HEPS_MOUSE
ID HEPS_MOUSE Reviewed; 436 AA.
AC O35453; B2RSC4; Q9CW97;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 3.
DT 03-AUG-2022, entry version 169.
DE RecName: Full=Serine protease hepsin;
DE EC=3.4.21.106 {ECO:0000305|PubMed:26673890, ECO:0000305|PubMed:9395459};
DE Contains:
DE RecName: Full=Serine protease hepsin non-catalytic chain;
DE Contains:
DE RecName: Full=Serine protease hepsin catalytic chain;
GN Name=Hpn;
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] (ISOFORM 2), ALTERNATIVE SPLICING, SUBCELLULAR
RP LOCATION, ACTIVE SITE, MUTAGENESIS OF SER-372, CATALYTIC ACTIVITY, AND
RP TISSUE SPECIFICITY.
RC TISSUE=Liver;
RX PubMed=9395459; DOI=10.1074/jbc.272.50.31315;
RA Vu T.-K.H., Liu R.W., Haaksma C., Tomasek J.J., Howard E.W.;
RT "Identification and cloning of the membrane-associated serine protease,
RT hepsin, from mouse preimplantation embryos.";
RL J. Biol. Chem. 272:31315-31320(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
RX PubMed=10411637; DOI=10.1046/j.1432-1327.1999.00431.x;
RA Kawamura S., Kurachi S., Deyashiki Y., Kurachi K.;
RT "Complete nucleotide sequence, origin of isoform and functional
RT characterization of the mouse hepsin gene.";
RL Eur. J. Biochem. 262:755-764(1999).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Kidney;
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Lung;
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 [6]
RP DISRUPTION PHENOTYPE, AND TISSUE SPECIFICITY.
RX PubMed=9435303; DOI=10.1172/jci1617;
RA Wu Q., Yu D., Post J., Halks-Miller M., Sadler J.E., Morser J.;
RT "Generation and characterization of mice deficient in hepsin, a hepatic
RT transmembrane serine protease.";
RL J. Clin. Invest. 101:321-326(1998).
RN [7]
RP DISRUPTION PHENOTYPE.
RX PubMed=11127869;
RA Yu I.S., Chen H.J., Lee Y.S., Huang P.H., Lin S.R., Tsai T.W., Lin S.W.;
RT "Mice deficient in hepsin, a serine protease, exhibit normal embryogenesis
RT and unchanged hepatocyte regeneration ability.";
RL Thromb. Haemost. 84:865-870(2000).
RN [8]
RP DISRUPTION PHENOTYPE.
RX PubMed=17620368; DOI=10.2353/ajpath.2007.070068;
RA Guipponi M., Tan J., Cannon P.Z., Donley L., Crewther P., Clarke M., Wu Q.,
RA Shepherd R.K., Scott H.S.;
RT "Mice deficient for the type II transmembrane serine protease,
RT TMPRSS1/hepsin, exhibit profound hearing loss.";
RL Am. J. Pathol. 171:608-616(2007).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Kidney, and Liver;
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 [10]
RP FUNCTION, CATALYTIC ACTIVITY, DISRUPTION PHENOTYPE, SUBCELLULAR LOCATION,
RP AND TISSUE SPECIFICITY.
RX PubMed=26673890; DOI=10.7554/elife.08887;
RA Brunati M., Perucca S., Han L., Cattaneo A., Consolato F., Andolfo A.,
RA Schaeffer C., Olinger E., Peng J., Santambrogio S., Perrier R., Li S.,
RA Bokhove M., Bachi A., Hummler E., Devuyst O., Wu Q., Jovine L.,
RA Rampoldi L.;
RT "The serine protease hepsin mediates urinary secretion and polymerisation
RT of Zona Pellucida domain protein uromodulin.";
RL Elife 4:0-0(2015).
CC -!- FUNCTION: Serine protease that cleaves extracellular substrates, and
CC contributes to the proteolytic processing of growth factors, such as
CC HGF and MST1/HGFL. Plays a role in cell growth and maintenance of cell
CC morphology. Plays a role in the proteolytic processing of ACE2 (By
CC similarity). Mediates the proteolytic cleavage of urinary UMOD that is
CC required for UMOD polymerization (PubMed:26673890).
CC {ECO:0000250|UniProtKB:P05981, ECO:0000269|PubMed:26673890}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Cleavage after basic amino-acid residues, with Arg strongly
CC preferred to Lys.; EC=3.4.21.106;
CC Evidence={ECO:0000305|PubMed:26673890, ECO:0000305|PubMed:9395459};
CC -!- SUBCELLULAR LOCATION: Apical cell membrane
CC {ECO:0000269|PubMed:26673890}; Single-pass type II membrane protein
CC {ECO:0000305}. Cell membrane {ECO:0000250|UniProtKB:P05981}; Single-
CC pass type II membrane protein {ECO:0000250|UniProtKB:P05981}.
CC -!- SUBCELLULAR LOCATION: [Isoform 2]: Secreted
CC {ECO:0000269|PubMed:9395459}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1; Synonyms=1a;
CC IsoId=O35453-1; Sequence=Displayed;
CC Name=2; Synonyms=2a;
CC IsoId=O35453-2; Sequence=VSP_007232;
CC -!- TISSUE SPECIFICITY: Detected in kidney, in thick ascending tubule
CC epithelial cells (at protein level) (PubMed:26673890). Detected in
CC kidney and liver (PubMed:9395459, PubMed:9435303).
CC {ECO:0000269|PubMed:9395459, ECO:0000269|PubMed:9435303}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype. Mice are viable and fertile
CC (PubMed:9435303, PubMed:11127869). They present no defect in blood
CC coagulation (PubMed:9435303). Likewise, they present no defect in liver
CC regeneration after liver resection (PubMed:11127869). Mice have
CC severely impaired hearing, with abnormal morphology of the tectorial
CC membrane in the cochlea, but no visible defects of the organ of Corti
CC and no loss of inner or outer hair cells. Mutant mice have reduced
CC levels of thyroid hormone. This may play a role in their hearing
CC deficit, since adequate levels of thyroid hormone are required for
CC normal development of the auditory system (PubMed:17620368). Urine from
CC mutant mice lacks normally processed Umod; contrary to wild-type,
CC urinary Umod from mutant mice does not polymerize into long fibers
CC (PubMed:26673890). {ECO:0000269|PubMed:11127869,
CC ECO:0000269|PubMed:17620368, ECO:0000269|PubMed:26673890,
CC ECO:0000269|PubMed:9435303}.
CC -!- MISCELLANEOUS: [Isoform 1]: Minor isoform.
CC -!- MISCELLANEOUS: [Isoform 2]: Major isoform. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the peptidase S1 family. {ECO:0000255|PROSITE-
CC ProRule:PRU00274}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB22289.2; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AF030065; AAB84221.1; -; mRNA.
DR EMBL; AK002694; BAB22289.2; ALT_FRAME; mRNA.
DR EMBL; CH466593; EDL23952.1; -; Genomic_DNA.
DR EMBL; BC138809; AAI38810.1; -; mRNA.
DR EMBL; BC145413; AAI45414.1; -; mRNA.
DR CCDS; CCDS52188.1; -. [O35453-1]
DR RefSeq; NP_001103722.1; NM_001110252.2. [O35453-1]
DR RefSeq; NP_001263198.1; NM_001276269.1.
DR RefSeq; NP_032307.2; NM_008281.4.
DR AlphaFoldDB; O35453; -.
DR SMR; O35453; -.
DR BioGRID; 200410; 3.
DR STRING; 10090.ENSMUSP00000103737; -.
DR MEROPS; S01.224; -.
DR GlyGen; O35453; 1 site.
DR iPTMnet; O35453; -.
DR PhosphoSitePlus; O35453; -.
DR SwissPalm; O35453; -.
DR jPOST; O35453; -.
DR MaxQB; O35453; -.
DR PaxDb; O35453; -.
DR PRIDE; O35453; -.
DR ProteomicsDB; 269736; -. [O35453-1]
DR ProteomicsDB; 269737; -. [O35453-2]
DR Antibodypedia; 1718; 185 antibodies from 33 providers.
DR DNASU; 15451; -.
DR Ensembl; ENSMUST00000108102; ENSMUSP00000103737; ENSMUSG00000001249. [O35453-1]
DR GeneID; 15451; -.
DR KEGG; mmu:15451; -.
DR UCSC; uc009gid.3; mouse. [O35453-1]
DR CTD; 3249; -.
DR MGI; MGI:1196620; Hpn.
DR VEuPathDB; HostDB:ENSMUSG00000001249; -.
DR eggNOG; KOG3627; Eukaryota.
DR GeneTree; ENSGT00940000159697; -.
DR InParanoid; O35453; -.
DR OrthoDB; 1314811at2759; -.
DR TreeFam; TF351678; -.
DR BRENDA; 3.4.21.106; 3474.
DR Reactome; R-MMU-6806942; MET Receptor Activation.
DR Reactome; R-MMU-8852405; Signaling by MST1.
DR BioGRID-ORCS; 15451; 2 hits in 76 CRISPR screens.
DR ChiTaRS; Hpn; mouse.
DR PRO; PR:O35453; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; O35453; protein.
DR Bgee; ENSMUSG00000001249; Expressed in right kidney and 182 other tissues.
DR ExpressionAtlas; O35453; baseline and differential.
DR Genevisible; O35453; MM.
DR GO; GO:0016324; C:apical plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0009986; C:cell surface; ISS:UniProtKB.
DR GO; GO:0005911; C:cell-cell junction; IMP:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; ISS:UniProtKB.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; ISO:MGI.
DR GO; GO:0005887; C:integral component of plasma membrane; ISS:UniProtKB.
DR GO; GO:0043025; C:neuronal cell body; IDA:UniProtKB.
DR GO; GO:0031965; C:nuclear membrane; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; IDA:MGI.
DR GO; GO:0008233; F:peptidase activity; ISO:MGI.
DR GO; GO:0004252; F:serine-type endopeptidase activity; ISO:MGI.
DR GO; GO:0070008; F:serine-type exopeptidase activity; IEA:InterPro.
DR GO; GO:0008236; F:serine-type peptidase activity; ISS:UniProtKB.
DR GO; GO:0034769; P:basement membrane disassembly; ISS:UniProtKB.
DR GO; GO:0042632; P:cholesterol homeostasis; IMP:MGI.
DR GO; GO:0090103; P:cochlea morphogenesis; IMP:UniProtKB.
DR GO; GO:0050910; P:detection of mechanical stimulus involved in sensory perception of sound; IMP:UniProtKB.
DR GO; GO:0060429; P:epithelium development; IEP:UniProtKB.
DR GO; GO:0010693; P:negative regulation of alkaline phosphatase activity; IMP:MGI.
DR GO; GO:0043066; P:negative regulation of apoptotic process; ISS:UniProtKB.
DR GO; GO:0050680; P:negative regulation of epithelial cell proliferation; ISS:UniProtKB.
DR GO; GO:0010719; P:negative regulation of epithelial to mesenchymal transition; ISS:UniProtKB.
DR GO; GO:0097195; P:pilomotor reflex; IMP:UniProtKB.
DR GO; GO:0043923; P:positive regulation by host of viral transcription; ISS:UniProtKB.
DR GO; GO:0030307; P:positive regulation of cell growth; ISS:UniProtKB.
DR GO; GO:0010628; P:positive regulation of gene expression; IMP:UniProtKB.
DR GO; GO:2000347; P:positive regulation of hepatocyte proliferation; ISS:UniProtKB.
DR GO; GO:0010756; P:positive regulation of plasminogen activation; ISS:UniProtKB.
DR GO; GO:2000611; P:positive regulation of thyroid hormone generation; IMP:UniProtKB.
DR GO; GO:0071805; P:potassium ion transmembrane transport; IMP:UniProtKB.
DR GO; GO:0006508; P:proteolysis; ISS:UniProtKB.
DR GO; GO:0008360; P:regulation of cell shape; ISS:UniProtKB.
DR GO; GO:0097066; P:response to thyroid hormone; IMP:UniProtKB.
DR GO; GO:0007605; P:sensory perception of sound; IMP:MGI.
DR CDD; cd00190; Tryp_SPc; 1.
DR Gene3D; 2.40.10.10; -; 2.
DR Gene3D; 3.10.250.10; -; 1.
DR InterPro; IPR038957; Hepsin.
DR InterPro; IPR015352; Hepsin-SRCR_dom.
DR InterPro; IPR009003; Peptidase_S1_PA.
DR InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin.
DR InterPro; IPR001314; Peptidase_S1A.
DR InterPro; IPR017448; SRCR-like_dom.
DR InterPro; IPR036772; SRCR-like_dom_sf.
DR InterPro; IPR001254; Trypsin_dom.
DR InterPro; IPR018114; TRYPSIN_HIS.
DR InterPro; IPR033116; TRYPSIN_SER.
DR PANTHER; PTHR24253:SF38; PTHR24253:SF38; 1.
DR Pfam; PF09272; Hepsin-SRCR; 1.
DR Pfam; PF00089; Trypsin; 1.
DR PRINTS; PR00722; CHYMOTRYPSIN.
DR SMART; SM00202; SR; 1.
DR SMART; SM00020; Tryp_SPc; 1.
DR SUPFAM; SSF50494; SSF50494; 1.
DR SUPFAM; SSF56487; SSF56487; 1.
DR PROSITE; PS50240; TRYPSIN_DOM; 1.
DR PROSITE; PS00134; TRYPSIN_HIS; 1.
DR PROSITE; PS00135; TRYPSIN_SER; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell membrane; Disulfide bond; Glycoprotein;
KW Hydrolase; Membrane; Protease; Reference proteome; Secreted;
KW Serine protease; Signal-anchor; Transmembrane; Transmembrane helix.
FT CHAIN 1..181
FT /note="Serine protease hepsin non-catalytic chain"
FT /evidence="ECO:0000255"
FT /id="PRO_0000027843"
FT CHAIN 182..436
FT /note="Serine protease hepsin catalytic chain"
FT /evidence="ECO:0000255"
FT /id="PRO_0000027844"
FT TOPO_DOM 1..38
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 39..59
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 60..436
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT DOMAIN 73..170
FT /note="SRCR"
FT DOMAIN 182..424
FT /note="Peptidase S1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT REGION 1..29
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 222
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:P05981"
FT ACT_SITE 276
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:P05981"
FT ACT_SITE 372
FT /note="Charge relay system"
FT /evidence="ECO:0000305|PubMed:9395459"
FT CARBOHYD 131
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 96..159
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 109..169
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 138..157
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 172..296
FT /note="Interchain (between non-catalytic and catalytic
FT chains)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 207..223
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 310..378
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 341..357
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DISULFID 368..400
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT VAR_SEQ 25..44
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:10411637,
FT ECO:0000303|PubMed:9395459"
FT /id="VSP_007232"
FT MUTAGEN 372
FT /note="S->A: Abolishes catalytic activity."
FT /evidence="ECO:0000269|PubMed:9395459"
FT CONFLICT 85
FT /note="F -> L (in Ref. 1; AAB84221)"
FT /evidence="ECO:0000305"
FT CONFLICT 204
FT /note="T -> Y (in Ref. 3; BAB22289)"
FT /evidence="ECO:0000305"
FT CONFLICT 214
FT /note="G -> R (in Ref. 3; BAB22289)"
FT /evidence="ECO:0000305"
FT CONFLICT 228..229
FT /note="NR -> ET (in Ref. 3; BAB22289)"
FT /evidence="ECO:0000305"
FT CONFLICT 264
FT /note="P -> L (in Ref. 3; BAB22289)"
FT /evidence="ECO:0000305"
FT CONFLICT 281
FT /note="H -> N (in Ref. 3; BAB22289)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 436 AA; 46821 MW; C0C71FFFF4D016F0 CRC64;
MAKEDEEPGA HRGGSTCSRP QPGKGGRTAA CCSRPKVAAL IVGTLLFLTG IGAASWAIVT
ILLQSDQEPL YQVQLSPGDS RLAVFDKTEG TWRLLCSSRS NARVAGLGCE EMGFLRALAH
SELDVRTAGA NGTSGFFCVD EGGLPLAQRL LDVISVCDCP RGRFLTATCQ DCGRRKLPVD
RIVGGQDSSL GRWPWQVSLR YDGTHLCGGS LLSGDWVLTA AHCFPERNRV LSRWRVFAGA
VARTSPHAVQ LGVQAVIYHG GYLPFRDPTI DENSNDIALV HLSSSLPLTE YIQPVCLPAA
GQALVDGKVC TVTGWGNTQF YGQQAMVLQE ARVPIISNEV CNSPDFYGNQ IKPKMFCAGY
PEGGIDACQG DSGGPFVCED SISGTSRWRL CGIVSWGTGC ALARKPGVYT KVTDFREWIF
KAIKTHSEAS GMVTQP
