ZP2_BOVIN
ID ZP2_BOVIN Reviewed; 713 AA.
AC Q9BH10;
DT 13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 25-MAY-2022, entry version 101.
DE RecName: Full=Zona pellucida sperm-binding protein 2;
DE AltName: Full=Zona pellucida glycoprotein 2;
DE Short=Zp-2;
DE AltName: Full=Zona pellucida protein A;
DE Contains:
DE RecName: Full=Processed zona pellucida sperm-binding protein 2;
DE Flags: Precursor;
GN Name=ZP2; Synonyms=ZPA;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND PROTEOLYTIC PROCESSING.
RC TISSUE=Ovary;
RX PubMed=11422390; DOI=10.1046/j.1432-1327.2001.02269.x;
RA Yonezawa N., Fukui N., Kuno M., Shinoda M., Goko S., Mitsui S., Nakano M.;
RT "Molecular cloning of bovine zona pellucida glycoproteins ZPA and ZPB and
RT analysis for sperm-binding component of the zona.";
RL Eur. J. Biochem. 268:3587-3594(2001).
RN [2]
RP PROTEIN SEQUENCE OF 81-91; 178-187; 189-208; 468-477 AND 525-534,
RP GLYCOSYLATION AT ASN-83; ASN-191 AND ASN-527, AND TISSUE SPECIFICITY.
RX PubMed=12199704; DOI=10.1046/j.1432-1033.2002.03111.x;
RA Ikeda K., Yonezawa N., Naoi K., Katsumata T., Hamano S., Nakano M.;
RT "Localization of N-linked carbohydrate chains in glycoprotein ZPA of the
RT bovine egg zona pellucida.";
RL Eur. J. Biochem. 269:4257-4266(2002).
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 ZP2 may act as a secondary sperm receptor.
CC {ECO:0000250|UniProtKB:P20239}.
CC -!- SUBUNIT: Can form homopolymers that assemble into long fibers (in
CC vitro). Polymers of ZP2 and ZP3 organized into long filaments cross-
CC linked by ZP1 homodimers. Interacts with ZP3.
CC {ECO:0000250|UniProtKB:P20239, ECO:0000250|UniProtKB:Q05996}.
CC -!- SUBCELLULAR LOCATION: [Processed zona pellucida sperm-binding protein
CC 2]: Zona pellucida {ECO:0000250|UniProtKB:P20239}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P20239};
CC Single-pass type I membrane protein {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: Expressed in oocytes (at protein level).
CC {ECO:0000269|PubMed:12199704}.
CC -!- DOMAIN: The ZP domain is involved in the polymerization of the ZP
CC proteins to form the zona pellucida. {ECO:0000250|UniProtKB:P20239}.
CC -!- PTM: Proteolytically cleaved before the transmembrane segment to yield
CC the secreted ectodomain incorporated in the zona pellucida.
CC {ECO:0000269|PubMed:11422390}.
CC -!- PTM: Additional proteolytically cleavage of the N-terminal peptide of
CC 30 kDa occurs in one-cell and two-cell embryos (By similarity).
CC Proteolytically cleaved in the N-terminal part probably by the
CC metalloendopeptidase ASTL exocytosed from cortical granules after
CC fertilization, yielding a N-terminal peptide of about 30 kDa which
CC remains covalently attached to the C-terminal peptide via disulfide
CC bond(s). This cleavage may play an important role in the post-
CC fertilization block to polyspermy. {ECO:0000250|UniProtKB:P20239,
CC ECO:0000269|PubMed:11422390}.
CC -!- PTM: N-glycosylated; N-linked glycans are of high-mannose/hybrid type,
CC as well as bi-, tri- and tetra-antennary sialylated complex types.
CC {ECO:0000269|PubMed:12199704}.
CC -!- PTM: O-glycosylated; contains sulfate-substituted glycans.
CC {ECO:0000250|UniProtKB:P20239}.
CC -!- SIMILARITY: Belongs to the ZP domain family. ZPA subfamily.
CC {ECO:0000305}.
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DR EMBL; AB042653; BAB21482.1; -; mRNA.
DR RefSeq; NP_776398.1; NM_173973.2.
DR AlphaFoldDB; Q9BH10; -.
DR SMR; Q9BH10; -.
DR STRING; 9913.ENSBTAP00000015289; -.
DR GlyConnect; 631; 9 N-Linked glycans.
DR iPTMnet; Q9BH10; -.
DR PaxDb; Q9BH10; -.
DR PRIDE; Q9BH10; -.
DR GeneID; 280963; -.
DR KEGG; bta:280963; -.
DR CTD; 7783; -.
DR eggNOG; ENOG502QPI2; Eukaryota.
DR InParanoid; Q9BH10; -.
DR OrthoDB; 586615at2759; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0062023; C:collagen-containing extracellular matrix; ISS:UniProtKB.
DR GO; GO:0035805; C:egg coat; ISS:UniProtKB.
DR GO; GO:0005783; C:endoplasmic reticulum; ISS:UniProtKB.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005771; C:multivesicular body; ISS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0032190; F:acrosin binding; IBA:GO_Central.
DR GO; GO:0035804; F:structural constituent of egg coat; ISS:UniProtKB.
DR GO; GO:0007339; P:binding of sperm to zona pellucida; ISS:UniProtKB.
DR GO; GO:0060468; P:prevention of polyspermy; ISS:UniProtKB.
DR Gene3D; 2.60.40.4100; -; 1.
DR InterPro; IPR042235; ZP-C.
DR InterPro; IPR001507; ZP_dom.
DR InterPro; IPR017977; ZP_dom_CS.
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 Cell membrane; Cleavage on pair of basic residues;
KW Direct protein sequencing; Disulfide bond; Extracellular matrix;
KW Fertilization; Glycoprotein; Membrane; Receptor; Reference proteome;
KW Secreted; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..35
FT /evidence="ECO:0000250|UniProtKB:P20239"
FT CHAIN 36..635
FT /note="Zona pellucida sperm-binding protein 2"
FT /id="PRO_0000041683"
FT CHAIN 36..?
FT /note="Processed zona pellucida sperm-binding protein 2"
FT /id="PRO_0000304556"
FT PROPEP 636..713
FT /note="Removed in mature form"
FT /evidence="ECO:0000250|UniProtKB:P20239"
FT /id="PRO_0000041684"
FT TOPO_DOM 36..682
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 683..703
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 704..713
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 366..632
FT /note="ZP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00375"
FT REGION 464..486
FT /note="Disordered"
FT /evidence="ECO:0000250|UniProtKB:P20239"
FT SITE 167..168
FT /note="Cleavage; by ASTL"
FT /evidence="ECO:0000250|UniProtKB:P20239"
FT SITE 635..636
FT /note="Cleavage"
FT /evidence="ECO:0000250|UniProtKB:P20239"
FT CARBOHYD 83
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:12199704"
FT CARBOHYD 191
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:12199704"
FT CARBOHYD 457
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000250"
FT CARBOHYD 527
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:12199704"
FT DISULFID 51..134
FT /evidence="ECO:0000250|UniProtKB:P20239"
FT DISULFID 84..102
FT /evidence="ECO:0000250|UniProtKB:P20239"
FT DISULFID 367..460
FT /evidence="ECO:0000250|UniProtKB:P20239"
FT DISULFID 398..419
FT /evidence="ECO:0000250|UniProtKB:P20239"
FT DISULFID 540..610
FT /evidence="ECO:0000250|UniProtKB:P20239"
FT DISULFID 561..629
FT /evidence="ECO:0000250|UniProtKB:P20239"
FT DISULFID 615..625
FT /evidence="ECO:0000250|UniProtKB:P20239"
SQ SEQUENCE 713 AA; 79548 MW; DB83ED66B10D3CE3 CRC64;
MACRQRGDSG RPSSWFRADW RSFFLSFTLL TSVNSIDVNQ LDPAFPGTVT CYENRMVVEF
KRTLGNKIQH ASVVDSLGLK MLNCTYVLDP EKLTLKAPYE SCTKRVLGQH QMTITFMNDN
TAHRQKTVLY HVSCPVMQAG RHDQHSGSTI CSKDFMSFTF HFFPGLADDT AGPKPQMGWT
VTVGDGERAQ NLTLQEALTQ GYNLLIENQK MSIQVLFHAT GVTHYSQGNS HLYMVPLKLT
HVSPGQTIIL SSRLICASDP VTCNATHMTL TIPEFPGKLK SVSFENKNIA VNQLHNSGIV
MEIANGLRLH FSKTLLKTKF SEKCLPYQFY LSSLKLTFYT QLETVSMVIY PECVCESTVS
IVSGELCTQD GFMDVEVYRH QTKPALNLDT LRVGDSSCQP TIKAPFQGLV KFHIPLNGCG
TRHKFENGKV IYENEIHALW ADLPPSTISR DSEFRMTVRC YYSSSNMLIN TNVESLPPPV
ASVKPGPLAL TLQTYPDNSY LQPYGDKDYP VVRYLRQPIY LEVRVLNRTD PNIKLVLDDC
WATSTMDPAS LPQWNIIVDG CEYNLDNHRT TFHPVGSSVA YPNHYQRFAV KTFAFVSEDP
AFSHLVYFHC SALICDQLSS NFPLCSASCL VSSRSRRATG ATEEEKMIVS LPGPILLLSD
GSSFRDAVDS KGHGTSGYAA FKTMVAVVAL AGVVATLSLI SYLRKKRITV LNH
