:3AB3"
FT STRAND 259..263
FT /evidence="ECO:0007829|PDB:1ZCB"
FT HELIX 264..276
FT /evidence="ECO:0007829|PDB:1ZCB"
FT HELIX 279..281
FT /evidence="ECO:0007829|PDB:1ZCB"
FT STRAND 284..291
FT /evidence="ECO:0007829|PDB:1ZCB"
FT HELIX 293..299
FT /evidence="ECO:0007829|PDB:1ZCB"
FT TURN 300..302
FT /evidence="ECO:0007829|PDB:1ZCB"
FT HELIX 305..307
FT /evidence="ECO:0007829|PDB:1ZCB"
FT HELIX 319..331
FT /evidence="ECO:0007829|PDB:1ZCB"
FT STRAND 343..346
FT /evidence="ECO:0007829|PDB:1ZCB"
FT HELIX 352..371
FT /evidence="ECO:0007829|PDB:1ZCB"
SQ SEQUENCE 377 AA; 44055 MW; 45A6A6DB47C707BB CRC64;
MADFLPSRSV LSVCFPGCVL TNGEAEQQRK SKEIDKCLSR EKTYVKRLVK ILLLGAGESG
KSTFLKQMRI IHGQDFDQRA REEFRPTIYS NVIKGMRVLV DAREKLHIPW GDNKNQLHGD
KLMAFDTRAP MAAQGMVETR VFLQYLPAIR ALWEDSGIQN AYDRRREFQL GESVKYFLDN
LDKLGVPDYI PSQQDILLAR RPTKGIHEYD FEIKNVPFKM VDVGGQRSER KRWFECFDSV
TSILFLVSSS EFDQVLMEDR QTNRLTESLN IFETIVNNRV FSNVSIILFL NKTDLLEEKV
QVVSIKDYFL EFEGDPHCLR DVQKFLVECF RGKRRDQQQR PLYHHFTTAI NTENIRLVFR
DVKDTILHDN LKQLMLQ
