ZP3_HUMAN
ID ZP3_HUMAN Reviewed; 424 AA.
AC P21754; Q06633; Q29RW0;
DT 01-MAY-1991, integrated into UniProtKB/Swiss-Prot.
DT 07-JUL-2009, sequence version 2.
DT 03-AUG-2022, entry version 195.
DE RecName: Full=Zona pellucida sperm-binding protein 3;
DE AltName: Full=Sperm receptor;
DE AltName: Full=ZP3A/ZP3B;
DE AltName: Full=Zona pellucida glycoprotein 3;
DE Short=Zp-3;
DE AltName: Full=Zona pellucida protein C;
DE Contains:
DE RecName: Full=Processed zona pellucida sperm-binding protein 3;
DE Flags: Precursor;
GN Name=ZP3; Synonyms=ZP3A, ZP3B, ZPC;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM ZP3A), AND VARIANT PRO-315.
RX PubMed=2385582; DOI=10.1073/pnas.87.16.6014;
RA Chamberlin M.E., Dean J.;
RT "Human homolog of the mouse sperm receptor.";
RL Proc. Natl. Acad. Sci. U.S.A. 87:6014-6018(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS ZP3A AND ZP3B), AND VARIANT PRO-315.
RC TISSUE=Ovary;
RX PubMed=1478648; DOI=10.1016/s0888-7543(05)80130-2;
RA van Duin M., Polman J.E., Verkoelen C.C., Bunschoten H., Meyerink J.H.,
RA Olijve W., Aitken R.J.;
RT "Cloning and characterization of the human sperm receptor ligand ZP3:
RT evidence for a second polymorphic allele with a different frequency in the
RT Caucasian and Japanese populations.";
RL Genomics 14:1064-1070(1992).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3), AND VARIANT PRO-315.
RC TISSUE=Lung;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12853948; DOI=10.1038/nature01782;
RA Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H.,
RA Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K.,
RA Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A.,
RA Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H., Sun H.,
RA Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A.,
RA Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P.,
RA Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M.,
RA Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S.,
RA Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R.,
RA Strowmatt C., Latreille P., Miller N., Johnson D., Murray J.,
RA Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W.,
RA Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A.,
RA Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E.,
RA Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E.,
RA Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A.,
RA Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A.,
RA Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R.,
RA McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H.,
RA Wilson R.K.;
RT "The DNA sequence of human chromosome 7.";
RL Nature 424:157-164(2003).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3), AND VARIANT PRO-315.
RC TISSUE=Brain;
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 SIGNAL SEQUENCE CLEAVAGE SITE, PYROGLUTAMATE FORMATION AT GLN-23,
RP PROTEOLYTIC PROCESSING, DISULFIDE BONDS, AND GLYCOSYLATION AT ASN-125;
RP ASN-147 AND ASN-272.
RX PubMed=15379548; DOI=10.1021/bi048958k;
RA Zhao M., Boja E.S., Hoodbhoy T., Nawrocki J., Kaufman J.B., Kresge N.,
RA Ghirlando R., Shiloach J., Pannell L., Levine R.L., Fales H.M., Dean J.;
RT "Mass spectrometry analysis of recombinant human ZP3 expressed in
RT glycosylation-deficient CHO cells.";
RL Biochemistry 43:12090-12104(2004).
RN [7]
RP INVOLVEMENT IN OOMD3, VARIANT OOMD3 THR-134, CHARACTERIZATION OF VARIANT
RP OOMD3 THR-134, AND INTERACTION WITH ZP1 AND ZP2.
RX PubMed=28886344; DOI=10.1016/j.ajhg.2017.08.001;
RA Chen T., Bian Y., Liu X., Zhao S., Wu K., Yan L., Li M., Yang Z., Liu H.,
RA Zhao H., Chen Z.J.;
RT "A recurrent missense mutation in ZP3 causes empty follicle syndrome and
RT female infertility.";
RL Am. J. Hum. Genet. 101:459-465(2017).
RN [8]
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=29895852; DOI=10.1038/s41436-018-0064-y;
RA Dai C., Hu L., Gong F., Tan Y., Cai S., Zhang S., Dai J., Lu C., Chen J.,
RA Chen Y., Lu G., Du J., Lin G.;
RT "ZP2 pathogenic variants cause in vitro fertilization failure and female
RT infertility.";
RL Genet. Med. 21:431-440(2019).
CC -!- FUNCTION: Component of the zona pellucida, an extracellular matrix
CC surrounding oocytes which mediates sperm binding, induction of the
CC acrosome reaction and prevents post-fertilization polyspermy. The zona
CC pellucida is composed of 3 to 4 glycoproteins, ZP1, ZP2, ZP3, and ZP4.
CC ZP3 is essential for sperm binding and zona matrix formation.
CC -!- SUBUNIT: Polymers of ZP2 and ZP3 organized into long filaments cross-
CC linked by ZP1 homodimers (By similarity). Interacts with ZP1 and ZP2
CC (PubMed:28886344). {ECO:0000250|UniProtKB:P20239,
CC ECO:0000269|PubMed:28886344}.
CC -!- INTERACTION:
CC P21754; P10323: ACR; NbExp=2; IntAct=EBI-11783624, EBI-21280149;
CC P21754; P45880-3: VDAC2; NbExp=2; IntAct=EBI-11783624, EBI-11614013;
CC P21754; P21754: ZP3; NbExp=6; IntAct=EBI-11783624, EBI-11783624;
CC P21754-1; P21754-1: ZP3; NbExp=5; IntAct=EBI-21279609, EBI-21279609;
CC P21754-3; O75508: CLDN11; NbExp=3; IntAct=EBI-17458299, EBI-12820543;
CC P21754-3; Q13021: MALL; NbExp=3; IntAct=EBI-17458299, EBI-750078;
CC -!- SUBCELLULAR LOCATION: [Processed zona pellucida sperm-binding protein
CC 3]: Zona pellucida {ECO:0000269|PubMed:29895852}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P48833};
CC Single-pass type I membrane protein {ECO:0000255}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=ZP3A;
CC IsoId=P21754-1; Sequence=Displayed;
CC Name=ZP3B;
CC IsoId=P21754-2; Sequence=VSP_006949, VSP_006950;
CC Name=3;
CC IsoId=P21754-3; Sequence=VSP_037556;
CC -!- TISSUE SPECIFICITY: Expressed in oocytes (at protein level).
CC {ECO:0000269|PubMed:29895852}.
CC -!- DOMAIN: The ZP domain is involved in the polymerization of the ZP
CC proteins to form the zona pellucida.
CC -!- PTM: Proteolytically cleaved before the transmembrane segment to yield
CC the secreted ectodomain incorporated in the zona pellucida.
CC {ECO:0000269|PubMed:15379548}.
CC -!- PTM: N-glycosylated. {ECO:0000250}.
CC -!- PTM: O-glycosylated; removal of O-linked glycans may play an important
CC role in the post-fertilization block to polyspermy. {ECO:0000250}.
CC -!- DISEASE: Oocyte maturation defect 3 (OOMD3) [MIM:617712]: An autosomal
CC dominant infertility disorder characterized by abnormal oocytes that
CC lack the zona pellucida, and oocytes degeneration.
CC {ECO:0000269|PubMed:28886344}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- MISCELLANEOUS: [Isoform ZP3B]: Found in a second polymorphic locus
CC which, due to an extra G residue in exon 8, has the potential to encode
CC a truncated protein of 372 amino acids. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the ZP domain family. ZPC subfamily.
CC {ECO:0000305}.
CC -!- WEB RESOURCE: Name=Protein Spotlight; Note=Molecular chastity - Issue
CC 93 of April 2008;
CC URL="https://web.expasy.org/spotlight/back_issues/093";
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DR EMBL; M60504; AAA61336.1; -; mRNA.
DR EMBL; X56777; CAA40095.1; -; mRNA.
DR EMBL; AK292763; BAF85452.1; -; mRNA.
DR EMBL; AC005522; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC113949; AAI13950.2; -; mRNA.
DR CCDS; CCDS47618.1; -. [P21754-1]
DR CCDS; CCDS5586.1; -. [P21754-3]
DR PIR; A36000; A36000.
DR RefSeq; NP_001103824.1; NM_001110354.1. [P21754-1]
DR RefSeq; NP_009086.4; NM_007155.5. [P21754-3]
DR AlphaFoldDB; P21754; -.
DR SMR; P21754; -.
DR BioGRID; 113565; 22.
DR CORUM; P21754; -.
DR IntAct; P21754; 18.
DR MINT; P21754; -.
DR STRING; 9606.ENSP00000378326; -.
DR GlyConnect; 634; 22 O-Linked glycans.
DR GlyGen; P21754; 7 sites, 28 O-linked glycans (1 site).
DR iPTMnet; P21754; -.
DR PhosphoSitePlus; P21754; -.
DR BioMuta; ZP3; -.
DR DMDM; 251757420; -.
DR MassIVE; P21754; -.
DR PaxDb; P21754; -.
DR PeptideAtlas; P21754; -.
DR PRIDE; P21754; -.
DR ProteomicsDB; 53897; -. [P21754-1]
DR ProteomicsDB; 53898; -. [P21754-2]
DR ProteomicsDB; 53899; -. [P21754-3]
DR ABCD; P21754; 1 sequenced antibody.
DR Antibodypedia; 29315; 121 antibodies from 24 providers.
DR DNASU; 7784; -.
DR Ensembl; ENST00000336517.8; ENSP00000337310.4; ENSG00000188372.15. [P21754-3]
DR Ensembl; ENST00000394857.8; ENSP00000378326.3; ENSG00000188372.15. [P21754-1]
DR GeneID; 7784; -.
DR KEGG; hsa:7784; -.
DR MANE-Select; ENST00000394857.8; ENSP00000378326.3; NM_001110354.2; NP_001103824.1.
DR UCSC; uc003ufc.5; human. [P21754-1]
DR CTD; 7784; -.
DR DisGeNET; 7784; -.
DR GeneCards; ZP3; -.
DR HGNC; HGNC:13189; ZP3.
DR HPA; ENSG00000188372; Low tissue specificity.
DR MalaCards; ZP3; -.
DR MIM; 182889; gene.
DR MIM; 617712; phenotype.
DR neXtProt; NX_P21754; -.
DR OpenTargets; ENSG00000188372; -.
DR Orphanet; 404466; Female infertility due to zona pellucida defect.
DR PharmGKB; PA37757; -.
DR VEuPathDB; HostDB:ENSG00000188372; -.
DR eggNOG; ENOG502QSZF; Eukaryota.
DR GeneTree; ENSGT01030000234567; -.
DR HOGENOM; CLU_047091_1_1_1; -.
DR InParanoid; P21754; -.
DR OMA; ECHYPRH; -.
DR OrthoDB; 495227at2759; -.
DR PhylomeDB; P21754; -.
DR TreeFam; TF331369; -.
DR PathwayCommons; P21754; -.
DR Reactome; R-HSA-2534343; Interaction With Cumulus Cells And The Zona Pellucida.
DR SignaLink; P21754; -.
DR SIGNOR; P21754; -.
DR BioGRID-ORCS; 7784; 12 hits in 1074 CRISPR screens.
DR ChiTaRS; ZP3; human.
DR GeneWiki; ZP3; -.
DR GenomeRNAi; 7784; -.
DR Pharos; P21754; Tbio.
DR PRO; PR:P21754; -.
DR Proteomes; UP000005640; Chromosome 7.
DR RNAct; P21754; protein.
DR Bgee; ENSG00000188372; Expressed in lower esophagus mucosa and 98 other tissues.
DR ExpressionAtlas; P21754; baseline and differential.
DR Genevisible; P21754; HS.
DR GO; GO:0062023; C:collagen-containing extracellular matrix; IDA:UniProtKB.
DR GO; GO:0035805; C:egg coat; IDA:UniProtKB.
DR GO; GO:0031012; C:extracellular matrix; IBA:GO_Central.
DR GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR GO; GO:0005615; C:extracellular space; IMP:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0032190; F:acrosin binding; IPI:UniProtKB.
DR GO; GO:0030246; F:carbohydrate binding; IDA:UniProtKB.
DR GO; GO:0005201; F:extracellular matrix structural constituent; HDA:BHF-UCL.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0048018; F:receptor ligand activity; ISS:UniProtKB.
DR GO; GO:0035804; F:structural constituent of egg coat; ISS:UniProtKB.
DR GO; GO:0007339; P:binding of sperm to zona pellucida; IDA:UniProtKB.
DR GO; GO:0001825; P:blastocyst formation; ISS:UniProtKB.
DR GO; GO:0035803; P:egg coat formation; ISS:UniProtKB.
DR GO; GO:0002455; P:humoral immune response mediated by circulating immunoglobulin; ISS:UniProtKB.
DR GO; GO:2000360; P:negative regulation of binding of sperm to zona pellucida; IDA:UniProtKB.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; ISS:UniProtKB.
DR GO; GO:0048599; P:oocyte development; ISS:UniProtKB.
DR GO; GO:2000368; P:positive regulation of acrosomal vesicle exocytosis; IDA:UniProtKB.
DR GO; GO:2000344; P:positive regulation of acrosome reaction; IDA:UniProtKB.
DR GO; GO:2000388; P:positive regulation of antral ovarian follicle growth; ISS:UniProtKB.
DR GO; GO:0002922; P:positive regulation of humoral immune response; IDA:UniProtKB.
DR GO; GO:0050729; P:positive regulation of inflammatory response; ISS:UniProtKB.
DR GO; GO:0032729; P:positive regulation of interferon-gamma production; ISS:UniProtKB.
DR GO; GO:0032753; P:positive regulation of interleukin-4 production; ISS:UniProtKB.
DR GO; GO:0002687; P:positive regulation of leukocyte migration; ISS:UniProtKB.
DR GO; GO:2000386; P:positive regulation of ovarian follicle development; ISS:UniProtKB.
DR GO; GO:0042102; P:positive regulation of T cell proliferation; ISS:UniProtKB.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; ISS:UniProtKB.
DR GO; GO:0001809; P:positive regulation of type IV hypersensitivity; ISS:UniProtKB.
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 Alternative splicing; Cell membrane; Cleavage on pair of basic residues;
KW Disease variant; Disulfide bond; Extracellular matrix; Fertilization;
KW Glycoprotein; Membrane; Pyrrolidone carboxylic acid; Receptor;
KW Reference proteome; Secreted; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..22
FT /evidence="ECO:0000269|PubMed:15379548"
FT CHAIN 23..350
FT /note="Zona pellucida sperm-binding protein 3"
FT /id="PRO_0000041709"
FT CHAIN 23..?
FT /note="Processed zona pellucida sperm-binding protein 3"
FT /id="PRO_0000304569"
FT PROPEP 351..424
FT /note="Removed in mature form"
FT /evidence="ECO:0000250"
FT /id="PRO_0000041710"
FT TOPO_DOM 23..387
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 388..408
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 409..424
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 45..307
FT /note="ZP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00375"
FT REGION 330..356
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 330..348
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 23
FT /note="Pyrrolidone carboxylic acid"
FT /evidence="ECO:0000269|PubMed:15379548"
FT CARBOHYD 125
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:15379548"
FT CARBOHYD 147
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:15379548"
FT CARBOHYD 156
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000250"
FT CARBOHYD 162
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000250"
FT CARBOHYD 163
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000250"
FT CARBOHYD 272
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:15379548"
FT DISULFID 46..140
FT /evidence="ECO:0000269|PubMed:15379548"
FT DISULFID 78..99
FT /evidence="ECO:0000269|PubMed:15379548"
FT DISULFID 217..282
FT /evidence="ECO:0000269|PubMed:15379548"
FT DISULFID 239..300
FT /evidence="ECO:0000269|PubMed:15379548"
FT VAR_SEQ 1..51
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_037556"
FT VAR_SEQ 364..372
FT /note="PLIFLDRRG -> ATDLPGQEW (in isoform ZP3B)"
FT /evidence="ECO:0000303|PubMed:1478648"
FT /id="VSP_006949"
FT VAR_SEQ 373..424
FT /note="Missing (in isoform ZP3B)"
FT /evidence="ECO:0000303|PubMed:1478648"
FT /id="VSP_006950"
FT VARIANT 31
FT /note="G -> R (in dbSNP:rs2286428)"
FT /id="VAR_058011"
FT VARIANT 134
FT /note="A -> T (in OOMD3; loss of interaction with ZP2;
FT dbSNP:rs1554625334)"
FT /evidence="ECO:0000269|PubMed:28886344"
FT /id="VAR_079712"
FT VARIANT 315
FT /note="S -> P (in dbSNP:rs2906999)"
FT /evidence="ECO:0000269|PubMed:14702039,
FT ECO:0000269|PubMed:1478648, ECO:0000269|PubMed:15489334,
FT ECO:0000269|PubMed:2385582"
FT /id="VAR_058012"
FT VARIANT 340
FT /note="M -> V (in dbSNP:rs2906997)"
FT /id="VAR_058013"
FT CONFLICT 345
FT /note="R -> T (in Ref. 2; CAA40095)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 424 AA; 47018 MW; 0F3CCDA2427C0E3A CRC64;
MELSYRLFIC LLLWGSTELC YPQPLWLLQG GASHPETSVQ PVLVECQEAT LMVMVSKDLF
GTGKLIRAAD LTLGPEACEP LVSMDTEDVV RFEVGLHECG NSMQVTDDAL VYSTFLLHDP
RPVGNLSIVR TNRAEIPIEC RYPRQGNVSS QAILPTWLPF RTTVFSEEKL TFSLRLMEEN
WNAEKRSPTF HLGDAAHLQA EIHTGSHVPL RLFVDHCVAT PTPDQNASPY HTIVDFHGCL
VDGLTDASSA FKVPRPGPDT LQFTVDVFHF ANDSRNMIYI TCHLKVTLAE QDPDELNKAC
SFSKPSNSWF PVEGSADICQ CCNKGDCGTP SHSRRQPHVM SQWSRSASRN RRHVTEEADV
TVGPLIFLDR RGDHEVEQWA LPSDTSVVLL GVGLAVVVSL TLTAVILVLT RRCRTASHPV
SASE
