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P38566

- HYALP_RABIT

UniProt

P38566 - HYALP_RABIT

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Protein

Hyaluronidase PH-20

Gene

SPAM1

Organism
Oryctolagus cuniculus (Rabbit)
Status
Reviewed - 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)LengthDescriptionGraphical viewFeature identifierActions
Active sitei148 – 1481Proton donorBy similarity

GO - Molecular functioni

  1. hyalurononglucosaminidase activity Source: UniProtKB-EC

GO - Biological processi

  1. carbohydrate metabolic process Source: InterPro
  2. cell adhesion Source: UniProtKB-KW
  3. fusion of sperm to egg plasma membrane Source: InterPro
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
OrganismiOryctolagus cuniculus (Rabbit)
Taxonomic identifieri9986 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresLagomorphaLeporidaeOryctolagus
ProteomesiUP000001811: Unplaced

Subcellular locationi

GO - Cellular componenti

  1. anchored component of membrane Source: UniProtKB-KW
  2. plasma membrane Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Propeptidei? – 545Removed in mature formSequence AnalysisPRO_0000012096
Signal peptidei1 – 3535By similarityAdd
BLAST
Chaini36 – ?Hyaluronidase PH-20PRO_0000012095

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi60 ↔ 355By similarity
Glycosylationi82 – 821N-linked (GlcNAc...)Sequence Analysis
Glycosylationi180 – 1801N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi224 ↔ 239By similarity
Glycosylationi372 – 3721N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi380 ↔ 391By similarity
Disulfide bondi385 ↔ 439By similarity
Disulfide bondi441 ↔ 468By similarity

Keywords - PTMi

Disulfide bond, Glycoprotein, GPI-anchor, Lipoprotein

Expressioni

Tissue specificityi

Testis.

Structurei

3D structure databases

ProteinModelPortaliP38566.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the glycosyl hydrolase 56 family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

HOVERGENiHBG052053.
InParanoidiP38566.

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.

Sequencei

Sequence statusi: Complete.

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

P38566 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MGVLKFKHIF FGSAVELSGV FQIVFIFLLI PCCLTANFRA PPVIPNVPFL
60 70 80 90 100
WAWNAPTEFC LGKSGEPLDM SLFSLFGSPR KNKTGQGITI FYVDRLGYYP
110 120 130 140 150
YIDPHTGAIV HGRIPQLGPL QQHLTKLRQE ILYYMPKDNV GLAVIDWEEW
160 170 180 190 200
LPTWLRNWKP KDIYRIKSIE LVKSQHPQYN HSYATEKAKR DFEKAGKDFM
210 220 230 240 250
EETLKLGRLL RPNHLWGYYL FPDCYNHHYD KPNLYKGSCF DIEKKRNDDL
260 270 280 290 300
SWLWKESTAL FPSVYLTSRA RSATALSKLY VVRNRVHEAI RVSKIPDDKS
310 320 330 340 350
PLPNFVYTRL VFTDQIFQFL SHHDLVYTIG EIVALGASGI VVWGSQSLAR
360 370 380 390 400
SMKSCLHLDN YMKTILNPYL INVTLAAKMC NQVLCQEQGV CTRKNWNPND
410 420 430 440 450
YLHLNPGNFA IQLGSNGTYK VDGKPTLTDL EQFSKNFQCS CYTNLNCKER
460 470 480 490 500
TDMNNVRTVN VCAVENVCID TNVGPQAVTY APKEKKDVAH ILSNTTSINS
510 520 530 540
STTMSLPFPR KHVSGCLLVL CMYSQYLNIC YRLVAIGIQH GYYLK
Length:545
Mass (Da):62,412
Last modified:October 1, 1996 - v2
Checksum:i125AF314FE05AEB4
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U09183 mRNA. Translation: AAA88913.1.
RefSeqiNP_001076141.1. NM_001082672.1.
UniGeneiOcu.2048.

Genome annotation databases

GeneIDi100009391.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U09183 mRNA. Translation: AAA88913.1 .
RefSeqi NP_001076141.1. NM_001082672.1.
UniGenei Ocu.2048.

3D structure databases

ProteinModelPortali P38566.
ModBasei Search...
MobiDBi Search...

Protein family/group databases

CAZyi GH56. Glycoside Hydrolase Family 56.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 100009391.

Organism-specific databases

CTDi 6677.

Phylogenomic databases

HOVERGENi HBG052053.
InParanoidi P38566.

Family and domain databases

Gene3Di 3.20.20.70. 1 hit.
InterProi IPR013785. Aldolase_TIM.
IPR017853. Glycoside_hydrolase_SF.
IPR018155. Hyaluronidase.
IPR001439. Hyaluronidase_PH20.
[Graphical view ]
PANTHERi PTHR11769. PTHR11769. 1 hit.
Pfami PF01630. Glyco_hydro_56. 1 hit.
[Graphical view ]
PIRSFi PIRSF038193. Hyaluronidase. 1 hit.
PIRSF500773. Hyaluronidase_PH20_Hyal5. 1 hit.
PRINTSi PR00846. GLHYDRLASE56.
SUPFAMi SSF51445. SSF51445. 1 hit.
ProtoNeti Search...

Publicationsi

  1. "The nucleic acid sequence of rabbit PH-20 cDNA."
    Andrews J.B., Holland M.K.
    Submitted (MAY-1994) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Testis.

Entry informationi

Entry nameiHYALP_RABIT
AccessioniPrimary (citable) accession number: P38566
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1994
Last sequence update: October 1, 1996
Last modified: October 29, 2014
This is version 90 of the entry and version 2 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

External Data

Dasty 3