PAPP1_MOUSE
ID PAPP1_MOUSE Reviewed; 1624 AA.
AC Q8R4K8; Q80VW3; Q80YY1; Q8K423; Q8R4K7; Q9ES06; Q9JK57;
DT 07-DEC-2004, integrated into UniProtKB/Swiss-Prot.
DT 07-DEC-2004, sequence version 2.
DT 03-AUG-2022, entry version 149.
DE RecName: Full=Pappalysin-1;
DE EC=3.4.24.79;
DE AltName: Full=Insulin-like growth factor-dependent IGF-binding protein 4 protease;
DE Short=IGF-dependent IGFBP-4 protease;
DE Short=IGFBP-4ase;
DE AltName: Full=Pregnancy-associated plasma protein A;
DE Short=PAPP-A;
DE Flags: Precursor;
GN Name=Pappa;
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 [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 [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 80-1624 (ISOFORMS 1 AND 2), FUNCTION, AND
RP TISSUE SPECIFICITY.
RX PubMed=11985604; DOI=10.1046/j.1432-1033.2002.02883.x;
RA Soe R., Overgaard M.T., Thomsen A.R., Laursen L.S., Olsen I.M.,
RA Sottrup-Jensen L., Haaning J., Giudice L.C., Conover C.A., Oxvig C.;
RT "Expression of recombinant murine pregnancy-associated plasma protein-A
RT (PAPP-A) and a novel variant (PAPP-Ai) with differential proteolytic
RT activity.";
RL Eur. J. Biochem. 269:2247-2256(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 136-489 (ISOFORM 1).
RC STRAIN=129/SvJ;
RX PubMed=12213189; DOI=10.1016/s1096-6374(02)00046-1;
RA Qin X., Sexton C., Byun D., Strong D.D., Baylink D.J., Mohan S.;
RT "Differential regulation of pregnancy associated plasma protein (PAPP)-A
RT during pregnancy in human and mouse.";
RL Growth Horm. IGF Res. 12:359-366(2002).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 258-1624 (ISOFORM 1), AND TISSUE SPECIFICITY.
RC STRAIN=C57BL/6J;
RX PubMed=11956166; DOI=10.1210/endo.143.5.8769;
RA Hourvitz A., Kuwahara A., Hennebold J.D., Tavares A.B., Negishi H.,
RA Lee T.H., Erickson G.F., Adashi E.Y.;
RT "The regulated expression of the pregnancy-associated plasma protein-A in
RT the rodent ovary: a proposed role in the development of dominant follicles
RT and of corpora lutea.";
RL Endocrinology 143:1833-1844(2002).
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1157-1624 (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Embryo;
RA Olesen C., Hansen C., Hayashizaki Y., Byskov A., Tommerup N.;
RT "Partial sequence of Mus musculus Mus musculus pregnancy-associated plasma
RT protein A (Pappa).";
RL Submitted (APR-2000) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Metalloproteinase which specifically cleaves IGFBP-4 and
CC IGFBP-5, resulting in release of bound IGF. Cleavage of IGFBP-4 is
CC dramatically enhanced by the presence of IGF, whereas cleavage of
CC IGFBP-5 is slightly inhibited by the presence of IGF. Isoform 2 cleaves
CC IGFBP-4 very slowly compared to PAPP-A, but its ability to cleave
CC IGFBP-5 is unaffected. {ECO:0000269|PubMed:11985604}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Cleavage of the 135-Met-|-Lys-136 bond in insulin-like growth
CC factor binding protein (IGFBP)-4, and the 143-Ser-|-Lys-144 bond in
CC IGFBP-5.; EC=3.4.24.79;
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000250};
CC -!- SUBUNIT: Homodimer; disulfide-linked. In pregnancy serum, predominantly
CC found as a disulfide-linked 2:2 heterotetramer with the proform of PRG2
CC (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8R4K8-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8R4K8-2; Sequence=VSP_012193;
CC -!- TISSUE SPECIFICITY: Detected in kidney, spleen, brain, ovary, breast,
CC skin, prostate, uterus, and placenta. {ECO:0000269|PubMed:11956166,
CC ECO:0000269|PubMed:11985604}.
CC -!- SIMILARITY: Belongs to the peptidase M43B family. {ECO:0000305}.
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DR EMBL; AL691454; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL691491; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AF439513; AAM12687.1; -; mRNA.
DR EMBL; AF439514; AAM12688.1; -; mRNA.
DR EMBL; AF510317; AAM44048.1; -; Genomic_DNA.
DR EMBL; AF258461; AAG09799.1; -; mRNA.
DR EMBL; AF260433; AAF70319.1; -; mRNA.
DR CCDS; CCDS18267.1; -. [Q8R4K8-1]
DR RefSeq; NP_067337.1; NM_021362.1. [Q8R4K8-1]
DR AlphaFoldDB; Q8R4K8; -.
DR BioGRID; 202026; 4.
DR STRING; 10090.ENSMUSP00000081545; -.
DR MEROPS; M43.004; -.
DR GlyGen; Q8R4K8; 13 sites.
DR iPTMnet; Q8R4K8; -.
DR PhosphoSitePlus; Q8R4K8; -.
DR CPTAC; non-CPTAC-3337; -.
DR PaxDb; Q8R4K8; -.
DR PeptideAtlas; Q8R4K8; -.
DR PRIDE; Q8R4K8; -.
DR ProteomicsDB; 294006; -. [Q8R4K8-1]
DR ProteomicsDB; 294007; -. [Q8R4K8-2]
DR Antibodypedia; 3385; 876 antibodies from 32 providers.
DR DNASU; 18491; -.
DR Ensembl; ENSMUST00000084501; ENSMUSP00000081545; ENSMUSG00000028370. [Q8R4K8-1]
DR GeneID; 18491; -.
DR KEGG; mmu:18491; -.
DR UCSC; uc008thm.1; mouse. [Q8R4K8-1]
DR UCSC; uc012dgb.1; mouse. [Q8R4K8-2]
DR CTD; 5069; -.
DR MGI; MGI:97479; Pappa.
DR VEuPathDB; HostDB:ENSMUSG00000028370; -.
DR eggNOG; ENOG502QQ7Z; Eukaryota.
DR GeneTree; ENSGT00940000156654; -.
DR HOGENOM; CLU_002636_2_0_1; -.
DR InParanoid; Q8R4K8; -.
DR OMA; FIDQTQC; -.
DR OrthoDB; 105200at2759; -.
DR PhylomeDB; Q8R4K8; -.
DR TreeFam; TF331636; -.
DR BRENDA; 3.4.24.79; 3474.
DR Reactome; R-MMU-381426; Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs).
DR BioGRID-ORCS; 18491; 1 hit in 73 CRISPR screens.
DR ChiTaRS; Pappa; mouse.
DR PRO; PR:Q8R4K8; -.
DR Proteomes; UP000000589; Chromosome 4.
DR RNAct; Q8R4K8; protein.
DR Bgee; ENSMUSG00000028370; Expressed in stroma of bone marrow and 147 other tissues.
DR Genevisible; Q8R4K8; MM.
DR GO; GO:0005576; C:extracellular region; ISO:MGI.
DR GO; GO:0005615; C:extracellular space; HDA:BHF-UCL.
DR GO; GO:0004175; F:endopeptidase activity; IDA:MGI.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004222; F:metalloendopeptidase activity; ISO:MGI.
DR GO; GO:0008237; F:metallopeptidase activity; ISO:MGI.
DR GO; GO:0007166; P:cell surface receptor signaling pathway; IBA:GO_Central.
DR GO; GO:0007565; P:female pregnancy; IEA:Ensembl.
DR GO; GO:0030163; P:protein catabolic process; IEA:Ensembl.
DR GO; GO:0006508; P:proteolysis; IBA:GO_Central.
DR GO; GO:0071548; P:response to dexamethasone; IEA:Ensembl.
DR GO; GO:0032354; P:response to follicle-stimulating hormone; IEA:Ensembl.
DR CDD; cd00033; CCP; 4.
DR CDD; cd04275; ZnMc_pappalysin_like; 1.
DR Gene3D; 3.40.390.10; -; 1.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR006558; LamG-like.
DR InterPro; IPR024079; MetalloPept_cat_dom_sf.
DR InterPro; IPR011936; Myxo_disulph_rpt.
DR InterPro; IPR000800; Notch_dom.
DR InterPro; IPR030433; PAPPA.
DR InterPro; IPR043543; PAPPA/PAPPA2.
DR InterPro; IPR008754; Peptidase_M43.
DR InterPro; IPR035976; Sushi/SCR/CCP_sf.
DR InterPro; IPR000436; Sushi_SCR_CCP_dom.
DR PANTHER; PTHR46130; PTHR46130; 1.
DR PANTHER; PTHR46130:SF2; PTHR46130:SF2; 1.
DR Pfam; PF05572; Peptidase_M43; 1.
DR Pfam; PF00084; Sushi; 3.
DR SMART; SM00032; CCP; 4.
DR SMART; SM00560; LamGL; 1.
DR SMART; SM00004; NL; 3.
DR SUPFAM; SSF49899; SSF49899; 1.
DR SUPFAM; SSF57535; SSF57535; 4.
DR TIGRFAMs; TIGR02232; myxo_disulf_rpt; 1.
DR PROSITE; PS50923; SUSHI; 5.
DR PROSITE; PS00142; ZINC_PROTEASE; 1.
PE 2: Evidence at transcript level;
KW Alternative splicing; Disulfide bond; Glycoprotein; Hydrolase;
KW Metal-binding; Metalloprotease; Protease; Reference proteome; Repeat;
KW Secreted; Signal; Sushi; Zinc; Zymogen.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT PROPEP 23..81
FT /evidence="ECO:0000250"
FT /id="PRO_0000029247"
FT CHAIN 82..1624
FT /note="Pappalysin-1"
FT /id="PRO_0000029248"
FT DOMAIN 1210..1279
FT /note="Sushi 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DOMAIN 1280..1341
FT /note="Sushi 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DOMAIN 1342..1409
FT /note="Sushi 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DOMAIN 1410..1470
FT /note="Sushi 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DOMAIN 1473..1553
FT /note="Sushi 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT REGION 28..93
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 272..583
FT /note="Metalloprotease"
FT ACT_SITE 560
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT BINDING 559
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT BINDING 563
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT BINDING 569
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT CARBOHYD 387
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 398
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 426
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 516
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 598
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 616
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 722
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 822
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1023
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1219
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1223
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1320
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1516
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 141..232
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DISULFID 324..619
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DISULFID 329..654
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DISULFID 411..425
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DISULFID 421..437
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DISULFID 454..470
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DISULFID 458
FT /note="Interchain (with C-49 in PRG2 proform)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DISULFID 471..482
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DISULFID 580..597
FT /note="Or C-580 with C-609"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DISULFID 584..609
FT /note="Or C-584 with C-597"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DISULFID 707..875
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DISULFID 710..878
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DISULFID 729
FT /note="Interchain (with C-170 in PRG2 proform)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DISULFID 750..832
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DISULFID 772..778
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DISULFID 944..972
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DISULFID 957..968
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DISULFID 980..987
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DISULFID 996..1008
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DISULFID 1033..1067
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DISULFID 1048..1136
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DISULFID 1189..1202
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DISULFID 1207
FT /note="Interchain"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DISULFID 1212..1266
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DISULFID 1224..1235
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DISULFID 1239..1277
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DISULFID 1282..1326
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DISULFID 1297..1307
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DISULFID 1311..1339
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DISULFID 1343..1396
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DISULFID 1359..1370
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DISULFID 1374..1407
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DISULFID 1412..1455
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DISULFID 1425..1435
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DISULFID 1439..1468
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DISULFID 1475..1536
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DISULFID 1489..1499
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DISULFID 1503..1551
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DISULFID 1555..1573
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT VAR_SEQ 490
FT /note="R -> RQSIRKRAHVVEESWLPHGKQKAKKRKRTR (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:11985604"
FT /id="VSP_012193"
SQ SEQUENCE 1624 AA; 181318 MW; B09404C206CB60D1 CRC64;
MRLWSWVLRL GLLSAALGCG LAERPRRVRR DPRAVRPPRP AAGPATCATR AARGRRASPP
PPPGGAWEAV RVPRRRQQRA ARGAEEPSPP SRALYFSGRG EQLRLRADLE LPRDAFTLQV
WLRAEGGQKS PAVITGLYDK CSYTSRDRGW VMGIHTTSDQ GNRDPRYFFS LKTDRARKVT
TIDAHRSYLP GQWVHLAATY DGRLMKLYMN GAQVATSAEQ VGGIFSPLTQ KCKVLMLGGS
ALNHNFRGHI EHFSLWKVAR TQREIVSDME TRGLHTPLPQ LLLQENWDNV KRTWSPMKDG
NSPQVEFSNA HGFLLDTNLE PPLCGQTLCD NTEVISSYNQ LPSFRQPKVV RYRVVNIYDD
HHENPTVSWQ QIDFQHQQLA EAFQHYNISW ELEVLNINSS SLRHRLILAN CDISKIGDEK
CDPECNHTLT GHDGGDCRQL RYPAFMKKQQ NGVCDMDCNY ERFNFDGGEC CDPDITDVTK
TCFDPDSPHR AYLDVNELKN ILRLDGSTHL NIFFANSSEE ELAGVATWPW DKEALMHLGG
IVLNPSFYGI PGHTHTMIHE IGHSLGLYHI FRGISEIQSC SDPCMETEPS FETGDLCNDT
NPAPKHKFCG DPGPGNDTCG FHGFFNTPYN NFMSYADDDC TDSFTPNQVS RMHCYLDLVY
QSWQPSRKPA PVALAPQVVG HTMDSVMLEW FPPIDGHFFE RELGSACDLC LEGRILVQYA
FNASSPMPCG PSGHWSPREA EGHPDVEQPC KSSVRTWSPN SAVNPHTVPP ACPEPQGCYL
ELEFRYPLVP ESLTIWVTFV SSDWDSSGAV NDIKLLTISG KNISLGPQNV FCDIPLTIRL
RDVGEEVYGI QIYTLDEHLE IDAAMLTSTV DSPLCLQCKP LQYKVLRDPP LLEDVASLLH
LNRRFMDTDL KLGSVYQYRI ITISGNEESE PSPAAIYTHG SGYCGDGVIQ KDQGEECDDM
NKVNGDGCSL FCKQEVSFNC IDEPSRCYFH DGDGMCEEFE QKTSIKDCGV YTPQGFLDQW
ASNASVSHQD QQCPGWVVIG QPAASQVCRT KVIDLSEGIS QHAWYPCTIT YPYYHLPQTT
FWLQTYFSQP MVAAAVIIHL VTDGTYYGDQ KQETISVQLL DTKDQSHDLG LHVLSCRNNP
LIIPVVHDLS QPFYHSQAVH VSFSSPLVAI SGVALRSFDN FDPVTLSSCQ RGETYSPAEQ
SCVHFACQAA DCPELAVGNA SLNCSSNHHY HGAQCTVSCQ TGYVLQIQRD DELIKSQVGP
SITVTCTEGK WNKQVACEPV DCGIPDHHHV YAASFSCPEG TTFGRRCSFQ CRHPAQLKGN
NSFLTCMEDG LWSFPEALCE LMCLAPPPVP NADLQTARCR ENKHKVGSFC KYKCKPGYHV
PGSSRKSKKR AFKTQCTQDG SWQEGTCVPV TCDPPPPKFH GLYQCTNGFQ FNSECRIKCE
DSDASQGRGS NIIHCRKDGT WSGSFHVCRE MQGQCSAPNQ LNSNLKLQCP DGYAIGSECA
ISCLDHNSES IILPVNLTVR DIPHWMNPTR VQRIVCTAGL QWYPHPALIH CVKGCEPFMG
DNYCDAINNR AFCNYDGGDC CTSTVKTKKV TPFPMSCDLQ NDCACRDPEA QEHNRKDLRG
YSHG
