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Protein

Zona pellucida sperm-binding protein 4

Gene

ZP4

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at transcript 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. ZP4 may act as a sperm receptor.

GO - Molecular functioni

  • acrosin binding Source: UniProtKB
  • signal transducer activity Source: UniProtKB

GO - Biological processi

  • acrosomal vesicle exocytosis Source: UniProtKB
  • binding of sperm to zona pellucida Source: Reactome
  • intracellular signal transduction Source: UniProtKB
  • negative regulation of binding of sperm to zona pellucida Source: UniProtKB
  • positive regulation of acrosome reaction Source: UniProtKB
  • positive regulation of humoral immune response Source: UniProtKB
  • positive regulation of protein kinase activity Source: UniProtKB
  • positive regulation of T cell proliferation Source: UniProtKB
  • protein kinase A signaling Source: UniProtKB
  • protein kinase C signaling Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Receptor

Keywords - Biological processi

Fertilization

Enzyme and pathway databases

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

Names & Taxonomyi

Protein namesi
Recommended name:
Zona pellucida sperm-binding protein 4
Alternative name(s):
Zona pellucida glycoprotein 4
Short name:
Zp-4
Zona pellucida protein B
Cleaved into the following chain:
Gene namesi
Name:ZP4
Synonyms:ZPB
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 1

Organism-specific databases

HGNCiHGNC:15770. ZP4.

Subcellular locationi

Processed zona pellucida sperm-binding protein 4 :
  • 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 domaini19 – 505487ExtracellularSequence analysisAdd
BLAST
Transmembranei506 – 52621HelicalSequence analysisAdd
BLAST
Topological domaini527 – 54014CytoplasmicSequence analysisAdd
BLAST

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Extracellular matrix, Membrane, Secreted

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA38036.

Polymorphism and mutation databases

BioMutaiZP4.
DMDMi46397080.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1818Sequence analysisAdd
BLAST
Chaini19 – 462444Zona pellucida sperm-binding protein 4PRO_0000041727Add
BLAST
Chaini19 – ?Processed zona pellucida sperm-binding protein 4PRO_0000304578
Propeptidei463 – 54078Removed in mature formBy similarityPRO_0000041728Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi69 – 691N-linked (GlcNAc...)Sequence analysis
Glycosylationi202 – 2021N-linked (GlcNAc...)By similarity
Glycosylationi219 – 2191N-linked (GlcNAc...)By similarity
Glycosylationi267 – 2671N-linked (GlcNAc...)Sequence analysis
Glycosylationi302 – 3021O-linked (GalNAc...)By similarity
Disulfide bondi367 ↔ 442PROSITE-ProRule annotation
Glycosylationi470 – 4701N-linked (GlcNAc...)Sequence analysis
Glycosylationi474 – 4741N-linked (GlcNAc...)Sequence analysis

Post-translational modificationi

Proteolytically cleaved before the transmembrane segment to yield the secreted ectodomain incorporated in the zona pellucida.

Keywords - PTMi

Cleavage on pair of basic residues, Disulfide bond, Glycoprotein

Proteomic databases

PaxDbiQ12836.
PRIDEiQ12836.

PTM databases

iPTMnetiQ12836.
PhosphoSiteiQ12836.

Expressioni

Tissue specificityi

Oocytes.

Gene expression databases

BgeeiQ12836.
CleanExiHS_ZP4.
GenevisibleiQ12836. HS.

Organism-specific databases

HPAiHPA008547.

Interactioni

GO - Molecular functioni

  • acrosin binding Source: UniProtKB

Protein-protein interaction databases

STRINGi9606.ENSP00000355529.

Structurei

3D structure databases

ProteinModelPortaliQ12836.
SMRiQ12836. Positions 139-195.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini141 – 18343P-typePROSITE-ProRule annotationAdd
BLAST
Domaini188 – 466279ZPPROSITE-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.
GeneTreeiENSGT00530000063096.
HOGENOMiHOG000059607.
HOVERGENiHBG050410.
InParanoidiQ12836.
OMAiSCYYGNT.
OrthoDBiEOG7KQ216.
PhylomeDBiQ12836.
TreeFamiTF332794.

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.

Q12836-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MWLLRCVLLC VSLSLAVSGQ HKPEAPDYSS VLHCGPWSFQ FAVNLNQEAT
60 70 80 90 100
SPPVLIAWDN QGLLHELQND SDCGTWIRKG PGSSVVLEAT YSSCYVTEWD
110 120 130 140 150
SHYIMPVGVE GAGAAEHKVV TERKLLKCPM DLLARDAPDT DWCDSIPARD
160 170 180 190 200
RLPCAPSPIS RGDCEGLGCC YSSEEVNSCY YGNTVTLHCT REGHFSIAVS
210 220 230 240 250
RNVTSPPLLL DSVRLALRND SACNPVMATQ AFVLFQFPFT SCGTTRQITG
260 270 280 290 300
DRAVYENELV ATRDVKNGSR GSVTRDSIFR LHVSCSYSVS SNSLPINVQV
310 320 330 340 350
FTLPPPFPET QPGPLTLELQ IAKDKNYGSY YGVGDYPVVK LLRDPIYVEV
360 370 380 390 400
SILHRTDPYL GLLLQQCWAT PSTDPLSQPQ WPILVKGCPY IGDNYQTQLI
410 420 430 440 450
PVQKALDLPF PSHHQRFSIF TFSFVNPTVE KQALRGPVHL HCSVSVCQPA
460 470 480 490 500
ETPSCVVTCP DLSRRRNFDN SSQNTTASVS SKGPMILLQA TKDPPEKLRV
510 520 530 540
PVDSKVLWVA GLSGTLILGA LLVSYLAVKK QKSCPDQMCQ
Length:540
Mass (Da):59,400
Last modified:November 1, 1996 - v1
Checksum:i9DAC310D808E1AC3
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti114 – 1141A → V.
Corresponds to variant rs34370253 [ dbSNP | Ensembl ].
VAR_052997
Natural varianti295 – 2951P → S.
Corresponds to variant rs34811980 [ dbSNP | Ensembl ].
VAR_052998

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U05781 Genomic DNA. Translation: AAA74391.1.
AK314151 mRNA. Translation: BAG36838.1.
AL359924 Genomic DNA. Translation: CAI22066.1.
CH471098 Genomic DNA. Translation: EAW70072.1.
BC069521 mRNA. Translation: AAH69521.1.
CCDSiCCDS1615.1.
PIRiS70403.
RefSeqiNP_067009.1. NM_021186.4.
UniGeneiHs.136241.

Genome annotation databases

EnsembliENST00000366570; ENSP00000355529; ENSG00000116996.
ENST00000611898; ENSP00000482304; ENSG00000116996.
GeneIDi57829.
KEGGihsa:57829.
UCSCiuc001hym.3. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U05781 Genomic DNA. Translation: AAA74391.1.
AK314151 mRNA. Translation: BAG36838.1.
AL359924 Genomic DNA. Translation: CAI22066.1.
CH471098 Genomic DNA. Translation: EAW70072.1.
BC069521 mRNA. Translation: AAH69521.1.
CCDSiCCDS1615.1.
PIRiS70403.
RefSeqiNP_067009.1. NM_021186.4.
UniGeneiHs.136241.

3D structure databases

ProteinModelPortaliQ12836.
SMRiQ12836. Positions 139-195.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9606.ENSP00000355529.

PTM databases

iPTMnetiQ12836.
PhosphoSiteiQ12836.

Polymorphism and mutation databases

BioMutaiZP4.
DMDMi46397080.

Proteomic databases

PaxDbiQ12836.
PRIDEiQ12836.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000366570; ENSP00000355529; ENSG00000116996.
ENST00000611898; ENSP00000482304; ENSG00000116996.
GeneIDi57829.
KEGGihsa:57829.
UCSCiuc001hym.3. human.

Organism-specific databases

CTDi57829.
GeneCardsiZP4.
HGNCiHGNC:15770. ZP4.
HPAiHPA008547.
MIMi613514. gene.
neXtProtiNX_Q12836.
PharmGKBiPA38036.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiENOG410IE4J. Eukaryota.
ENOG4111H75. LUCA.
GeneTreeiENSGT00530000063096.
HOGENOMiHOG000059607.
HOVERGENiHBG050410.
InParanoidiQ12836.
OMAiSCYYGNT.
OrthoDBiEOG7KQ216.
PhylomeDBiQ12836.
TreeFamiTF332794.

Enzyme and pathway databases

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

Miscellaneous databases

GeneWikiiZP4.
GenomeRNAii57829.
PROiQ12836.
SOURCEiSearch...

Gene expression databases

BgeeiQ12836.
CleanExiHS_ZP4.
GenevisibleiQ12836. HS.

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

« Hide 'large scale' publications
  1. "Cloning and characterization of zona pellucida genes and cDNAs from a variety of mammalian species: the ZPA, ZPB and ZPC gene families."
    Harris J.D., Hibler D.W., Fontenot G.K., Hsu K.T., Yurewicz E.C., Sacco A.G.
    DNA Seq. 4:361-393(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Tissue: Ovary.
  2. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  3. "The DNA sequence and biological annotation of human chromosome 1."
    Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.
    , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
    Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].

Entry informationi

Entry nameiZP4_HUMAN
AccessioniPrimary (citable) accession number: Q12836
Secondary accession number(s): B2RAE1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 13, 2004
Last sequence update: November 1, 1996
Last modified: July 6, 2016
This is version 125 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 1
    Human chromosome 1: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. 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.