ID A0A2K5F4R2_AOTNA Unreviewed; 424 AA.
AC A0A2K5F4R2;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE RecName: Full=Zona pellucida sperm-binding protein 3 {ECO:0000256|ARBA:ARBA00017980, ECO:0000256|RuleBase:RU367066};
OS Aotus nancymaae (Ma's night monkey).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Platyrrhini; Aotidae;
OC Aotus.
OX NCBI_TaxID=37293 {ECO:0000313|Ensembl:ENSANAP00000040389.1, ECO:0000313|Proteomes:UP000233020};
RN [1] {ECO:0000313|Ensembl:ENSANAP00000040389.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
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 {ECO:0000256|ARBA:ARBA00003205, ECO:0000256|RuleBase:RU367066}.
CC -!- SUBCELLULAR LOCATION: Zona pellucida {ECO:0000256|RuleBase:RU367066}.
CC Cell membrane {ECO:0000256|RuleBase:RU367066}; Single-pass type I
CC membrane protein {ECO:0000256|RuleBase:RU367066}.
CC -!- DOMAIN: The ZP domain is involved in the polymerization of the ZP
CC proteins to form the zona pellucida. {ECO:0000256|RuleBase:RU367066}.
CC -!- PTM: Proteolytically cleaved before the transmembrane segment to yield
CC the secreted ectodomain incorporated in the zona pellucida.
CC {ECO:0000256|RuleBase:RU367066}.
CC -!- SIMILARITY: Belongs to the ZP domain family. ZPC subfamily.
CC {ECO:0000256|ARBA:ARBA00006735, ECO:0000256|RuleBase:RU367066}.
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DR RefSeq; XP_012304443.1; XM_012449020.1.
DR AlphaFoldDB; A0A2K5F4R2; -.
DR STRING; 37293.ENSANAP00000040389; -.
DR Ensembl; ENSANAT00000058498.1; ENSANAP00000040389.1; ENSANAG00000037554.1.
DR GeneID; 105714888; -.
DR CTD; 7784; -.
DR GeneTree; ENSGT01030000234567; -.
DR OMA; CSYINGW; -.
DR OrthoDB; 5355932at2759; -.
DR Proteomes; UP000233020; Unplaced.
DR GO; GO:0062023; C:collagen-containing extracellular matrix; IEA:Ensembl.
DR GO; GO:0035805; C:egg coat; IEA:UniProtKB-SubCell.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0048018; F:receptor ligand activity; IEA:Ensembl.
DR GO; GO:0035804; F:structural constituent of egg coat; IEA:UniProtKB-UniRule.
DR GO; GO:0007339; P:binding of sperm to zona pellucida; IEA:UniProtKB-UniRule.
DR GO; GO:0001825; P:blastocyst formation; IEA:Ensembl.
DR GO; GO:0035803; P:egg coat formation; IEA:UniProtKB-UniRule.
DR GO; GO:0002455; P:humoral immune response mediated by circulating immunoglobulin; IEA:Ensembl.
DR GO; GO:0045892; P:negative regulation of DNA-templated transcription; IEA:Ensembl.
DR GO; GO:0048599; P:oocyte development; IEA:Ensembl.
DR GO; GO:2000344; P:positive regulation of acrosome reaction; IEA:UniProtKB-UniRule.
DR GO; GO:2000388; P:positive regulation of antral ovarian follicle growth; IEA:Ensembl.
DR GO; GO:0045893; P:positive regulation of DNA-templated transcription; IEA:Ensembl.
DR GO; GO:0032753; P:positive regulation of interleukin-4 production; IEA:Ensembl.
DR GO; GO:0002687; P:positive regulation of leukocyte migration; IEA:Ensembl.
DR GO; GO:2000386; P:positive regulation of ovarian follicle development; IEA:Ensembl.
DR GO; GO:0042102; P:positive regulation of T cell proliferation; IEA:Ensembl.
DR GO; GO:0032729; P:positive regulation of type II interferon production; IEA:Ensembl.
DR GO; GO:0001809; P:positive regulation of type IV hypersensitivity; IEA:Ensembl.
DR Gene3D; 2.60.40.4100; Zona pellucida, ZP-C domain; 1.
DR Gene3D; 2.60.40.3210; Zona pellucida, ZP-N domain; 1.
DR InterPro; IPR042235; ZP-C.
DR InterPro; IPR048290; ZP_chr.
DR InterPro; IPR001507; ZP_dom.
DR InterPro; IPR017977; ZP_dom_CS.
DR PANTHER; PTHR11576; ZONA PELLUCIDA SPERM-BINDING PROTEIN 3; 1.
DR PANTHER; PTHR11576:SF2; ZONA PELLUCIDA SPERM-BINDING PROTEIN 3; 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 3: Inferred from homology;
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475,
KW ECO:0000256|RuleBase:RU367066};
KW Cleavage on pair of basic residues {ECO:0000256|RuleBase:RU367066};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157,
KW ECO:0000256|RuleBase:RU367066};
KW Extracellular matrix {ECO:0000256|RuleBase:RU367066};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU367066};
KW Pyrrolidone carboxylic acid {ECO:0000256|ARBA:ARBA00023283};
KW Reference proteome {ECO:0000313|Proteomes:UP000233020};
KW Secreted {ECO:0000256|ARBA:ARBA00022525, ECO:0000256|RuleBase:RU367066};
KW Signal {ECO:0000256|RuleBase:RU367066};
KW Transmembrane {ECO:0000256|RuleBase:RU367066};
KW Transmembrane helix {ECO:0000256|RuleBase:RU367066}.
FT SIGNAL 1..22
FT /evidence="ECO:0000256|RuleBase:RU367066"
FT CHAIN 23..424
FT /note="Zona pellucida sperm-binding protein 3"
FT /evidence="ECO:0000256|RuleBase:RU367066"
FT /id="PRO_5025705626"
FT TRANSMEM 387..409
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367066"
FT DOMAIN 45..307
FT /note="ZP"
FT /evidence="ECO:0000259|PROSITE:PS51034"
SQ SEQUENCE 424 AA; 46799 MW; C8447F8E74C75E8B CRC64;
MELNYGLFIC LLLWGSTELC YPQPLRLLQG GASRSETAVQ PVVVECREAT LVVTVSKDLF
GTRKLIRAVD LTLGPEGCEP LVSTDTEDVV RFEVGLHECG NSMQVTDDAL VYSTFLLHDP
RPVGNLSIVR TNRAEIPIEC HYPRRGNVSS QAILPTWLPF RTTVFSEEKL TFSLRLMEEN
WSAEKRTPTF HLGDAAYLQA EIHTGSHVPL RLFVDQCVAT PTPDQNASPY HTIVDFHGCL
VDGLTDASSA FQVPRPRPDT LQFTVDVFHF ANDSRNMIYI TCHLKVTLAE QDPDELNKAC
SFSKPSNSWF PVEGPADICQ CCSKGDCGTP SHARRQPHVV SLGSSSSARN RRHVTEEADV
TVGPLIFLDR TGDHKMEQWA LPADTSLLLL GTGLAVVAFL TLTAVILVLT RRCRTASHPV
SASQ
//
