ZP3_CHICK
ID ZP3_CHICK Reviewed; 437 AA.
AC P79762; Q4VU46; Q4VU49; Q4VU50; Q4VU53; Q4VU54; Q4VU57; Q4VU62; Q4VU63;
AC Q4VU66; Q9PWF8;
DT 08-MAR-2011, integrated into UniProtKB/Swiss-Prot.
DT 08-MAR-2011, sequence version 4.
DT 03-AUG-2022, entry version 123.
DE RecName: Full=Zona pellucida sperm-binding protein 3;
DE AltName: Full=Sperm receptor;
DE AltName: Full=Zona pellucida C protein;
DE AltName: Full=Zona pellucida glycoprotein 3;
DE Short=Zp-3;
DE Contains:
DE RecName: Full=Processed zona pellucida sperm-binding protein 3;
DE Flags: Precursor;
GN Name=ZP3; Synonyms=ZPC;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 21-35; 47-66 AND 265-280,
RP SUBCELLULAR LOCATION, GLYCOSYLATION, AND TISSUE SPECIFICITY.
RC STRAIN=White leghorn; TISSUE=Ovarian follicle;
RX PubMed=10103002; DOI=10.1046/j.1432-1327.1999.00203.x;
RA Takeuchi Y., Nishimura K., Aoki N., Adachi T., Sato C., Kitajima K.,
RA Matsuda T.;
RT "A 42-kDa glycoprotein from chicken egg-envelope, an avian homolog of the
RT ZPC family glycoproteins in mammalian Zona pellucida. Its first
RT identification, cDNA cloning and granulosa cell-specific expression.";
RL Eur. J. Biochem. 260:736-742(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=16283938; DOI=10.1186/1471-2148-5-65;
RA Berlin S., Smith N.G.;
RT "Testing for adaptive evolution of the female reproductive protein ZPC in
RT mammals, birds and fishes reveals problems with the M7-M8 likelihood ratio
RT test.";
RL BMC Evol. Biol. 5:65-65(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC TISSUE=Liver;
RA Kono Y., Matsuda T.;
RT "Gallus gallus zona pellucida C protein gene.";
RL Submitted (AUG-1999) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=15115720; DOI=10.1095/biolreprod.104.028605;
RA Bausek N., Ruckenbauer H.H., Pfeifer S., Schneider W.J., Wohlrab F.;
RT "Interaction of sperm with purified native chicken ZP1 and ZPC proteins.";
RL Biol. Reprod. 71:684-690(2004).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 53-383 OF MUTANT GLN-159,
RP FUNCTION, GLYCOSYLATION AT ASN-159 AND THR-168, SUBUNIT, SUBCELLULAR
RP LOCATION, IDENTIFICATION BY MASS SPECTROMETRY, MUTAGENESIS OF CYS-58;
RP CYS-90; ARG-142; CYS-152; ASN-159; THR-168; GLU-196; CYS-229; PRO-235;
RP PRO-241; CYS-251; TYR-292; CYS-313; CYS-332; CYS-334; CYS-335; CYS-340 AND
RP 359-ARG--ARG-362, AND DISULFIDE BONDS.
RX PubMed=20970175; DOI=10.1016/j.cell.2010.09.041;
RA Han L., Monne M., Okumura H., Schwend T., Cherry A.L., Flot D., Matsuda T.,
RA Jovine L.;
RT "Insights into egg coat assembly and egg-sperm interaction from the X-ray
RT structure of full-length ZP3.";
RL Cell 143:404-415(2010).
CC -!- FUNCTION: Component of the zona pellucida, which mediates species-
CC specific sperm binding. Directly binds to sperm. Important for egg
CC fertilization. {ECO:0000269|PubMed:15115720,
CC ECO:0000269|PubMed:20970175}.
CC -!- SUBUNIT: Homodimer. Forms higher oligomers, once its C-terminus has
CC been proteolytically removed. Forms heterooligomers with other zona
CC pellucida glycoproteins (By similarity). {ECO:0000250}.
CC -!- INTERACTION:
CC P79762; P79762: ZP3; NbExp=3; IntAct=EBI-2942236, EBI-2942236;
CC -!- SUBCELLULAR LOCATION: [Processed zona pellucida sperm-binding protein
CC 3]: Secreted, extracellular space, extracellular matrix
CC {ECO:0000269|PubMed:10103002}. Note=The glycoproteinaceous translucent
CC extracellular matrix that surrounds the mammalian oocyte is called zona
CC pellucida. {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:10103002,
CC ECO:0000269|PubMed:20970175}; Single-pass type I membrane protein
CC {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: Detected in the ovarian perivitteline layer.
CC Detected in granulosa cells in ovarian follicle (at protein level).
CC Detected in granulosa cells in ovarian follicle.
CC {ECO:0000269|PubMed:10103002, ECO:0000269|PubMed:15115720}.
CC -!- DOMAIN: The ZP domain is involved in the polymerization of the ZP
CC proteins to form the zona pellucida. {ECO:0000250}.
CC -!- PTM: Proteolytically cleaved before the transmembrane segment to yield
CC the secreted ectodomain incorporated in the zona pellucida.
CC -!- PTM: N-glycosylated.
CC -!- PTM: O-glycosylated. O-glycosylation at Thr-168 is important for
CC efficient interaction with the sperm head.
CC {ECO:0000269|PubMed:20970175}.
CC -!- SIMILARITY: Belongs to the ZP domain family. ZPC subfamily.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAV35179.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAV35180.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAV35181.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAV35182.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAV35183.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAV35184.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAV35185.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAV35186.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAV35187.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAV35188.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAV35189.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAV35190.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAV35191.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAV35192.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAV35193.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAV35194.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAV35195.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAV35196.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAV35197.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAV35198.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAV35199.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAV35200.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAV35201.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAA83418.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; D89097; BAA13760.3; -; mRNA.
DR EMBL; AY628608; AAV35179.1; ALT_INIT; Genomic_DNA.
DR EMBL; AY628609; AAV35180.1; ALT_INIT; Genomic_DNA.
DR EMBL; AY628610; AAV35181.1; ALT_INIT; Genomic_DNA.
DR EMBL; AY628611; AAV35182.1; ALT_INIT; Genomic_DNA.
DR EMBL; AY628612; AAV35183.1; ALT_INIT; Genomic_DNA.
DR EMBL; AY628613; AAV35184.1; ALT_INIT; Genomic_DNA.
DR EMBL; AY628614; AAV35185.1; ALT_INIT; Genomic_DNA.
DR EMBL; AY628615; AAV35186.1; ALT_INIT; Genomic_DNA.
DR EMBL; AY628616; AAV35187.1; ALT_INIT; Genomic_DNA.
DR EMBL; AY628617; AAV35188.1; ALT_INIT; Genomic_DNA.
DR EMBL; AY628618; AAV35189.1; ALT_INIT; Genomic_DNA.
DR EMBL; AY628619; AAV35190.1; ALT_INIT; Genomic_DNA.
DR EMBL; AY628620; AAV35191.1; ALT_INIT; Genomic_DNA.
DR EMBL; AY628621; AAV35192.1; ALT_INIT; Genomic_DNA.
DR EMBL; AY628622; AAV35193.1; ALT_INIT; Genomic_DNA.
DR EMBL; AY628623; AAV35194.1; ALT_INIT; Genomic_DNA.
DR EMBL; AY628624; AAV35195.1; ALT_INIT; Genomic_DNA.
DR EMBL; AY628625; AAV35196.1; ALT_INIT; Genomic_DNA.
DR EMBL; AY628626; AAV35197.1; ALT_INIT; Genomic_DNA.
DR EMBL; AY628627; AAV35198.1; ALT_INIT; Genomic_DNA.
DR EMBL; AY628628; AAV35199.1; ALT_INIT; Genomic_DNA.
DR EMBL; AY628629; AAV35200.1; ALT_INIT; Genomic_DNA.
DR EMBL; AY628630; AAV35201.1; ALT_INIT; Genomic_DNA.
DR EMBL; AB031033; BAA83418.1; ALT_INIT; Genomic_DNA.
DR RefSeq; NP_989720.3; NM_204389.2.
DR PDB; 3NK3; X-ray; 2.60 A; A/B=53-347, C/D=359-382.
DR PDB; 3NK4; X-ray; 2.00 A; A/B=53-347, C/D=359-382.
DR PDBsum; 3NK3; -.
DR PDBsum; 3NK4; -.
DR AlphaFoldDB; P79762; -.
DR SMR; P79762; -.
DR STRING; 9031.ENSGALP00000002368; -.
DR iPTMnet; P79762; -.
DR PaxDb; P79762; -.
DR Ensembl; ENSGALT00000002370; ENSGALP00000002368; ENSGALG00000001559.
DR GeneID; 378906; -.
DR KEGG; gga:378906; -.
DR CTD; 7784; -.
DR VEuPathDB; HostDB:geneid_378906; -.
DR eggNOG; ENOG502QSZF; Eukaryota.
DR GeneTree; ENSGT01030000234567; -.
DR HOGENOM; CLU_047091_1_1_1; -.
DR InParanoid; P79762; -.
DR OMA; HNTVTFA; -.
DR OrthoDB; 495227at2759; -.
DR PhylomeDB; P79762; -.
DR TreeFam; TF331369; -.
DR PRO; PR:P79762; -.
DR Proteomes; UP000000539; Chromosome 10.
DR Bgee; ENSGALG00000001559; Expressed in testis and 4 other tissues.
DR ExpressionAtlas; P79762; baseline and differential.
DR GO; GO:0045177; C:apical part of cell; IDA:AgBase.
DR GO; GO:0031012; C:extracellular matrix; IBA:GO_Central.
DR GO; GO:0005615; C:extracellular space; IDA:AgBase.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0032190; F:acrosin binding; IBA:GO_Central.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0035804; F:structural constituent of egg coat; ISS:UniProtKB.
DR GO; GO:0007339; P:binding of sperm to zona pellucida; IBA:GO_Central.
DR GO; GO:0035803; P:egg coat formation; IBA:GO_Central.
DR GO; GO:2000344; P:positive regulation of acrosome reaction; IBA:GO_Central.
DR GO; GO:0032570; P:response to progesterone; ISS:AgBase.
DR GO; GO:0033574; P:response to testosterone; ISS:AgBase.
DR Gene3D; 2.60.40.4100; -; 1.
DR InterPro; IPR042235; ZP-C.
DR InterPro; IPR040196; ZP3.
DR InterPro; IPR001507; ZP_dom.
DR InterPro; IPR017977; ZP_dom_CS.
DR PANTHER; PTHR11576:SF2; PTHR11576:SF2; 1.
DR Pfam; PF00100; Zona_pellucida; 1.
DR PRINTS; PR00023; ZPELLUCIDA.
DR SMART; SM00241; ZP; 1.
DR PROSITE; PS00682; ZP_1; 1.
DR PROSITE; PS51034; ZP_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell membrane; Cleavage on pair of basic residues;
KW Direct protein sequencing; Disulfide bond; Extracellular matrix;
KW Fertilization; Glycoprotein; Membrane; Reference proteome; Secreted;
KW Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..20
FT /evidence="ECO:0000269|PubMed:10103002"
FT CHAIN 21..360
FT /note="Zona pellucida sperm-binding protein 3"
FT /id="PRO_0000405431"
FT CHAIN 21..?
FT /note="Processed zona pellucida sperm-binding protein 3"
FT /id="PRO_0000405432"
FT PROPEP 361..437
FT /note="Removed in mature form"
FT /evidence="ECO:0000250"
FT /id="PRO_0000405433"
FT TOPO_DOM 21..405
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 406..426
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 427..437
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 57..320
FT /note="ZP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00375"
FT REGION 368..380
FT /note="Extracellular hydrophobic patch"
FT CARBOHYD 159
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:20970175"
FT CARBOHYD 168
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000269|PubMed:20970175"
FT DISULFID 58..152
FT /evidence="ECO:0000269|PubMed:20970175"
FT DISULFID 90..111
FT /evidence="ECO:0000269|PubMed:20970175"
FT DISULFID 229..295
FT /evidence="ECO:0000269|PubMed:20970175"
FT DISULFID 251..335
FT /evidence="ECO:0000269|PubMed:20970175"
FT DISULFID 313..332
FT /evidence="ECO:0000269|PubMed:20970175"
FT DISULFID 334..340
FT /evidence="ECO:0000269|PubMed:20970175"
FT MUTAGEN 58
FT /note="C->A: Abolishes secretion of processed zona
FT pellucida sperm-binding protein 3; when associated with A-
FT 152."
FT /evidence="ECO:0000269|PubMed:20970175"
FT MUTAGEN 90
FT /note="C->A: Abolishes secretion of processed zona
FT pellucida sperm-binding protein 3; when associated with A-
FT 111."
FT /evidence="ECO:0000269|PubMed:20970175"
FT MUTAGEN 111
FT /note="C->A: Abolishes secretion of processed zona
FT pellucida sperm-binding protein 3; when associated with A-
FT 90."
FT MUTAGEN 142
FT /note="R->A: Impaired homodimerization and abolished
FT secretion of processed zona pellucida sperm-binding protein
FT 3."
FT /evidence="ECO:0000269|PubMed:20970175"
FT MUTAGEN 152
FT /note="C->A: Abolishes secretion of processed zona
FT pellucida sperm-binding protein 3; when associated with A-
FT 58."
FT /evidence="ECO:0000269|PubMed:20970175"
FT MUTAGEN 159
FT /note="N->Q: Loss of N-glycosylation."
FT /evidence="ECO:0000269|PubMed:20970175"
FT MUTAGEN 168
FT /note="T->A: Loss of O-glycosylation. No effect on
FT secretion. Reduces binding to the sperm head by about 80%."
FT /evidence="ECO:0000269|PubMed:20970175"
FT MUTAGEN 196
FT /note="E->A: No effect on secretion."
FT /evidence="ECO:0000269|PubMed:20970175"
FT MUTAGEN 229
FT /note="C->A: Impaired secretion of processed zona pellucida
FT sperm-binding protein 3; when associated with A-295."
FT /evidence="ECO:0000269|PubMed:20970175"
FT MUTAGEN 235
FT /note="P->D: Abolishes secretion of processed zona
FT pellucida sperm-binding protein 3."
FT /evidence="ECO:0000269|PubMed:20970175"
FT MUTAGEN 241
FT /note="P->A: No effect on dimerization or secretion."
FT /evidence="ECO:0000269|PubMed:20970175"
FT MUTAGEN 251
FT /note="C->A: Abolishes secretion of processed zona
FT pellucida sperm-binding protein 3; when associated with A-
FT 335."
FT /evidence="ECO:0000269|PubMed:20970175"
FT MUTAGEN 292
FT /note="Y->A: Abolishes secretion of processed zona
FT pellucida sperm-binding protein 3."
FT /evidence="ECO:0000269|PubMed:20970175"
FT MUTAGEN 295
FT /note="C->A: Impaired secretion of processed zona pellucida
FT sperm-binding protein 3; when associated with A-229."
FT MUTAGEN 313
FT /note="C->A: Abolishes secretion of processed zona
FT pellucida sperm-binding protein 3; when associated with A-
FT 332."
FT /evidence="ECO:0000269|PubMed:20970175"
FT MUTAGEN 332
FT /note="C->A: Abolishes secretion of processed zona
FT pellucida sperm-binding protein 3; when associated with A-
FT 313."
FT /evidence="ECO:0000269|PubMed:20970175"
FT MUTAGEN 334
FT /note="C->A: Abolishes secretion of processed zona
FT pellucida sperm-binding protein 3; when associated with A-
FT 340."
FT /evidence="ECO:0000269|PubMed:20970175"
FT MUTAGEN 335
FT /note="C->A: Abolishes secretion of processed zona
FT pellucida sperm-binding protein 3; when associated with A-
FT 251."
FT /evidence="ECO:0000269|PubMed:20970175"
FT MUTAGEN 340
FT /note="C->A: Abolishes secretion of processed zona
FT pellucida sperm-binding protein 3; when associated with A-
FT 334."
FT /evidence="ECO:0000269|PubMed:20970175"
FT MUTAGEN 359..362
FT /note="RFRR->AFAA: Abolishes cleavage of C-terminal
FT propeptide."
FT /evidence="ECO:0000269|PubMed:20970175"
FT CONFLICT 43
FT /note="A -> V (in Ref. 2; AAV35184)"
FT /evidence="ECO:0000305"
FT CONFLICT 48
FT /note="V -> M (in Ref. 2; AAV35193/AAV35180/AAV35179)"
FT /evidence="ECO:0000305"
FT CONFLICT 424
FT /note="G -> C (in Ref. 1; BAA13760 and 3; BAA83418)"
FT /evidence="ECO:0000305"
FT CONFLICT 435
FT /note="A -> T (in Ref. 1; BAA13760)"
FT /evidence="ECO:0000305"
FT STRAND 53..58
FT /evidence="ECO:0007829|PDB:3NK4"
FT STRAND 60..69
FT /evidence="ECO:0007829|PDB:3NK4"
FT HELIX 80..82
FT /evidence="ECO:0007829|PDB:3NK4"
FT STRAND 83..85
FT /evidence="ECO:0007829|PDB:3NK4"
FT TURN 86..89
FT /evidence="ECO:0007829|PDB:3NK4"
FT STRAND 93..96
FT /evidence="ECO:0007829|PDB:3NK4"
FT TURN 97..100
FT /evidence="ECO:0007829|PDB:3NK4"
FT STRAND 101..107
FT /evidence="ECO:0007829|PDB:3NK4"
FT STRAND 114..117
FT /evidence="ECO:0007829|PDB:3NK4"
FT STRAND 119..130
FT /evidence="ECO:0007829|PDB:3NK4"
FT STRAND 140..143
FT /evidence="ECO:0007829|PDB:3NK4"
FT STRAND 146..155
FT /evidence="ECO:0007829|PDB:3NK4"
FT TURN 171..173
FT /evidence="ECO:0007829|PDB:3NK3"
FT STRAND 184..189
FT /evidence="ECO:0007829|PDB:3NK4"
FT STRAND 193..196
FT /evidence="ECO:0007829|PDB:3NK4"
FT STRAND 199..202
FT /evidence="ECO:0007829|PDB:3NK3"
FT STRAND 207..214
FT /evidence="ECO:0007829|PDB:3NK4"
FT STRAND 217..219
FT /evidence="ECO:0007829|PDB:3NK3"
FT STRAND 222..235
FT /evidence="ECO:0007829|PDB:3NK4"
FT STRAND 239..247
FT /evidence="ECO:0007829|PDB:3NK4"
FT TURN 248..250
FT /evidence="ECO:0007829|PDB:3NK4"
FT HELIX 253..256
FT /evidence="ECO:0007829|PDB:3NK4"
FT STRAND 273..279
FT /evidence="ECO:0007829|PDB:3NK4"
FT STRAND 290..301
FT /evidence="ECO:0007829|PDB:3NK4"
FT STRAND 313..316
FT /evidence="ECO:0007829|PDB:3NK4"
FT TURN 317..320
FT /evidence="ECO:0007829|PDB:3NK4"
FT STRAND 321..327
FT /evidence="ECO:0007829|PDB:3NK4"
FT HELIX 329..332
FT /evidence="ECO:0007829|PDB:3NK4"
FT HELIX 333..337
FT /evidence="ECO:0007829|PDB:3NK4"
FT STRAND 368..379
FT /evidence="ECO:0007829|PDB:3NK4"
SQ SEQUENCE 437 AA; 46766 MW; A9B59E9DE71819B3 CRC64;
MQGGRVVLGL LCCLVAGVGS YTPWDISWAA RGDPSAWSWG AEAHSRAVAG SHPVAVQCQE
AQLVVTVHRD LFGTGRLINA ADLTLGPAAC KHSSLNAAHN TVTFAAGLHE CGSVVQVTPD
TLIYRTLINY DPSPASNPVI IRTNPAVIPI ECHYPRRENV SSNAIRPTWS PFNSALSAEE
RLVFSLRLMS DDWSTERPFT GFQLGDILNI QAEVSTENHV PLRLFVDSCV AALSPDGDSS
PHYAIIDFNG CLVDGRVDDT SSAFITPRPR EDVLRFRIDV FRFAGDNRNL IYITCHLKVT
PADQGPDPQN KACSFNKARN TWVPVEGSRD VCNCCETGNC EPPALSRRLN PMERWQSRRF
RRDAGKEVAA DVVIGPVLLS ADPGAVGQQE EGGDGAAVMV PSVGTGLVCV AVAVALAAVG
VAVGIARKGC TRTSAAV
