ID HTRA1_MOUSE Reviewed; 480 AA.
AC Q9R118; Q8BN04; Q8BN05; Q91WS3; Q9QZK6;
DT 18-OCT-2001, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 27-MAR-2024, entry version 173.
DE RecName: Full=Serine protease HTRA1;
DE EC=3.4.21.-;
DE AltName: Full=High-temperature requirement A serine peptidase 1;
DE AltName: Full=Serine protease 11;
DE Flags: Precursor;
GN Name=Htra1; Synonyms=Htra, Prss11;
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], FUNCTION, INTERACTION WITH BMP4; TGFB2; TGFB1;
RP ACTIVIN A AND GDF5, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, AND
RP MUTAGENESIS OF SER-328.
RC STRAIN=ICR; TISSUE=Brain;
RX PubMed=14973287; DOI=10.1242/dev.00999;
RA Oka C., Tsujimoto R., Kajikawa M., Koshiba-Takeuchi K., Ina J., Yano M.,
RA Tsuchiya A., Ueta Y., Soma A., Kanda H., Matsumoto M., Kawaichi M.;
RT "HtrA1 serine protease inhibits signaling mediated by Tgfbeta family
RT proteins.";
RL Development 131:1041-1053(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=C57BL/6J; TISSUE=Ovary;
RA Hourvitz A., Hennebold J.D., King G., Negishi H., Erickson G.F., Roby J.A.,
RA Mayo K.E., Adashi E.Y.;
RT "Mouse insulin-like growth factor binding protein 5-directed endopeptidase:
RT structural assessment, evolutionary analysis, ovarian expression, hormonal
RT regulation and cellular localization.";
RL Submitted (AUG-1999) to the EMBL/GenBank/DDBJ databases.
RN [3]
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 (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 73-480.
RC STRAIN=C57BL/6J;
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 [6]
RP MUTAGENESIS OF PHE-171.
RX PubMed=15101818; DOI=10.1042/bj20040435;
RA Murwantoko I., Yano M., Ueta Y., Murasaki A., Kanda H., Oka C.,
RA Kawaichi M.;
RT "Binding of proteins to the PDZ domain regulates proteolytic activity of
RT HtrA1 serine protease.";
RL Biochem. J. 381:895-904(2004).
RN [7]
RP FUNCTION, TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=15993670; DOI=10.1016/j.bone.2005.03.015;
RA Tsuchiya A., Yano M., Tocharus J., Kojima H., Fukumoto M., Kawaichi M.,
RA Oka C.;
RT "Expression of mouse HtrA1 serine protease in normal bone and cartilage and
RT its upregulation in joint cartilage damaged by experimental arthritis.";
RL Bone 37:323-336(2005).
RN [8]
RP FUNCTION, TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=18551132; DOI=10.1038/cdd.2008.82;
RA Launay S., Maubert E., Lebeurrier N., Tennstaedt A., Campioni M.,
RA Docagne F., Gabriel C., Dauphinot L., Potier M.C., Ehrmann M., Baldi A.,
RA Vivien D.;
RT "HtrA1-dependent proteolysis of TGF-beta controls both neuronal maturation
RT and developmental survival.";
RL Cell Death Differ. 15:1408-1416(2008).
RN [9]
RP DISRUPTION PHENOTYPE, AND FUNCTION.
RX PubMed=22049084; DOI=10.1074/jbc.m111.275990;
RA Zhang L., Lim S.L., Du H., Zhang M., Kozak I., Hannum G., Wang X.,
RA Ouyang H., Hughes G., Zhao L., Zhu X., Lee C., Su Z., Zhou X., Shaw R.,
RA Geum D., Wei X., Zhu J., Ideker T., Oka C., Wang N., Yang Z., Shaw P.X.,
RA Zhang K.;
RT "High temperature requirement factor A1 (HTRA1) gene regulates angiogenesis
RT through transforming growth factor-beta family member growth
RT differentiation factor 6.";
RL J. Biol. Chem. 287:1520-1526(2012).
CC -!- FUNCTION: Serine protease with a variety of targets, including
CC extracellular matrix proteins such as fibronectin. HTRA1-generated
CC fibronectin fragments further induce synovial cells to up-regulate MMP1
CC and MMP3 production. May also degrade proteoglycans, such as aggrecan,
CC decorin and fibromodulin. Through cleavage of proteoglycans, may
CC release soluble FGF-glycosaminoglycan complexes that promote the range
CC and intensity of FGF signals in the extracellular space. Regulates the
CC availability of insulin-like growth factors (IGFs) by cleaving IGF-
CC binding proteins. Inhibits signaling mediated by TGF-beta family
CC members. This activity requires the integrity of the catalytic site,
CC but it is unclear whether it leads to the proteolytic degradation of
CC TGF-beta proteins themselves (PubMed:18551132) or not
CC (PubMed:14973287). By acting on TGF-beta signaling, may regulate many
CC physiological processes, including retinal angiogenesis and neuronal
CC survival and maturation during development. Intracellularly, degrades
CC TSC2, leading to the activation of TSC2 downstream targets.
CC {ECO:0000269|PubMed:14973287, ECO:0000269|PubMed:15993670,
CC ECO:0000269|PubMed:18551132, ECO:0000269|PubMed:22049084}.
CC -!- SUBUNIT: Forms homotrimers. In the presence of substrate, may form
CC higher-order multimers in a PDZ-independent manner (By similarity).
CC Interacts with TGF-beta family members, including BMP4, TGFB1, TGFB2,
CC activin A and GDF5. {ECO:0000250, ECO:0000269|PubMed:14973287}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q92743}.
CC Secreted {ECO:0000250|UniProtKB:Q92743}. Cytoplasm, cytosol
CC {ECO:0000250|UniProtKB:Q92743}. Note=Predominantly secreted. Also found
CC associated with the plasma membrane. {ECO:0000250|UniProtKB:Q92743}.
CC -!- TISSUE SPECIFICITY: In the brain, mainly expressed in cortical areas
CC both in glial cells and neurons (at protein level). In bones, deposited
CC in the matrix, with higher level in newly formed bone compared to fully
CC calcified bone (at protein level). Also expressed in the tendons (at
CC protein level). In the articular cartilage, detected only in the
CC deepest zone of the joint cartilage. Not detected in the chondrocytes
CC of the growth plate (at protein level). In an experimental arthritis
CC model, at early disease stages, up-regulated in articular chondrocytes
CC in the deep layers of the cartilage (at protein level). As arthritis
CC progresses, chondrocyte expression expands toward the surface.
CC {ECO:0000269|PubMed:14973287, ECO:0000269|PubMed:15993670,
CC ECO:0000269|PubMed:18551132}.
CC -!- DEVELOPMENTAL STAGE: First detected at 10.5 dpc. At 11.5 dpc, in the
CC developing heart, expressed in the atrioventricular endocardial cushion
CC and the outflow tract (at protein level). At 14.5 dpc, strong
CC expression in the outflow tracts, including valves. In the developing
CC skeleton, expressed at 12.5 dpc in the vertebral column and limbs. At
CC 14.5 dpc, expressed in rudiments of tendons and ligaments along the
CC vertebrae, as well as in mesenchymal cells surrounding precartilage
CC condensations. Not detected in precartilage condensations, nor in
CC chondrocytes, but strongly expressed in ossification centers. At 17.5
CC dpc, in the hind limb, significant expression persists in tendons and
CC ligaments, but expression in the forming joints is reduced. At this
CC stage, weakly detected in the thin layer of articular surfaces.
CC Postnatally, in long bones, expressed by terminally differentiated
CC hypertrophic chondrocytes that are committed to degeneration and
CC eventually replaced by bone, as well as by osteoblasts at late
CC differentiation stages and by mature osteocytes. In the developing
CC brain, expressed in specific regions of the neuroepithelium in the
CC forebrain and hindbrain adjacent to the forming choroid plexus. From
CC 17.5 dpc till birth, expressed in neurogenic areas including
CC ventricular zones (at protein level). At 12.5 and 14.5 dpc, expressed
CC in Muellerian duct cells and in the surrounding mesenchyme in both male
CC and female gonads. In the lung, detected in the mesenchymal cells.
CC Expressed at 12.5 dpc in abdominal skin, both in epidermis and dermis.
CC Also expressed in the epithelium of developing whiskers at 14.5 dpc. At
CC later stages, localized in the basal layer of epidermis and in the
CC invading epidermal cells that formed the whisker rudiments (at protein
CC level). 9 days after birth, detected in the whisker outer root sheet
CC (at protein level). {ECO:0000269|PubMed:14973287,
CC ECO:0000269|PubMed:15993670, ECO:0000269|PubMed:18551132}.
CC -!- DOMAIN: The IGFBP N-terminal domain mediates interaction with TSC2
CC substrate. {ECO:0000250}.
CC -!- DISRUPTION PHENOTYPE: Mutants mice exhibit reduced retinal capillary
CC density, as compared to wild type animals, in all 3 retinal layers,
CC nerve fiber layer, as well as inner and outer plexiform layers.
CC {ECO:0000269|PubMed:22049084}.
CC -!- SIMILARITY: Belongs to the peptidase S1C family. {ECO:0000305}.
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DR EMBL; AF172994; AAD49422.1; -; mRNA.
DR EMBL; AF179369; AAD52682.1; -; mRNA.
DR EMBL; CH466531; EDL17689.1; -; Genomic_DNA.
DR EMBL; BC013516; AAH13516.1; -; mRNA.
DR EMBL; AK090320; BAC41168.1; -; mRNA.
DR EMBL; AK090321; BAC41169.1; -; mRNA.
DR CCDS; CCDS21908.1; -.
DR RefSeq; NP_062510.2; NM_019564.3.
DR AlphaFoldDB; Q9R118; -.
DR SMR; Q9R118; -.
DR BioGRID; 207847; 7.
DR IntAct; Q9R118; 2.
DR MINT; Q9R118; -.
DR STRING; 10090.ENSMUSP00000006367; -.
DR MEROPS; S01.277; -.
DR CarbonylDB; Q9R118; -.
DR PhosphoSitePlus; Q9R118; -.
DR SwissPalm; Q9R118; -.
DR MaxQB; Q9R118; -.
DR PaxDb; 10090-ENSMUSP00000006367; -.
DR PeptideAtlas; Q9R118; -.
DR ProteomicsDB; 273199; -.
DR Antibodypedia; 32265; 315 antibodies from 32 providers.
DR DNASU; 56213; -.
DR Ensembl; ENSMUST00000006367.8; ENSMUSP00000006367.8; ENSMUSG00000006205.14.
DR GeneID; 56213; -.
DR KEGG; mmu:56213; -.
DR UCSC; uc009kau.2; mouse.
DR AGR; MGI:1929076; -.
DR CTD; 5654; -.
DR MGI; MGI:1929076; Htra1.
DR VEuPathDB; HostDB:ENSMUSG00000006205; -.
DR eggNOG; KOG1320; Eukaryota.
DR GeneTree; ENSGT00940000156955; -.
DR HOGENOM; CLU_020120_6_2_1; -.
DR InParanoid; Q9R118; -.
DR OMA; THGWVLE; -.
DR OrthoDB; 2159919at2759; -.
DR PhylomeDB; Q9R118; -.
DR TreeFam; TF323480; -.
DR BRENDA; 3.4.21.107; 3474.
DR Reactome; R-MMU-1474228; Degradation of the extracellular matrix.
DR BioGRID-ORCS; 56213; 1 hit in 80 CRISPR screens.
DR ChiTaRS; Htra1; mouse.
DR PRO; PR:Q9R118; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; Q9R118; Protein.
DR Bgee; ENSMUSG00000006205; Expressed in decidua and 322 other cell types or tissues.
DR Genevisible; Q9R118; MM.
DR GO; GO:0062023; C:collagen-containing extracellular matrix; HDA:BHF-UCL.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0019838; F:growth factor binding; IEA:UniProtKB-KW.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0140677; F:molecular function activator activity; ISO:MGI.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IBA:GO_Central.
DR GO; GO:0008236; F:serine-type peptidase activity; IDA:UniProtKB.
DR GO; GO:0060718; P:chorionic trophoblast cell differentiation; IMP:MGI.
DR GO; GO:0030514; P:negative regulation of BMP signaling pathway; IDA:MGI.
DR GO; GO:0050687; P:negative regulation of defense response to virus; ISO:MGI.
DR GO; GO:0030512; P:negative regulation of transforming growth factor beta receptor signaling pathway; IDA:MGI.
DR GO; GO:0001890; P:placenta development; IMP:MGI.
DR GO; GO:0043065; P:positive regulation of apoptotic process; IBA:GO_Central.
DR GO; GO:0050679; P:positive regulation of epithelial cell proliferation; ISO:MGI.
DR GO; GO:0012501; P:programmed cell death; IBA:GO_Central.
DR GO; GO:0006508; P:proteolysis; IDA:UniProtKB.
DR CDD; cd00104; KAZAL_FS; 1.
DR CDD; cd00987; PDZ_serine_protease; 1.
DR Gene3D; 2.30.42.10; -; 1.
DR Gene3D; 2.40.10.120; -; 1.
DR Gene3D; 3.30.60.30; -; 1.
DR Gene3D; 4.10.40.20; -; 1.
DR InterPro; IPR009030; Growth_fac_rcpt_cys_sf.
DR InterPro; IPR000867; IGFBP-like.
DR InterPro; IPR002350; Kazal_dom.
DR InterPro; IPR036058; Kazal_dom_sf.
DR InterPro; IPR001478; PDZ.
DR InterPro; IPR041489; PDZ_6.
DR InterPro; IPR036034; PDZ_sf.
DR InterPro; IPR009003; Peptidase_S1_PA.
DR InterPro; IPR001940; Peptidase_S1C.
DR PANTHER; PTHR22939; SERINE PROTEASE FAMILY S1C HTRA-RELATED; 1.
DR PANTHER; PTHR22939:SF13; SERINE PROTEASE HTRA1; 1.
DR Pfam; PF00219; IGFBP; 1.
DR Pfam; PF07648; Kazal_2; 1.
DR Pfam; PF17820; PDZ_6; 1.
DR Pfam; PF13365; Trypsin_2; 1.
DR PRINTS; PR00834; PROTEASES2C.
DR SMART; SM00121; IB; 1.
DR SMART; SM00280; KAZAL; 1.
DR SMART; SM00228; PDZ; 1.
DR SUPFAM; SSF57184; Growth factor receptor domain; 1.
DR SUPFAM; SSF100895; Kazal-type serine protease inhibitors; 1.
DR SUPFAM; SSF50156; PDZ domain-like; 1.
DR SUPFAM; SSF50494; Trypsin-like serine proteases; 1.
DR PROSITE; PS51323; IGFBP_N_2; 1.
DR PROSITE; PS51465; KAZAL_2; 1.
DR PROSITE; PS50106; PDZ; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Cytoplasm; Disulfide bond; Growth factor binding; Hydrolase;
KW Membrane; Protease; Reference proteome; Secreted; Serine protease; Signal.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT CHAIN 23..480
FT /note="Serine protease HTRA1"
FT /id="PRO_0000026944"
FT DOMAIN 33..113
FT /note="IGFBP N-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00653"
FT DOMAIN 98..157
FT /note="Kazal-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT DOMAIN 365..467
FT /note="PDZ"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT REGION 204..364
FT /note="Serine protease"
FT ACT_SITE 220
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:Q92743"
FT ACT_SITE 250
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:Q92743"
FT ACT_SITE 328
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:Q92743"
FT SITE 169
FT /note="Involved in trimer stabilization"
FT /evidence="ECO:0000250|UniProtKB:Q92743"
FT SITE 171
FT /note="Involved in trimer stabilization"
FT /evidence="ECO:0000250|UniProtKB:Q92743"
FT SITE 278
FT /note="Involved in trimer stabilization"
FT /evidence="ECO:0000250|UniProtKB:Q92743"
FT DISULFID 37..62
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00653"
FT DISULFID 41..64
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00653"
FT DISULFID 46..65
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00653"
FT DISULFID 53..68
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00653"
FT DISULFID 76..89
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00653"
FT DISULFID 83..110
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00653"
FT DISULFID 112..130
FT /evidence="ECO:0000305"
FT DISULFID 119..155
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT MUTAGEN 171
FT /note="F->D: Loss of efficient trimer formation."
FT /evidence="ECO:0000269|PubMed:15101818"
FT MUTAGEN 328
FT /note="S->A: Loss of enzymatic activity. No effect on BMP4-
FT binding."
FT /evidence="ECO:0000269|PubMed:14973287"
FT CONFLICT 91
FT /note="V -> L (in Ref. 1; AAD49422)"
FT /evidence="ECO:0000305"
FT CONFLICT 143
FT /note="R -> P (in Ref. 1; AAD49422)"
FT /evidence="ECO:0000305"
FT CONFLICT 179
FT /note="I -> F (in Ref. 1; AAD49422)"
FT /evidence="ECO:0000305"
FT CONFLICT 182
FT /note="A -> D (in Ref. 1; AAD49422)"
FT /evidence="ECO:0000305"
FT CONFLICT 185..186
FT /note="HI -> KH (in Ref. 1; AAD49422)"
FT /evidence="ECO:0000305"
FT CONFLICT 241
FT /note="K -> I (in Ref. 1; AAD49422)"
FT /evidence="ECO:0000305"
FT CONFLICT 259
FT /note="Q -> K (in Ref. 5; BAC41168)"
FT /evidence="ECO:0000305"
FT CONFLICT 366
FT /note="E -> Q (in Ref. 4; AAH13516)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 480 AA; 51214 MW; 92BDDA85CF5B12B7 CRC64;
MQSLRTTLLS LLLLLLAAPS LALPSGTGRS APAATVCPEH CDPTRCAPPP TDCEGGRVRD
ACGCCEVCGA LEGAACGLQE GPCGEGLQCV VPFGVPASAT VRRRAQAGLC VCASSEPVCG
SDAKTYTNLC QLRAASRRSE KLRQPPVIVL QRGACGQGQE DPNSLRHKYN FIADVVEKIA
PAVVHIELYR KLPFSKREVP VASGSGFIVS EDGLIVTNAH VVTNKNRVKV ELKNGATYEA
KIKDVDEKAD IALIKIDHQG KLPVLLLGRS SELRPGEFVV AIGSPFSLQN TVTTGIVSTT
QRGGKELGLR NSDMDYIQTD AIINYGNSGG PLVNLDGEVI GINTLKVTAG ISFAIPSDKI
KKFLTESHDR QAKGKAVTKK KYIGIRMMSL TSSKAKELKD RHRDFPDVLS GAYIIEVIPD
TPAEAGGLKE NDVIISINGQ SVVTANDVSD VIKKENTLNM VVRRGNEDIV ITVIPEEIDP
//
