ZAN_MOUSE
ID ZAN_MOUSE Reviewed; 5376 AA.
AC O88799; O08647;
DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 29-SEP-2021, entry version 136.
DE RecName: Full=Zonadhesin;
DE Flags: Precursor;
GN Name=Zan;
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=Testis;
RX PubMed=9452463; DOI=10.1074/jbc.273.6.3415;
RA Gao Z., Garbers D.L.;
RT "Species diversity in the structure of zonadhesin, a sperm-specific
RT membrane protein containing multiple cell adhesion molecule-like domains.";
RL J. Biol. Chem. 273:3415-3421(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 4864-5376.
RC TISSUE=Testis;
RX PubMed=9126492; DOI=10.1006/geno.1997.4620;
RA Gao Z., Harumi T., Garbers D.L.;
RT "Chromosome localization of the mouse zonadhesin gene and the human
RT zonadhesin gene (ZAN).";
RL Genomics 41:119-122(1997).
RN [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=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).
CC -!- FUNCTION: Binds in a species-specific manner to the zona pellucida of
CC the egg. May be involved in gamete recognition and/or signaling.
CC -!- SUBUNIT: Probably forms covalent oligomers.
CC -!- SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane
CC protein. Note=Exclusively on the apical region of the sperm head.
CC -!- TISSUE SPECIFICITY: In testis, primarily in haploid spermatids.
CC -!- DOMAIN: The MAM domains probably mediates sperm adhesion to the zona
CC pellucida.
CC -!- DOMAIN: During sperm migration through the reproductive tracts, the
CC mucin-like domain might inhibit inappropriate trapping of spermatozoa
CC or promoting adhesion to the oviductal isthmus.
CC -!- DOMAIN: The VWFD domain 2 may mediate covalent oligomerization.
CC {ECO:0000250}.
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DR EMBL; U97068; AAC26680.1; -; mRNA.
DR EMBL; U83190; AAC53125.1; -; mRNA.
DR PIR; T42215; T42215.
DR SMR; O88799; -.
DR IntAct; O88799; 1.
DR MINT; O88799; -.
DR STRING; 10090.ENSMUSP00000114068; -.
DR GlyGen; O88799; 32 sites.
DR iPTMnet; O88799; -.
DR PhosphoSitePlus; O88799; -.
DR PaxDb; O88799; -.
DR PRIDE; O88799; -.
DR ProteomicsDB; 275335; -.
DR MGI; MGI:106656; Zan.
DR eggNOG; KOG1216; Eukaryota.
DR InParanoid; O88799; -.
DR PhylomeDB; O88799; -.
DR PRO; PR:O88799; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; O88799; protein.
DR GO; GO:0031012; C:extracellular matrix; IBA:GO_Central.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0050840; F:extracellular matrix binding; ISO:MGI.
DR GO; GO:0007339; P:binding of sperm to zona pellucida; ISO:MGI.
DR GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR GO; GO:2000359; P:regulation of binding of sperm to zona pellucida; IMP:MGI.
DR CDD; cd06263; MAM; 3.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR000742; EGF-like_dom.
DR InterPro; IPR003645; Fol_N.
DR InterPro; IPR000998; MAM_dom.
DR InterPro; IPR036084; Ser_inhib-like_sf.
DR InterPro; IPR002919; TIL_dom.
DR InterPro; IPR025615; TILa_dom.
DR InterPro; IPR014853; Unchr_dom_Cys-rich.
DR InterPro; IPR001007; VWF_dom.
DR InterPro; IPR001846; VWF_type-D.
DR Pfam; PF00629; MAM; 3.
DR Pfam; PF01826; TIL; 25.
DR Pfam; PF12714; TILa; 25.
DR Pfam; PF00094; VWD; 4.
DR SMART; SM00832; C8; 4.
DR SMART; SM00181; EGF; 16.
DR SMART; SM00274; FOLN; 20.
DR SMART; SM00137; MAM; 3.
DR SMART; SM00214; VWC; 23.
DR SMART; SM00215; VWC_out; 15.
DR SMART; SM00216; VWD; 4.
DR SUPFAM; SSF49899; SSF49899; 3.
DR SUPFAM; SSF57567; SSF57567; 25.
DR PROSITE; PS00022; EGF_1; 1.
DR PROSITE; PS01186; EGF_2; 18.
DR PROSITE; PS50026; EGF_3; 1.
DR PROSITE; PS00740; MAM_1; 1.
DR PROSITE; PS50060; MAM_2; 3.
DR PROSITE; PS51233; VWFD; 4.
PE 1: Evidence at protein level;
KW Cell adhesion; Cell membrane; Disulfide bond; EGF-like domain;
KW Glycoprotein; Membrane; Reference proteome; Repeat; Signal; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..17
FT /evidence="ECO:0000255"
FT CHAIN 18..5376
FT /note="Zonadhesin"
FT /id="PRO_0000007784"
FT TOPO_DOM 18..5310
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 5311..5337
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 5338..5376
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 45..210
FT /note="MAM 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00128"
FT DOMAIN 215..374
FT /note="MAM 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00128"
FT DOMAIN 377..542
FT /note="MAM 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00128"
FT DOMAIN 1171..1220
FT /note="TIL 1"
FT DOMAIN 1227..1275
FT /note="VWFC 1"
FT DOMAIN 1280..1462
FT /note="VWFD 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00580"
FT DOMAIN 1555..1608
FT /note="TIL 2"
FT DOMAIN 1609..1664
FT /note="VWFC 2"
FT DOMAIN 1669..1849
FT /note="VWFD 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00580"
FT DOMAIN 1941..1995
FT /note="TIL 3"
FT DOMAIN 1996..2052
FT /note="VWFC 3"
FT DOMAIN 2056..2239
FT /note="VWFD 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00580"
FT DOMAIN 2340..2398
FT /note="TIL 4"
FT DOMAIN 2399..2454
FT /note="VWFC 4"
FT DOMAIN 2460..2518
FT /note="TIL 5"
FT DOMAIN 2519..2574
FT /note="VWFC 5"
FT DOMAIN 2580..2638
FT /note="TIL 6"
FT DOMAIN 2639..2694
FT /note="VWFC 6"
FT DOMAIN 2700..2758
FT /note="TIL 7"
FT DOMAIN 2759..2814
FT /note="VWFC 7"
FT DOMAIN 2820..2878
FT /note="TIL 8"
FT DOMAIN 2879..2934
FT /note="VWFC 8"
FT DOMAIN 2940..2998
FT /note="TIL 9"
FT DOMAIN 2999..3054
FT /note="VWFC 9"
FT DOMAIN 3060..3118
FT /note="TIL 10"
FT DOMAIN 3119..3174
FT /note="VWFC 10"
FT DOMAIN 3180..3238
FT /note="TIL 11"
FT DOMAIN 3239..3294
FT /note="VWFC 11"
FT DOMAIN 3300..3355
FT /note="TIL 12"
FT DOMAIN 3356..3411
FT /note="VWFC 12"
FT DOMAIN 3417..3475
FT /note="TIL 13"
FT DOMAIN 3476..3531
FT /note="VWFC 13"
FT DOMAIN 3537..3595
FT /note="TIL 14"
FT DOMAIN 3596..3651
FT /note="VWFC 14"
FT DOMAIN 3657..3715
FT /note="TIL 15"
FT DOMAIN 3716..3771
FT /note="VWFC 15"
FT DOMAIN 3777..3835
FT /note="TIL 16"
FT DOMAIN 3836..3891
FT /note="VWFC 16"
FT DOMAIN 3893..3951
FT /note="TIL 17"
FT DOMAIN 3952..4007
FT /note="VWFC 17"
FT DOMAIN 4029..4087
FT /note="TIL 18"
FT DOMAIN 4088..4143
FT /note="VWFC 18"
FT DOMAIN 4149..4207
FT /note="TIL 19"
FT DOMAIN 4208..4262
FT /note="VWFC 19"
FT DOMAIN 4264..4322
FT /note="TIL 20"
FT DOMAIN 4323..4378
FT /note="VWFC 20"
FT DOMAIN 4384..4442
FT /note="TIL 21"
FT DOMAIN 4443..4498
FT /note="VWFC 21"
FT DOMAIN 4504..4562
FT /note="TIL 22"
FT DOMAIN 4563..4618
FT /note="VWFC 22"
FT DOMAIN 4624..4682
FT /note="TIL 23"
FT DOMAIN 4683..4738
FT /note="VWFC 23"
FT DOMAIN 4744..4802
FT /note="TIL 24"
FT DOMAIN 4803..4858
FT /note="VWFC 24"
FT DOMAIN 4863..5038
FT /note="VWFD 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00580"
FT DOMAIN 5150..5203
FT /note="TIL 25"
FT DOMAIN 5204..5258
FT /note="VWFC 25"
FT DOMAIN 5259..5295
FT /note="EGF-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT REGION 547..1170
FT /note="80 X heptapeptide repeats (approximate) (mucin-like
FT domain)"
FT REGION 553..579
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1037..1113
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 563..579
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1048..1084
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1099..1113
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 339
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 499
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1216
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1239
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1314
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1814
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1908
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1933
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2028
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2111
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2142
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2332
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2533
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2575
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2692
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2812
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 3052
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 3065
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 3144
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 3172
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 3288
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 3292
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 3782
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 4005
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 4136
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 4243
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 4254
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 4335
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 4376
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 4586
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 5136
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 5252
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 1282..1417
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00580"
FT DISULFID 1304..1461
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00580"
FT DISULFID 1671..1809
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00580"
FT DISULFID 1693..1848
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00580"
FT DISULFID 2058..2200
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00580"
FT DISULFID 2080..2238
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00580"
FT DISULFID 4865..5001
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00580"
FT DISULFID 5263..5274
FT /evidence="ECO:0000250"
FT DISULFID 5268..5283
FT /evidence="ECO:0000250"
FT DISULFID 5285..5294
FT /evidence="ECO:0000250"
SQ SEQUENCE 5376 AA; 579913 MW; 0E44DB77DF2A2620 CRC64;
MALPVWTLML LVGAAWGQEQ VPAWRPNSPD LGPMVHTSRE DSILSKCDFE DNSRPFCDWS
QMSADDGDWI RTTGPSLTGT SGPPGGYPNG EGYYLHMDPK TFPQGGVARL RSPDIWEQGP
LCVHFAFHMF GLSWGAQLRL LLLRGRKHLR PYVLWKHVNT QSPSWMPTTV TVPADHDIPS
WLMFEGMRGN TAYLDISLDG LSIQRGTCNQ VCMSQMCTFD TLNDLCGWSW VPTATGAKWT
QKKGPTGKQG VGPAEDFSNP GNGYYMLLDS TNARPGQKAV LLSPLSHSRG CMTLSFHYIM
HGQGHEEGLF VYATFLGNIR KYTLFSGHPG PDWQAVSVNY TGQGQIQFMV VGMFGNIPEP
AIAVDAISIA PCGESFPQCD FEDRVHPFCD WNQVYGDMGH WSWGSKSVPT LIAGSPREFP
YGGEHYIFFD SVKLSQEGQS ARLVSPPFCA PGGICVEFAY HMYGLGKGTT LKLLLGSPAG
SSPIPLWNRV GSQSSGWMNS SVTIPKGYQQ PMQLFIEATR GTSTAFVVAL NFILISHGPC
RVLLQTEIPS SPLLPPTGPS ESTVPTLPME QPTSPTKATT VTIEIPTTPT EEATIPTETT
TVPTEVINVS PKETSIPPEV TIPTEVITVS PEEIISPTEV TPVPTDVTAA YVEATNASPE
ETSVPPEVTI LTEVTTVSPE ETTVPTEVPI VLIEATAFPT GETTLYTEVP TVPTEVTGVH
TEVTNVSPEE TSVPTEETIS TEVTTVSPEE TTVPTEVPIV LIEATASPTG EITLYTEVPT
VPTEVTGVHT EVTNVSPEET SVPTEETIST EVTTVSPEET TLPTEVPTVS TEVTNVSPEE
TSVPPEETIL TTLYTEVPTV PTEVTGVHTE VTNVSPEETS VPTEETISTE VTTVSPEETT
LPTEVPTVST EVTNVSPEET SVPPEETILT EITTVSPEET VFPIEGTTLP TEVLTVPIEV
TTFPTGETTV PTEVPTVSTE MTGVHTEVTT VFPEETSIPT EVATVLPASI PPEETTTPTE
VTTTPPEETT IPAEVTTVPP ASIPPEETAS LTEVTTTPPE ETTTPTEVTT VPPEKTTIPT
EVTTVPPASI FPEETTVPPE ETTIASEETT VSTQETTLLT EQSAVTQTSI ACRPPCPSPP
LMPIGPLLSK PPGVSMFSLA PTTGVSTTES CPPNAHIELC ACPASCESPK PSCQPPCIPG
CVCNPGFLFS NNQCINESSC NCPYNNKHYK PGEEWFTPNC TERCRCLPGS LMECQISQCG
THTVCQLKSD QYQCEPYGKA TCLVYGDLHF VTFDERHIGF TGTCTYILTQ TCSNSTDHFF
RITANTEERG VEGVSCLDKV VISLPETTVT MISGRHTLIG DQEVTLPAIL SDDTYVGLSG
RFVELRTTFG LRVRWDGDQQ LFVTVSSTFS GKLCGFCGNY DGDSSNDNLK SDGMMTHDEE
ELRLSWQVEE DEDKDWVSSR CQKKKNPPSC DAALGSTMSG PKLCGQLVNP SGPFEACLLH
LKASSFLDNC VTDMCSFQGL QQKLCARMSA MTATCQDAGY PVKPWREPQF CPLVCPKNSR
YSLCAKPCPE TCHPISTTQH CSDKCVEGCE CDPGFILSGS ECVPSSQCGC TSFQGRYFKL
QEQWFNPDCK EICTCESHNH ILCKPWKCKA QEACSYKNGV LGCHAQGAAT CMVSGDPHYL
TFDGALHHFM GTCTYVLTQP CWSKSQENNF VVSATNEIHD GNLEVSYVKA VHVQVFDLKI
SMFKGQKVVL NNQRVVLPVW PSQGRVTIRL SGIFVLLYTN FGLQVRYDGR HLVEVTVPSS
YTGSLCGLCG NYNNNSMDDN LRADMKPAGN SLLLGAAWKI LEASDPGCFL AGGKPSRCAD
SDMDDVWTKK CAILMNPLGP FSNCHEAVPP QASFSSCVYG QCETNGDNLT FCHSLQAYAS
LCAQAGQVTT WRNSTFCPMR CPPRSSYNPC ANSCPATCLT LSTPRDCPTL PCVEGCECQS
GHILSGTTCV PLRQCGCSDQ DGSYHLLGES WYTEKTCTTL CTCSAHSNIT CSPTACKANH
VCLRQEGLLR CAAEMGECRI SEDSQIVSFD DHSHPIQDTC TYILVKVCHP NTNMPFFMIS
AKTDINTNGK NKTFGVYQLY IDIFNFHITL QKDHLVLISL INDSIVTLPT TTHIPGVSVM
TEDVYTIVTI KDEIQVKFES NNFLDVKIPA SSNGKVCGVC GNFNGEEEDE LMTPSGELAE
DEQEFMNSWK DKSMDPNCQK IEGQNLQVEQ QEIMNGKCRP IDFEKAQANC QTALQGPAWA
HCSSRVPIKP FLLKCMNSFC EFRELFRALC DSLQSFEDAC QNQGLKPPIW RNSSFCPLEC
PAHSHYTNCL PSCPPSCLDP DSRCEGSGHK VPATCREGCI CQPDYVLLND KCVLRSHCGC
KDAQGVFIPA GKTWISEDCT QSCTCMKGSM RCWDFQCPPG TYCKNSNDGS SNCVKISLQC
PAHSKFTDCL PPCHPSCSDP DGHCEGISTN AHSNCKEGCV CQPGYVLRND KCVLRIECGC
QHTQGGFIPA GKNWTSRGCS QSCDCMEGVI RCQNFQCPSG TYCQDIEDGT SNCANITLQC
PAHSSFTNCL PPCQPSCSDP EGHCGGSTTK APSACQEGCV CEPDYVVLNN KCVPRIECGC
KDAQGVLIPA DKIWINKGCT QTCACVTGTI HCRDFQCPSG TYCKDIKDDA SNCTEIILQC
PDHSLYTHCL PSCLLSCSDP DGLCRGTSPE APSTCKEGCV CDPDYVLSND KCVLRIECGC
KDAQGVLIPA GKTWINRGCT QSCSCMGGAI QCQNFKCPSE AYCQDMEDGN SNCTSIPLQC
PAHSHYTNCL PTCQPSCSDP DGHCEGSSTK APSACKEGCV CEPDYVMLNN KCVPRIECGC
KDTQGVLIPA DKTWINRGCT QSCTCRGGAI QCQKYHCSSG TYCKDMEDDS SSCATITLQC
PAHSHFTNCL PPCQPSCLDS EGHCEGSTTK APSACQEGCV CEPDYVVLNN KCVPRIECGC
KDAQGVLIPA DKTWINRGCT QSCTCKGGAI QCQKFQCPSE TYCKDIEDGN SNCTRISLQC
PANSNFTSCL PSCQPSCSNT DVHCEGSSPN TLSSCREGCV CQSGYVLHND KCILRNQCGC
KDAQGALIPE GKTWITSGCT QSCNCTGGAI QCQNFQCPLK TYCKDLKDGS SNCTNIPLQC
PAHSRYTNCL PSCPPLCLDP EGLCEGTSPK VPSTCREGCI CQPGYLMHKN KCVLRIFCGC
KNTQGAFISA DKTWISRGCT QSCTCPAGAI HCRNFKCPSG TYCKNGDNGS SNCTEITLQC
PTNSQFTDCL PSCVPSCSNR CEVTSPSVPS SCREGCLCNH GFVFSEDKCV PRTQCGCKDA
RGAIIPAGKT WTSKGCTQSC ACVEGNIQCQ NFQCPPETYC KDNSEGSSTC TKITLQCPAH
TQYTSCLPSC LPSCLDPEGL CKDISPKVPS TCKEGCVCQS GYVLNSDKCV LRAECDCKDA
QGALIPAGKT WTSPGCTQSC ACMGGAVQCQ SSQCPPGTYC KDNEDGNSNC AKITLQCPAH
SLFTNCLPPC LPSCLDPDGL CKGASPKVPS TCKEGCICQS GYVLSNNKCL LRNRCGCKDA
HGALIPEDKT WVSRGCTQSC VCTGGSIQCL SSQCPPGAYC KDNEDGSSNC ARIPPQCPAN
SHYTDCFPPC PPSCSDPEGH CEASGPRVLS TCREGCLCNP GFVLDRDKCV PRVECGCKDA
QGALIPSGKT WTSPGCTQSC ACMGGVVQCQ SSQCPPGTYC KDNEDGNSNC AKITLQCPTH
SNYTDCLPFC LPSCLDPSAL CGGTSPKGPS TCKEGCVCQP GYVLDKDKCI LKIECGCRDT
QGAVIPAGKT WLSTGCIQSC ACVEGTIQCQ NFQCPPGTYC NHNNNCAKIP LQCPAHSHFT
SCLPSCPPSC ANLDGSCEQT SPKVPSTCKE GCLCQPGYFL NNGKCVLQTH CDCKDAEGGL
VPAGKTWTSK DCTQSCACTG GAVQCQNFQC PLGTYCKDSG DGSSNCTKIH KGAMGDGVLM
AGGIRALQCP AHSHFTSCLP SCPPSCSNLD GSCVESNFKA PSVCKKGCIC QPGYLLNNDK
CVLRIQCGCK DTQGGLIPAG RTWISSDCTK SCSCMGGIIQ CRDFQCPPGT YCKESNDSSR
TCAKIPLQCP AHSHYTNCLP ACSRSCTDLD GHCEGTSPKV PSPCKEGCLC QPGYVVHNHK
CVLQIHCGCK DAQGGFVPAG KTWISRGCTQ SCACVGGAVQ CHNFTCPTGT QCQNSSCSKI
TVQCPAHSQY TTCLPSCLPS CFDPEGLCGG ASPRAPSTCR EGCVCEADYV LREDKCVLRT
QCGCKDAQGD LIPANKTWLT RGCAQKCTCK GGNIHCWNFK CPLGTECKDS VDGGSNCTKI
ALQCPAHSHH TYCLPSCIPS CSNVNDRCES TSLQRPSTCI EGCLCHSGFV FSKDKCVPRT
QCGCKDSQGT LIPAGKNWIT TGCSQRCTCT GGLVQCHDFQ CPSGAECQDI EDGNSNCVEI
TVQCPAHSHY SKCLPPCQPS CSDPDGHCEG TSPEAPSTCE EGCVCEPDYV LSNDKCVPSS
ECGCKDAHGV LIPESKTWVS RGCTKNCTCK GGTVQCHDFS CPTGSRCLDN NEGNSNCVTY
ALKCPAHSLY TNCLPSCLPS CSDPEGLCGG TSPEVPSTCK EGCICQSGYV LHKNKCMLRI
HCDCKDFQGS LIKTGQTWIS SGCSKICTCK GGFFQCQSYK CPSGTQCEES EDGSSNCVSS
TMKCPANSLY THCLPTCLPS CSNPDGRCEG TSHKAPSTCR EGCVCQPGYL LNKDTCVHKN
QCGCKDIRGN IIPAGNTWIS SDCTQSCACT DGVIQCQNFV CPSGSHCQYN EDGSSDCAAN
KLERCTIFGD PYYLTFDGFT YHFLGRMNYY LIKTVDKLPR GIEPLIMEGR NKISPKGSST
LHEVTTIVYG YKIQLQEELV VLVNDEKVAV PYNPNEHLRV MLRAQRLLLV TDFEMVLDFD
GKHSAVISLP TTYRGLTRGL CGNYDRDQSN ELMLPSGVLT SNVHVFGNSW EVKAQHAFFR
FPRALPEDEE RDEEPDLLQS ECSQEQTALI SSTQACRVLV DPQGPFAACH QIIAPEPFEQ
RCMLDMCTGW KTKEEEELRC RVLSGYAIIC QEAGANMTGW RDHTHCAMTC PANTVYQRCM
TPCPASCAKF VTPKVCEGPC VEGCASLPGY IYSDTQSLPV THCGCTADGI YYKLGDSFVT
NDCSQHCTCA SQGILLCEPY GCRAGESCMV ANFTRGCFQD SPCLQNPCHN DGRCEEQGAT
FICHCDFGYG GEFCTEPQDI TTRKKIEASS LVAILPGVLV MVLVPVLLPR VYVYMATRTT
MGRRRMKRKE KKLLRQSRLR LEDADVPEPT FKATEF
