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Protein

Hyaluronidase PH-20

Gene

SPAM1

Organism
Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at transcript leveli

Functioni

Involved in sperm-egg adhesion. Upon fertilization sperm must first penetrate a layer of cumulus cells that surrounds the egg before reaching the zona pellucida. The cumulus cells are embedded in a matrix containing hyaluronic acid which is formed prior to ovulation. This protein aids in penetrating the layer of cumulus cells by digesting hyaluronic acid.

Catalytic activityi

Random hydrolysis of (1->4)-linkages between N-acetyl-beta-D-glucosamine and D-glucuronate residues in hyaluronate.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei148Proton donorBy similarity1

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Glycosidase, Hydrolase

Keywords - Biological processi

Cell adhesion

Protein family/group databases

CAZyiGH56. Glycoside Hydrolase Family 56.

Names & Taxonomyi

Protein namesi
Recommended name:
Hyaluronidase PH-20 (EC:3.2.1.35)
Short name:
Hyal-PH20
Alternative name(s):
Hyaluronoglucosaminidase PH-20
Sperm adhesion molecule 1
Sperm surface protein PH-20
Gene namesi
Name:SPAM1
Synonyms:PH20
ORF Names:EGM_12920
OrganismiMacaca fascicularis (Crab-eating macaque) (Cynomolgus monkey)
Taxonomic identifieri9541 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniCercopithecidaeCercopithecinaeMacaca
Proteomesi
  • UP000009130 Componenti: Chromosome 3

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 35By similarityAdd BLAST35
ChainiPRO_000001209136 – 491Hyaluronidase PH-20Add BLAST456
PropeptideiPRO_0000012092492 – 510Removed in mature formSequence analysisAdd BLAST19

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi60 ↔ 351By similarity
Glycosylationi82N-linked (GlcNAc...)Sequence analysis1
Glycosylationi166N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi224 ↔ 238By similarity
Glycosylationi235N-linked (GlcNAc...)Sequence analysis1
Glycosylationi254N-linked (GlcNAc...)Sequence analysis1
Glycosylationi368N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi376 ↔ 387By similarity
Disulfide bondi381 ↔ 435By similarity
Glycosylationi393N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi437 ↔ 464By similarity
Glycosylationi440N-linked (GlcNAc...)Sequence analysis1
Glycosylationi484N-linked (GlcNAc...)Sequence analysis1
Lipidationi491GPI-anchor amidated serineSequence analysis1

Keywords - PTMi

Disulfide bond, Glycoprotein, GPI-anchor, Lipoprotein

Expressioni

Tissue specificityi

Testis.

Structurei

3D structure databases

ProteinModelPortaliP38568.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the glycosyl hydrolase 56 family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

HOVERGENiHBG052053.

Family and domain databases

Gene3Di3.20.20.70. 1 hit.
InterProiIPR013785. Aldolase_TIM.
IPR017853. Glycoside_hydrolase_SF.
IPR018155. Hyaluronidase.
IPR001439. Hyaluronidase_PH20.
[Graphical view]
PANTHERiPTHR11769. PTHR11769. 1 hit.
PfamiPF01630. Glyco_hydro_56. 1 hit.
[Graphical view]
PIRSFiPIRSF038193. Hyaluronidase. 1 hit.
PIRSF500773. Hyaluronidase_PH20_Hyal5. 1 hit.
PRINTSiPR00846. GLHYDRLASE56.
SUPFAMiSSF51445. SSF51445. 1 hit.

Sequences (2)i

Sequence statusi: Complete.

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

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: P38568-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MGVLKFKHIF FRSFVKSSGV SQIVFTFLLI PCCLTLNFRA PPIIPNVPFL
60 70 80 90 100
WAWNAPSEFC LGKFNEPLDM SLFTLMGSPR INVTGQGVTI FYVDRLGYYP
110 120 130 140 150
YIDLTTGVTV HGGIPQKVSL QDHLDKSKQD ILFYMPVDNL GMAVIDWEEW
160 170 180 190 200
RPTWARNWKP KDVYKNRSIE LVQQQNVQLS LPQATDKAKQ EFEKAGKDFM
210 220 230 240 250
LETIKLGRSL RPNHLWGYYL FPDCYNHHYR KPGYNGSCFD VEIKRNDDLS
260 270 280 290 300
WLWNESTALY PSIYLNTQQS VVVATLYVRN RVREAIRVSK IPDAKNPLPV
310 320 330 340 350
FVYARLVFTD QVLKFLSREE LVSTLGETVA LGASGIVIWG SLSITRSMKS
360 370 380 390 400
CLLLDTYMET ILNPYIINVT LAAKMCSQVL CQEQGVCIRK DWNSSDYLHL
410 420 430 440 450
NPDNFDIRLE KGGKFTVHGK PTVEDLEEFS EKFYCSCYTN LSCKEKADVK
460 470 480 490 500
DTDAVDVCIA DGVCIDASLK PPVETEGSPP IFYNTSSSTV STTMFIVNIL
510
FLIISSVASL
Length:510
Mass (Da):57,935
Last modified:October 1, 1994 - v1
Checksum:iD50EE36C67CF1BBF
GO
Isoform 2 (identifier: P38568-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     497-510: VNILFLIISSVASL → WRLEVWDQGISRIGFF

Note: No experimental confirmation available.
Show »
Length:512
Mass (Da):58,455
Checksum:iBC638EE841D2485F
GO

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_046430497 – 510VNILF…SVASL → WRLEVWDQGISRIGFF in isoform 2. CuratedAdd BLAST14

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L13780 mRNA. No translation available.
CM001278 Genomic DNA. Translation: EHH52472.1.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L13780 mRNA. No translation available.
CM001278 Genomic DNA. Translation: EHH52472.1.

3D structure databases

ProteinModelPortaliP38568.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

CAZyiGH56. Glycoside Hydrolase Family 56.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

HOVERGENiHBG052053.

Family and domain databases

Gene3Di3.20.20.70. 1 hit.
InterProiIPR013785. Aldolase_TIM.
IPR017853. Glycoside_hydrolase_SF.
IPR018155. Hyaluronidase.
IPR001439. Hyaluronidase_PH20.
[Graphical view]
PANTHERiPTHR11769. PTHR11769. 1 hit.
PfamiPF01630. Glyco_hydro_56. 1 hit.
[Graphical view]
PIRSFiPIRSF038193. Hyaluronidase. 1 hit.
PIRSF500773. Hyaluronidase_PH20_Hyal5. 1 hit.
PRINTSiPR00846. GLHYDRLASE56.
SUPFAMiSSF51445. SSF51445. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiHYALP_MACFA
AccessioniPrimary (citable) accession number: P38568
Secondary accession number(s): G7P0K2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1994
Last sequence update: October 1, 1994
Last modified: January 7, 2015
This is version 87 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, Reference proteome

Documents

  1. Glycosyl hydrolases
    Classification of glycosyl hydrolase families and list of entries
  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.