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Protein

Zona pellucida sperm-binding protein 1

Gene

Zp1

Organism
Rattus norvegicus (Rat)
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

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
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Unplaced

Organism-specific databases

RGDi620604. 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)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini21 – 588568ExtracellularSequence analysisAdd
BLAST
Transmembranei589 – 60921HelicalSequence analysisAdd
BLAST
Topological domaini610 – 6178CytoplasmicSequence analysis

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Extracellular matrix, Membrane, Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 20201 PublicationAdd
BLAST
Chaini21 – 544524Zona pellucida sperm-binding protein 1PRO_0000041681Add
BLAST
Chaini21 – ?Processed zona pellucida sperm-binding protein 1PRO_0000304555
Propeptidei545 – 61773Removed in mature form1 PublicationPRO_0000041682Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei21 – 211Pyrrolidone carboxylic acid1 Publication
Glycosylationi49 – 491N-linked (GlcNAc...)1 Publication
Glycosylationi68 – 681N-linked (GlcNAc...)1 Publication
Disulfide bondi226 ↔ 251PROSITE-ProRule annotation
Disulfide bondi235 ↔ 250PROSITE-ProRule annotation
Disulfide bondi245 ↔ 260PROSITE-ProRule annotation
Glycosylationi369 – 3691N-linked (GlcNAc...)1 Publication
Disulfide bondi447 ↔ 468PROSITE-ProRule annotation1 Publication

Post-translational modificationi

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

Keywords - PTMi

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

Proteomic databases

PaxDbiO54766.
PRIDEiO54766.

Expressioni

Tissue specificityi

Oocytes.

Interactioni

Subunit structurei

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

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000028396.

Structurei

3D structure databases

ProteinModelPortaliO54766.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini224 – 26441P-typePROSITE-ProRule annotationAdd
BLAST
Domaini269 – 540272ZPPROSITE-ProRule annotationAdd
BLAST

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.
HOGENOMiHOG000118071.
HOVERGENiHBG036289.
InParanoidiO54766.
KOiK19926.
PhylomeDBiO54766.

Family and domain databases

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.

O54766-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAWGCFVVLL LLVAAPLRLG QHLHLKPGFQ YSYDCGVQGM QLLVFPRPNQ
60 70 80 90 100
TIQFKVLDEF GNRFEVNNCS ICYHWVISEA QKPAVFSADY KGCHVLEKQD
110 120 130 140 150
GRFHLRVFIQ AVLPNGRVDT AQDVTLICPK PDHILTPESY LAPPTTPQPF
160 170 180 190 200
IPHTFALHPI SGHTLAGSGH TGLTTLYPET HPTPAPPSSE PGPVGPTVPQ
210 220 230 240 250
SQWGTLGSWE LTELDSIGTH LLQERCQVAS GHIPCMVKGS SEEACQQAGC
260 270 280 290 300
CYDNTKEMPC YYGNTVTLQC FRSGYFTLVM SQETALTHGV MLDNVHLAYA
310 320 330 340 350
PNGCPPTQKT SAFVVFHVPL TLCGTAIQVV GKQLVYENQL VSNIEVQTGP
360 370 380 390 400
QGSITRDGVF RLHVRCIFNA SDFLPIRASI FSPQPPAPVT RSGPLRLELR
410 420 430 440 450
IATDKTFSSY YQGSDYPLVR LLQEPVYIEV RLLQRTDPGL ALMLHQCWAT
460 470 480 490 500
PSASPFEQPQ WPILSDGCPF KGDNYRTQMV AADRATLPFW SHYQRFTIAT
510 520 530 540 550
FTLLDSSSQN ALRGQVYFFC SASACHPVGS ETCSTTCDSE IARHRRSSGH
560 570 580 590 600
HNSTIRALDI VSSPGAVGFE DAPKLEPSGS TRNSGSRPLL WVLQLLALTL
610
VLGDGVLVGL SWAWAWA
Length:617
Mass (Da):67,853
Last modified:June 1, 1998 - v1
Checksum:iAF52D9227F8A4CCC
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB000928 mRNA. Translation: BAA24486.1.
RefSeqiNP_445961.1. NM_053509.1.
UniGeneiRn.10890.

Genome annotation databases

GeneIDi85271.
KEGGirno:85271.
UCSCiRGD:620604. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB000928 mRNA. Translation: BAA24486.1.
RefSeqiNP_445961.1. NM_053509.1.
UniGeneiRn.10890.

3D structure databases

ProteinModelPortaliO54766.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000028396.

Proteomic databases

PaxDbiO54766.
PRIDEiO54766.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi85271.
KEGGirno:85271.
UCSCiRGD:620604. rat.

Organism-specific databases

CTDi22917.
RGDi620604. Zp1.

Phylogenomic databases

eggNOGiENOG410IE4J. Eukaryota.
ENOG4111H75. LUCA.
HOGENOMiHOG000118071.
HOVERGENiHBG036289.
InParanoidiO54766.
KOiK19926.
PhylomeDBiO54766.

Miscellaneous databases

NextBioi617430.
PROiO54766.

Family and domain databases

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...

Publicationsi

  1. "Rat zona pellucida glycoproteins: molecular cloning and characterization of the three major components."
    Akatsuka K., Yoshida-Komiya H., Tulsiani D.R.P., Orgebin-Crist M.-C., Hiroi M., Araki Y.
    Mol. Reprod. Dev. 51:454-467(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: Sprague-Dawley.
    Tissue: Ovary.
  2. "Structural conservation of mouse and rat zona pellucida glycoproteins. Probing the native rat zona pellucida proteome by mass spectrometry."
    Boja E.S., Hoodbhoy T., Garfield M., Fales H.M.
    Biochemistry 44:16445-16460(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF C-TERMINUS, PYROGLUTAMATE FORMATION AT GLN-21, DISULFIDE BOND FORMATION AT 447-CYS--CYS-468, GLYCOSYLATION AT ASN-49; ASN-68 AND ASN-369, IDENTIFICATION BY MASS SPECTROMETRY.

Entry informationi

Entry nameiZP1_RAT
AccessioniPrimary (citable) accession number: O54766
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 13, 2004
Last sequence update: June 1, 1998
Last modified: May 11, 2016
This is version 98 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. 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.