Q05996 (ZP2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Zona pellucida sperm-binding protein 2

Alternative name(s):
Zona pellucida glycoprotein 2
Short name=Zp-2
Zona pellucida protein A

Cleaved into the following chain:

1. Processed zona pellucida sperm-binding protein 2

Gene names

Name:	ZP2
Synonyms:	ZPA

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	745 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at transcript level

General annotation (Comments)

Function	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. ZP2 may act as a secondary sperm receptor.
Subunit structure	Polymers of ZP2 and ZP3 organized into long filaments cross-linked by ZP1 homodimers By similarity.
Subcellular location	Processed zona pellucida sperm-binding protein 2: Secreted › extracellular space › extracellular matrix. Cell membrane; Single-pass type I membrane protein.
Tissue specificity	Oocytes.
Developmental stage	Expressed during the 2-week growth phase of oogenesis, prior to ovulation.
Domain	The ZP domain is involved in the polymerization of the ZP proteins to form the zona pellucida.
Post-translational modification	Proteolytically cleaved before the transmembrane segment to yield the secreted ectodomain incorporated in the zona pellucida. Proteolytically cleaved in the N-terminal part after fertilization, yielding a N-terminal peptide of about 30 kDa which remains covalently attached to the C-terminal peptide via disulfide bond(s). This cleavage may play an important role in the post-fertilization block to polyspermy By similarity. O-glycosylated; contains sulfate-substituted glycans By similarity.
Sequence similarities	Belongs to the ZP domain family. ZPA subfamily. Contains 1 ZP domain.

Ontologies

Keywords
Biological process	Fertilization
Cellular component	Cell membrane Extracellular matrix Membrane Secreted
Coding sequence diversity	Polymorphism
Domain	Signal Transmembrane Transmembrane helix
Molecular function	Receptor
PTM	Cleavage on pair of basic residues Disulfide bond Glycoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	binding of sperm to zona pellucida Traceable author statement. Source: ProtInc intracellular protein transport Inferred from sequence or structural similarity. Source: UniProtKB
Cellular component	Golgi apparatus Inferred from sequence or structural similarity. Source: UniProtKB endoplasmic reticulum Inferred from sequence or structural similarity. Source: UniProtKB integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW multivesicular body Inferred from sequence or structural similarity. Source: UniProtKB plasma membrane Inferred from sequence or structural similarity. Source: UniProtKB proteinaceous extracellular matrix Inferred from electronic annotation. Source: UniProtKB-SubCell secretory granule Inferred from sequence or structural similarity. Source: UniProtKB
Molecular function	acrosin binding Inferred from physical interaction. Source: UniProtKB coreceptor activity Traceable author statement. Source: ProtInc
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 38	38
	Chain	39 – 640	602	Zona pellucida sperm-binding protein 2		PRO_0000041689
	Chain	39 – ?		Processed zona pellucida sperm-binding protein 2		PRO_0000304559
	Propeptide	641 – 745	105	Removed in mature form By similarity		PRO_0000041690
Regions
	Topological domain	39 – 716	678	Extracellular Potential
	Transmembrane	717 – 736	20	Helical; Potential
	Topological domain	737 – 745	9	Cytoplasmic Potential
	Domain	371 – 637	267	ZP
Sites
	Site	172 – 173	2	Cleavage By similarity
Amino acid modifications
	Glycosylation	87	1	N-linked (GlcNAc...) By similarity
	Glycosylation	105	1	N-linked (GlcNAc...) Potential
	Glycosylation	122	1	N-linked (GlcNAc...) Potential
	Glycosylation	223	1	N-linked (GlcNAc...) By similarity
	Glycosylation	269	1	N-linked (GlcNAc...) By similarity
	Glycosylation	400	1	N-linked (GlcNAc...) By similarity
	Glycosylation	462	1	O-linked (GalNAc...) By similarity
	Disulfide bond	88 ↔ 106		By similarity
	Disulfide bond	372 ↔ 465		By similarity
	Disulfide bond	403 ↔ 424		By similarity
	Disulfide bond	615 ↔ 620		By similarity
	Disulfide bond	630 ↔ 634		By similarity
Natural variations
	Natural variant	36	1	G → V. Ref.5 Corresponds to variant rs2075520 [ dbSNP | Ensembl ].		VAR_024705

Sequences

	Sequence		Length	Mass (Da)
	Q05996 [UniParc]. Last modified February 1, 1994. Version 1. Checksum: 2614DA79738F2CDD	FASTA	745	82,357
	10 20 30 40 50 60 MACRQRGGSW SPSGWFNAGW STYRSISLFF ALVTSGNSID VSQLVNPAFP GTVTCDEREI 70 80 90 100 110 120 TVEFPSSPGT KKWHASVVDP LGLDMPNCTY ILDPEKLTLR ATYDNCTRRV HGGHQMTIRV 130 140 150 160 170 180 MNNSAALRHG AVMYQFFCPA MQVEETQGLS ASTICQKDFM SFSLPRVFSG LADDSKGTKV 190 200 210 220 230 240 QMGWSIEVGD GARAKTLTLP EAMKEGFSLL IDNHRMTFHV PFNATGVTHY VQGNSHLYMV 250 260 270 280 290 300 SLKLTFISPG QKVIFSSQAI CAPDPVTCNA THMTLTIPEF PGKLKSVSFE NQNIDVSQLH 310 320 330 340 350 360 DNGIDLEATN GMKLHFSKTL LKTKLSEKCL LHQFYLASLK LTFLLRPETV SMVIYPECLC 370 380 390 400 410 420 ESPVSIVTGE LCTQDGFMDV EVYSYQTQPA LDLGTLRVGN SSCQPVFEAQ SQGLVRFHIP 430 440 450 460 470 480 LNGCGTRYKF EDDKVVYENE IHALWTDFPP SKISRDSEFR MTVKCSYSRN DMLLNINVES 490 500 510 520 530 540 LTPPVASVKL GPFTLILQSY PDNSYQQPYG ENEYPLVRFL RQPIYMEVRV LNRDDPNIKL 550 560 570 580 590 600 VLDDCWATST MDPDSFPQWN VVVDGCAYDL DNYQTTFHPV GSSVTHPDHY QRFDMKAFAF 610 620 630 640 650 660 VSEAHVLSSL VYFHCSALIC NRLSPDSPLC SVTCPVSSRH RRATGATEAE KMTVSLPGPI 670 680 690 700 710 720 LLLSDDSSFR GVGSSDLKAS GSSGEKSRSE TGEEVGSRGA MDTKGHKTAG DVGSKAVAAV 730 740 AAFAGVVATL GFIYYLYEKR TVSNH

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Conservation of mammalian secondary sperm receptor genes enables the promoter of the human gene to function in mouse oocytes." Liang L.-F., Dean J. Dev. Biol. 156:399-408(1993) [PubMed: 8385033] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. 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: 14702039] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Cerebellum.
[3]	"Genome duplications and other features in 12 Mb of DNA sequence from human chromosome 16p and 16q." Loftus B.J., Kim U.-J., Sneddon V.P., Kalush F., Brandon R., Fuhrmann J., Mason T., Crosby M.L., Barnstead M., Cronin L., Mays A.D., Cao Y., Xu R.X., Kang H.-L., Mitchell S., Eichler E.E., Harris P.C., Venter J.C., Adams M.D. Genomics 60:295-308(1999) [PubMed: 10493829] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]	Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases 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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT VAL-36.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	M90366 mRNA. Translation: AAA61335.1. AK313003 mRNA. Translation: BAG35839.1. AF001550 Genomic DNA. Translation: AAB67599.1. CH471228 Genomic DNA. Translation: EAW66859.1. BC096304 mRNA. Translation: AAH96304.1. BC096306 mRNA. Translation: AAH96306.1. BC096307 mRNA. Translation: AAH96307.1.
IPI	IPI00016870.
PIR	A48833.
RefSeq	NP_003451.1. NM_003460.1.
UniGene	Hs.73982.
3D structure databases
ProteinModelPortal	Q05996.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q05996. 2 interactions.
MINT	MINT-7241855.
STRING	Q05996.
PTM databases
PhosphoSite	Q05996.
Polymorphism databases
DMDM	466206.
Proteomic databases
PRIDE	Q05996.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000219593; ENSP00000219593; ENSG00000103310. ENST00000423164; ENSP00000413783; ENSG00000103310.
GeneID	7783.
KEGG	hsa:7783.
UCSC	uc002dii.2. human.
Organism-specific databases
CTD	7783.
GeneCards	GC16M021116.
H-InvDB	HIX0038649.
HGNC	HGNC:13188. ZP2.
HPA	HPA011296.
MIM	182888. gene.
neXtProt	NX_Q05996.
PharmGKB	PA37756.
GenAtlas	Search...
Phylogenomic databases
eggNOG	prNOG17048.
HOGENOM	HBG267689.
HOVERGEN	HBG004379.
InParanoid	Q05996.
OMA	NRNDPNI.
OrthoDB	EOG4CG085.
PhylomeDB	Q05996.
Gene expression databases
ArrayExpress	Q05996.
Bgee	Q05996.
CleanEx	HS_ZP2.
Genevestigator	Q05996.
GermOnline	ENSG00000103310. Homo sapiens.
Family and domain databases
InterPro	IPR017977. Endoglin/CD105_CS. IPR017976. Endoglin/CD105_subgr. IPR001507. Zona_pellucida_Endoglin/CD105. [Graphical view]
Pfam	PF00100. Zona_pellucida. 1 hit. [Graphical view]
PRINTS	PR00023. ZPELLUCIDA.
SMART	SM00241. ZP. 1 hit. [Graphical view]
PROSITE	PS00682. ZP_1. 1 hit. PS51034. ZP_2. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	30133.
SOURCE	Search...

Entry information

Entry name

ZP2_HUMAN

Accession

Primary (citable) accession number: Q05996
Secondary accession number(s): B2R7J2, Q4VAN9, Q4VAP0

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1994
Last sequence update:	February 1, 1994
Last modified:	January 25, 2012
This is version 94 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.