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Protein

Zona pellucida sperm-binding protein 1

Gene

Zp1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

The mammalian zona pellucida, which mediates species-specific sperm binding, induction of the acrosome reaction and prevents post-fertilization polyspermy, is composed of three to four glycoproteins, ZP1, ZP2, ZP3, and ZP4. ZP1 ensures the structural integrity of the zona pellucida.

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Fertilization

Enzyme and pathway databases

ReactomeiR-MMU-1300644. Interaction With The Zona Pellucida.

Names & Taxonomyi

Protein namesi
Recommended name:
Zona pellucida sperm-binding protein 1
Alternative name(s):
Zona pellucida glycoprotein 1
Short name:
Zp-1
Cleaved into the following chain:
Gene namesi
Name:Zp1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 19

Organism-specific databases

MGIiMGI:103073. Zp1.

Subcellular locationi

Processed zona pellucida sperm-binding protein 1 :
  • Secretedextracellular spaceextracellular matrix By similarity

  • Note: The glycoproteinaceous translucent extracellular matrix that surrounds the mammalian oocyte is called zona pellucida.Curated

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini21 – 590ExtracellularSequence analysisAdd BLAST570
Transmembranei591 – 611HelicalSequence analysisAdd BLAST21
Topological domaini612 – 623CytoplasmicSequence analysisAdd BLAST12

GO - Cellular componenti

  • extracellular matrix Source: UniProtKB
  • Golgi apparatus Source: UniProtKB
  • integral component of membrane Source: UniProtKB-KW
  • plasma membrane Source: UniProtKB-SubCell
  • proteinaceous extracellular matrix Source: UniProtKB-SubCell
  • secretory granule Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Extracellular matrix, Membrane, Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 202 PublicationsAdd BLAST20
ChainiPRO_000004167921 – 546Zona pellucida sperm-binding protein 1Add BLAST526
ChainiPRO_000030455421 – ?Processed zona pellucida sperm-binding protein 1
PropeptideiPRO_0000041680547 – 623Removed in mature form1 PublicationAdd BLAST77

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei21Pyrrolidone carboxylic acid1 Publication1
Glycosylationi49N-linked (GlcNAc...)1 Publication1
Glycosylationi68N-linked (GlcNAc...)1 Publication1
Disulfide bondi228 ↔ 253PROSITE-ProRule annotation
Disulfide bondi237 ↔ 252PROSITE-ProRule annotation
Glycosylationi240N-linked (GlcNAc...)1 Publication1
Disulfide bondi247 ↔ 262PROSITE-ProRule annotation
Glycosylationi371N-linked (GlcNAc...)1 Publication1
Disulfide bondi449 ↔ 4701 Publication
Glycosylationi554N-linked (GlcNAc...)Sequence analysis1
Glycosylationi585N-linked (GlcNAc...)Sequence analysis1

Post-translational modificationi

Proteolytically cleaved before the transmembrane segment to yield the secreted ectodomain incorporated in the zona pellucida.
O-glycosylated.1 Publication

Keywords - PTMi

Cleavage on pair of basic residues, Disulfide bond, Glycoprotein, Pyrrolidone carboxylic acid

Proteomic databases

PaxDbiQ62005.
PRIDEiQ62005.

PTM databases

iPTMnetiQ62005.
PhosphoSitePlusiQ62005.

Expressioni

Tissue specificityi

Oocytes.1 Publication

Developmental stagei

Not detected in resting oocytes. As oocytes begin to grow, levels increase to reach a maximum in midsized oocytes. Levels decrease in later stages of oocyte growth.1 Publication

Gene expression databases

BgeeiENSMUSG00000024734.
CleanExiMM_ZP1.
ExpressionAtlasiQ62005. baseline and differential.
GenevisibleiQ62005. MM.

Interactioni

Subunit structurei

Polymers of ZP2 and ZP3 organized into long filaments cross-linked by ZP1 homodimers.

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000025641.

Structurei

3D structure databases

ProteinModelPortaliQ62005.
SMRiQ62005.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini226 – 266P-typePROSITE-ProRule annotationAdd BLAST41
Domaini271 – 542ZPPROSITE-ProRule annotationAdd BLAST272

Domaini

The ZP domain is involved in the polymerization of the ZP proteins to form the zona pellucida.

Sequence similaritiesi

Belongs to the ZP domain family. ZPB subfamily.Curated
Contains 1 P-type (trefoil) domain.PROSITE-ProRule annotation
Contains 1 ZP domain.PROSITE-ProRule annotation

Keywords - Domaini

Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiENOG410IE4J. Eukaryota.
ENOG4111H75. LUCA.
GeneTreeiENSGT00530000063096.
HOGENOMiHOG000118071.
HOVERGENiHBG036289.
InParanoidiQ62005.
KOiK19926.
OMAiFCSASAC.
OrthoDBiEOG091G0UNU.
PhylomeDBiQ62005.
TreeFamiTF332794.

Family and domain databases

CDDicd00111. Trefoil. 1 hit.
Gene3Di4.10.110.10. 1 hit.
InterProiIPR017957. P_trefoil_CS.
IPR000519. P_trefoil_dom.
IPR001507. ZP_dom.
IPR017977. ZP_dom_CS.
[Graphical view]
PfamiPF00088. Trefoil. 1 hit.
PF00100. Zona_pellucida. 1 hit.
[Graphical view]
PRINTSiPR00023. ZPELLUCIDA.
SMARTiSM00018. PD. 1 hit.
SM00241. ZP. 1 hit.
[Graphical view]
SUPFAMiSSF57492. SSF57492. 1 hit.
PROSITEiPS00025. P_TREFOIL_1. 1 hit.
PS51448. P_TREFOIL_2. 1 hit.
PS00682. ZP_1. 1 hit.
PS51034. ZP_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q62005-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAWGCFVVLL LLAAAPLRLG QRLHLEPGFE YSYDCGVRGM QLLVFPRPNQ
60 70 80 90 100
TVQFKVLDEF GNRFEVNNCS ICYHWVTSEA QEHTVFSADY KGCHVLEKDG
110 120 130 140 150
RFHLRVFIQA VLPNGRVDIA QDVTLICPKP DHTVTPDPYL APPTTPEPFT
160 170 180 190 200
PHAFALHPIP DHTLAGSGHT GLTTLYPEQS FIHPTPAPPS LGPGPAGSTV
210 220 230 240 250
PHSQWGTLEP WELTELDSVG THLPQERCQV ASGHIPCMVN GSSKETCQQA
260 270 280 290 300
GCCYDSTKEE PCYYGNTVTL QCFKSGYFTL VMSQETALTH GVLLDNVHLA
310 320 330 340 350
YAPNGCPPTQ KTSAFVVFHV PLTLCGTAIQ VVGEQLIYEN QLVSDIDVQK
360 370 380 390 400
GPQGSITRDS AFRLHVRCIF NASDFLPIQA SIFSPQPPAP VTQSGPLRLE
410 420 430 440 450
LRIATDKTFS SYYQGSDYPL VRLLREPVYV EVRLLQRTDP SLVLVLHQCW
460 470 480 490 500
ATPTTSPFEQ PQWPILSDGC PFKGDNYRTQ VVAADREALP FWSHYQRFTI
510 520 530 540 550
TTFMLLDSSS QNALRGQVYF FCSASACHPL GSDTCSTTCD SGIARRRRSS
560 570 580 590 600
GHHNITLRAL DIVSSPGAVG FEDAAKLEPS GSSRNSSSRM LLLLLAITLA
610 620
LAAGIFVGLI WAWAQKLWEG IRY
Length:623
Mass (Da):68,723
Last modified:November 1, 1996 - v1
Checksum:i9D95B8613B3B95C8
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti246T → A in AAC48480 (PubMed:7635043).Curated1
Sequence conflicti445V → L in AAC48480 (PubMed:7635043).Curated1
Sequence conflicti486R → K in AAC48480 (PubMed:7635043).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U24230
, U24227, U24228, U24229 Genomic DNA. Translation: AAB60507.1.
U20448 mRNA. Translation: AAC48480.1.
CCDSiCCDS37918.1.
PIRiI46382.
RefSeqiNP_033606.2. NM_009580.2.
UniGeneiMm.24767.

Genome annotation databases

EnsembliENSMUST00000025641; ENSMUSP00000025641; ENSMUSG00000024734.
GeneIDi22786.
KEGGimmu:22786.
UCSCiuc008grh.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U24230
, U24227, U24228, U24229 Genomic DNA. Translation: AAB60507.1.
U20448 mRNA. Translation: AAC48480.1.
CCDSiCCDS37918.1.
PIRiI46382.
RefSeqiNP_033606.2. NM_009580.2.
UniGeneiMm.24767.

3D structure databases

ProteinModelPortaliQ62005.
SMRiQ62005.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000025641.

PTM databases

iPTMnetiQ62005.
PhosphoSitePlusiQ62005.

Proteomic databases

PaxDbiQ62005.
PRIDEiQ62005.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000025641; ENSMUSP00000025641; ENSMUSG00000024734.
GeneIDi22786.
KEGGimmu:22786.
UCSCiuc008grh.2. mouse.

Organism-specific databases

CTDi22917.
MGIiMGI:103073. Zp1.

Phylogenomic databases

eggNOGiENOG410IE4J. Eukaryota.
ENOG4111H75. LUCA.
GeneTreeiENSGT00530000063096.
HOGENOMiHOG000118071.
HOVERGENiHBG036289.
InParanoidiQ62005.
KOiK19926.
OMAiFCSASAC.
OrthoDBiEOG091G0UNU.
PhylomeDBiQ62005.
TreeFamiTF332794.

Enzyme and pathway databases

ReactomeiR-MMU-1300644. Interaction With The Zona Pellucida.

Miscellaneous databases

PROiQ62005.
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000024734.
CleanExiMM_ZP1.
ExpressionAtlasiQ62005. baseline and differential.
GenevisibleiQ62005. MM.

Family and domain databases

CDDicd00111. Trefoil. 1 hit.
Gene3Di4.10.110.10. 1 hit.
InterProiIPR017957. P_trefoil_CS.
IPR000519. P_trefoil_dom.
IPR001507. ZP_dom.
IPR017977. ZP_dom_CS.
[Graphical view]
PfamiPF00088. Trefoil. 1 hit.
PF00100. Zona_pellucida. 1 hit.
[Graphical view]
PRINTSiPR00023. ZPELLUCIDA.
SMARTiSM00018. PD. 1 hit.
SM00241. ZP. 1 hit.
[Graphical view]
SUPFAMiSSF57492. SSF57492. 1 hit.
PROSITEiPS00025. P_TREFOIL_1. 1 hit.
PS51448. P_TREFOIL_2. 1 hit.
PS00682. ZP_1. 1 hit.
PS51034. ZP_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiZP1_MOUSE
AccessioniPrimary (citable) accession number: Q62005
Secondary accession number(s): Q62016
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 19, 2002
Last sequence update: November 1, 1996
Last modified: November 2, 2016
This is version 127 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.