PTPRH_MOUSE
ID PTPRH_MOUSE Reviewed; 971 AA.
AC E9Q0N2; B6ZDS3; Q8BIW7;
DT 30-NOV-2016, integrated into UniProtKB/Swiss-Prot.
DT 05-APR-2011, sequence version 1.
DT 03-AUG-2022, entry version 92.
DE RecName: Full=Receptor-type tyrosine-protein phosphatase H {ECO:0000312|MGI:MGI:3026877};
DE Short=R-PTP-H {ECO:0000250|UniProtKB:Q9HD43};
DE EC=3.1.3.48 {ECO:0000269|PubMed:26195794};
DE AltName: Full=Stomach cancer-associated protein tyrosine phosphatase 1 {ECO:0000250|UniProtKB:Q9HD43};
DE Short=SAP-1 {ECO:0000250|UniProtKB:Q9HD43};
DE Flags: Precursor;
GN Name=Ptprh {ECO:0000312|MGI:MGI:3026877};
GN Synonyms=SAP-1 {ECO:0000312|MGI:MGI:3026877};
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 {ECO:0000312|Proteomes:UP000000589};
RN [1] {ECO:0000312|EMBL:BAH03209.1}
RP NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, TISSUE SPECIFICITY,
RP DEVELOPMENTAL STAGE, AND DISRUPTION PHENOTYPE.
RC STRAIN=C57BL/6J {ECO:0000312|EMBL:BAH03209.1};
RC TISSUE=Colon {ECO:0000312|EMBL:BAH03209.1};
RX PubMed=19170756; DOI=10.1111/j.1365-2443.2008.01270.x;
RA Sadakata H., Okazawa H., Sato T., Supriatna Y., Ohnishi H., Kusakari S.,
RA Murata Y., Ito T., Nishiyama U., Minegishi T., Harada A., Matozaki T.;
RT "SAP-1 is a microvillus-specific protein tyrosine phosphatase that
RT modulates intestinal tumorigenesis.";
RL Genes Cells 14:295-308(2009).
RN [2] {ECO:0000312|EMBL:BAC37443.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J {ECO:0000312|EMBL:BAC37443.1};
RC TISSUE=Colon {ECO:0000312|EMBL:BAC37443.1};
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3] {ECO:0000312|Proteomes:UP000000589}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [4] {ECO:0000305}
RP INTERACTION WITH GRB2 AND FYN, PHOSPHORYLATION AT TYR-945 AND TYR-953, AND
RP MUTAGENESIS OF TYR-945 AND TYR-953.
RX PubMed=20398064; DOI=10.1111/j.1365-2443.2010.01398.x;
RA Murata Y., Mori M., Kotani T., Supriatna Y., Okazawa H., Kusakari S.,
RA Saito Y., Ohnishi H., Matozaki T.;
RT "Tyrosine phosphorylation of R3 subtype receptor-type protein tyrosine
RT phosphatases and their complex formations with Grb2 or Fyn.";
RL Genes Cells 15:513-524(2010).
RN [5] {ECO:0000305}
RP FUNCTION, CATALYTIC ACTIVITY, INTERACTION WITH CEACAM20, SUBCELLULAR
RP LOCATION, DISRUPTION PHENOTYPE, AND MUTAGENESIS OF ASP-837 AND CYS-871.
RX PubMed=26195794; DOI=10.1073/pnas.1510167112;
RA Murata Y., Kotani T., Supriatna Y., Kitamura Y., Imada S., Kawahara K.,
RA Nishio M., Daniwijaya E.W., Sadakata H., Kusakari S., Mori M., Kanazawa Y.,
RA Saito Y., Okawa K., Takeda-Morishita M., Okazawa H., Ohnishi H., Azuma T.,
RA Suzuki A., Matozaki T.;
RT "Protein tyrosine phosphatase SAP-1 protects against colitis through
RT regulation of CEACAM20 in the intestinal epithelium.";
RL Proc. Natl. Acad. Sci. U.S.A. 112:E4264-E4271(2015).
CC -!- FUNCTION: Protein phosphatase that may contribute to contact inhibition
CC of cell growth and motility by mediating the dephosphorylation of focal
CC adhesion-associated substrates and thus negatively regulating integrin-
CC promoted signaling processes. Induces apoptotic cell death by at least
CC two distinct mechanisms: inhibition of cell survival signaling mediated
CC by PI 3-kinase, Akt, and ILK and activation of a caspase-dependent
CC proapoptotic pathway. Inhibits the basal activity of LCK and its
CC activation in response to TCR stimulation and TCR-induced activation of
CC MAP kinase and surface expression of CD69. Inhibits TCR-induced
CC tyrosine phosphorylation of LAT and ZAP70. Inhibits both basal activity
CC of DOK1 and its CD2-induced tyrosine phosphorylation. Induces
CC dephosphorylation of BCAR1, focal adhesion kinase and SRC. Reduces
CC migratory activity of Jurkat cells (By similarity). Reduces tyrosine
CC phosphorylation of CEACAM20 and thereby contributes to suppress the
CC intestinal immune response (PubMed:26195794).
CC {ECO:0000250|UniProtKB:Q9HD43, ECO:0000269|PubMed:26195794}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + O-phospho-L-tyrosyl-[protein] = L-tyrosyl-[protein] +
CC phosphate; Xref=Rhea:RHEA:10684, Rhea:RHEA-COMP:10136, Rhea:RHEA-
CC COMP:10137, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:46858,
CC ChEBI:CHEBI:82620; EC=3.1.3.48;
CC Evidence={ECO:0000269|PubMed:26195794};
CC -!- SUBUNIT: Homodimer; disulfide-linked (By similarity). Interacts with
CC LCK (By similarity). Interacts (phosphorylated form) with GRB2 (via SH2
CC domain) (PubMed:20398064). Interacts (phosphorylated form) with FYN
CC (via SH2 domain) (PubMed:20398064). Interacts (via extracellular
CC domain) with CEACAM20 (via extracellular domain); the interaction
CC dephosphorylates CEACAM20 (PubMed:26195794).
CC {ECO:0000250|UniProtKB:Q9HD43, ECO:0000269|PubMed:20398064,
CC ECO:0000269|PubMed:26195794}.
CC -!- SUBCELLULAR LOCATION: Cell projection, microvillus membrane
CC {ECO:0000269|PubMed:19170756, ECO:0000269|PubMed:26195794}; Single-pass
CC type I membrane protein {ECO:0000305}. Cytoplasm
CC {ECO:0000250|UniProtKB:Q9HD43}. Apical cell membrane
CC {ECO:0000269|PubMed:19170756, ECO:0000269|PubMed:26195794}; Single-pass
CC type I membrane protein {ECO:0000305}. Note=Colocalizes with CEACAM20
CC at the apical brush border of intestinal cells.
CC {ECO:0000269|PubMed:26195794}.
CC -!- TISSUE SPECIFICITY: Expressed strongly in the intestinal tract, with
CC particularly high levels in the duodenum and jejunum (at protein
CC level). Also expressed at low level in the testis (at protein level).
CC Not detected in other tissues tested (at protein level).
CC {ECO:0000269|PubMed:19170756}.
CC -!- DEVELOPMENTAL STAGE: Detected from embryonic stage 16.5 dpc onwards,
CC with marked increase in expression level after birth.
CC {ECO:0000269|PubMed:19170756}.
CC -!- DISRUPTION PHENOTYPE: Viable and fertile (PubMed:19170756). No
CC significant effect on body weight or nutrient absorption
CC (PubMed:19170756). Morphology of intestinal epithelium cells appears to
CC be normal (PubMed:19170756). Double knockouts with APC heterozygotes, a
CC model for intestinal tumorigenesis, show reduced adenoma growth
CC (PubMed:19170756). Double knockouts with IL10, a model of inflammatory
CC bowel disease, show significantly increased colonic inflammation in the
CC presence of commensal bacteria and reduced survival rates
CC (PubMed:26195794). {ECO:0000269|PubMed:19170756,
CC ECO:0000269|PubMed:26195794}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC37443.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AB217856; BAH03209.1; -; mRNA.
DR EMBL; AK078884; BAC37443.1; ALT_FRAME; mRNA.
DR EMBL; AC161197; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC161218; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS51974.1; -.
DR RefSeq; NP_997153.2; NM_207270.2.
DR AlphaFoldDB; E9Q0N2; -.
DR SMR; E9Q0N2; -.
DR STRING; 10090.ENSMUSP00000125833; -.
DR GlyGen; E9Q0N2; 7 sites.
DR iPTMnet; E9Q0N2; -.
DR PhosphoSitePlus; E9Q0N2; -.
DR PaxDb; E9Q0N2; -.
DR PRIDE; E9Q0N2; -.
DR ProteomicsDB; 301918; -.
DR Antibodypedia; 33039; 92 antibodies from 17 providers.
DR DNASU; 545902; -.
DR Ensembl; ENSMUST00000049113; ENSMUSP00000042396; ENSMUSG00000035429.
DR Ensembl; ENSMUST00000166650; ENSMUSP00000125833; ENSMUSG00000035429.
DR Ensembl; ENSMUST00000206999; ENSMUSP00000145543; ENSMUSG00000035429.
DR GeneID; 545902; -.
DR KEGG; mmu:545902; -.
DR UCSC; uc009exz.1; mouse.
DR CTD; 5794; -.
DR MGI; MGI:3026877; Ptprh.
DR VEuPathDB; HostDB:ENSMUSG00000035429; -.
DR eggNOG; KOG0791; Eukaryota.
DR GeneTree; ENSGT00940000162227; -.
DR HOGENOM; CLU_001541_2_0_1; -.
DR InParanoid; E9Q0N2; -.
DR OMA; QNLTYWV; -.
DR OrthoDB; 411281at2759; -.
DR PhylomeDB; E9Q0N2; -.
DR TreeFam; TF351926; -.
DR BioGRID-ORCS; 545902; 1 hit in 74 CRISPR screens.
DR ChiTaRS; Elk4; mouse.
DR PRO; PR:E9Q0N2; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; E9Q0N2; protein.
DR Bgee; ENSMUSG00000035429; Expressed in jejunum and 23 other tissues.
DR GO; GO:0016324; C:apical plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005902; C:microvillus; IDA:MGI.
DR GO; GO:0031528; C:microvillus membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0045296; F:cadherin binding; ISO:MGI.
DR GO; GO:0004725; F:protein tyrosine phosphatase activity; IBA:GO_Central.
DR GO; GO:0005001; F:transmembrane receptor protein tyrosine phosphatase activity; IEA:InterPro.
DR GO; GO:1990264; P:peptidyl-tyrosine dephosphorylation involved in inactivation of protein kinase activity; IDA:CACAO.
DR GO; GO:0006470; P:protein dephosphorylation; IBA:GO_Central.
DR CDD; cd00063; FN3; 5.
DR Gene3D; 2.60.40.10; -; 6.
DR Gene3D; 3.90.190.10; -; 1.
DR InterPro; IPR003961; FN3_dom.
DR InterPro; IPR036116; FN3_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR029021; Prot-tyrosine_phosphatase-like.
DR InterPro; IPR000242; PTP_cat.
DR InterPro; IPR028855; R-PTP-H.
DR InterPro; IPR016130; Tyr_Pase_AS.
DR InterPro; IPR003595; Tyr_Pase_cat.
DR InterPro; IPR000387; Tyr_Pase_dom.
DR PANTHER; PTHR19134:SF297; PTHR19134:SF297; 6.
DR Pfam; PF00041; fn3; 5.
DR Pfam; PF00102; Y_phosphatase; 1.
DR PRINTS; PR00700; PRTYPHPHTASE.
DR SMART; SM00060; FN3; 6.
DR SMART; SM00194; PTPc; 1.
DR SMART; SM00404; PTPc_motif; 1.
DR SUPFAM; SSF49265; SSF49265; 3.
DR SUPFAM; SSF52799; SSF52799; 1.
DR PROSITE; PS50853; FN3; 6.
DR PROSITE; PS00383; TYR_PHOSPHATASE_1; 1.
DR PROSITE; PS50056; TYR_PHOSPHATASE_2; 1.
DR PROSITE; PS50055; TYR_PHOSPHATASE_PTP; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Cell projection; Cytoplasm; Disulfide bond; Glycoprotein;
KW Hydrolase; Membrane; Phosphoprotein; Protein phosphatase;
KW Reference proteome; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..27
FT /evidence="ECO:0000255"
FT CHAIN 28..971
FT /note="Receptor-type tyrosine-protein phosphatase H"
FT /id="PRO_5007654674"
FT TOPO_DOM 28..604
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 605..625
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 626..971
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT DOMAIN 69..158
FT /note="Fibronectin type-III 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 159..246
FT /note="Fibronectin type-III 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 247..336
FT /note="Fibronectin type-III 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 337..425
FT /note="Fibronectin type-III 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 429..518
FT /note="Fibronectin type-III 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 519..603
FT /note="Fibronectin type-III 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 671..930
FT /note="Tyrosine-protein phosphatase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00160"
FT ACT_SITE 871
FT /note="Phosphocysteine intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00160,
FT ECO:0000305|PubMed:26195794"
FT MOD_RES 945
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000269|PubMed:20398064"
FT MOD_RES 953
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000269|PubMed:20398064"
FT CARBOHYD 80
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 115
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 169
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 293
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 382
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 440
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 520
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT MUTAGEN 837
FT /note="D->A: Impairs phosphatase activity."
FT /evidence="ECO:0000269|PubMed:26195794"
FT MUTAGEN 871
FT /note="C->S: Impairs phosphatase activity."
FT /evidence="ECO:0000269|PubMed:26195794"
FT MUTAGEN 945
FT /note="Y->S: Reduces tyrosine phosphorylation. Abolishes
FT tyrosine phosphorylation and interaction with GRB2 and FYN;
FT when associated with A-953."
FT /evidence="ECO:0000269|PubMed:20398064"
FT MUTAGEN 953
FT /note="Y->A: Reduces tyrosine phosphorylation. Abolishes
FT tyrosine phosphorylation and interaction with GRB2 and FYN;
FT when associated with A-945."
FT /evidence="ECO:0000269|PubMed:20398064"
FT CONFLICT 182
FT /note="P -> S (in Ref. 1; BAH03209)"
FT /evidence="ECO:0000305"
FT CONFLICT 436..437
FT /note="EG -> KS (in Ref. 1; BAH03209)"
FT /evidence="ECO:0000305"
FT CONFLICT 453
FT /note="S -> P (in Ref. 1; BAH03209)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 971 AA; 106952 MW; 9992614E4A5C1543 CRC64;
MARAGGNCGV WRSLVLLGLY GCSVVRAAGT SVTVDRHAPA SSYEFSMWVE KDGVSSSPQI
PVTTAAPNPV RNLRVEGQNN ISISLSWEPP DQSSLQGLTY WTQCSRHGGQ TETRNTTDTS
VTVDGLDPGS SYECSVWVEK DGLYSKNETL NTSTAPNPVR NLRVEGQNNI SISLSWEPPD
QPSLQGLTYW AQCSRHGGQT ETRNTADTSV TVDGLDPGSS YECSVWVEKD GVYSTNETLN
TSTAPNPVRN LRVEGQNNIS ISLSWEPPDQ PSLQGLTYWA QCSRHGGQTE TRNTTDTSIT
VDGLDPGSSY ECSVWVEKDG VYSTNETLSN TTAPNPVRNL RVKSQNNFSI SLSWEPPDQP
SLQGLIYWAQ CSRHGGQTET RNTTDTSVTV DGLDPGFLYK CSVWVEKDGV YSTNETLNTS
TVPISASNPV RNLRVEGQNN FSISLSWEPP DQSSLQGLTY WAQCSRHGGQ TETRNTADTS
VTVDGLDPGS SYECSVWVEK DGVYSTNETL NTSTVPAAVN ITSCISTSGG YGVLLTWSCP
SGGYESFEVK VGRKWRSENG SLCGKGVTVS DLEPAQSYTA TVTTVFKDLK AQSLSTTCHT
ESAAIIAGAI VGILLLFILV GLLIVFLKRR RKKRQPKEVP KDLVCSCPGD ILAKDFADHV
RENEKDSNCG FAEEYQQLAL EGQGQSQITA SALENRSKNR YRNVLPYDWS RVPLQPLQEE
PGSDYINASF MPGLWSPKEF IATQGPLPNT VGDFWRMVWE QQSHTLVMLT NCMESGRVKC
EHYWPLDAQP CIHGQLQVML ISEEASENWT VRHLQLFHMK EQQTLSLRQF HYLAWPDHGV
PYSPDPLLAF RKMLRQWMDQ TTDGGPPIVH CSAGVGRTGT LIALDVLLRQ LECEGLVGPF
SFVKKMRESR PLMVQTEAQY VFLHQCILKS LQKPAPALVP EEAMYENVAS LVYENASAIM
AHESEFSASG C
