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Protein

Granzyme M

Gene

Gzmm

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Cleaves peptide substrates after methionine, leucine, and norleucine. Physiological substrates include EZR, alpha-tubulins and the apoptosis inhibitor BIRC5/Survivin. Promotes caspase activation and subsequent apoptosis of target cells (By similarity).By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei61 – 611Charge relay systemBy similarity
Active sitei107 – 1071Charge relay systemBy similarity
Active sitei204 – 2041Charge relay systemBy similarity

GO - Molecular functioni

  1. serine-type endopeptidase activity Source: InterPro
  2. serine-type peptidase activity Source: RGD

GO - Biological processi

  1. apoptotic process Source: UniProtKB-KW
  2. cytolysis Source: UniProtKB-KW
  3. innate immune response Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protease, Serine protease

Keywords - Biological processi

Apoptosis, Cytolysis, Immunity, Innate immunity

Enzyme and pathway databases

BRENDAi3.4.21.B2. 5301.

Protein family/group databases

MEROPSiS01.139.

Names & Taxonomyi

Protein namesi
Recommended name:
Granzyme M (EC:3.4.21.-)
Alternative name(s):
Met-ase
Natural killer cell granular protease
RNK-Met-1
Gene namesi
Name:Gzmm
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
ProteomesiUP000002494 Componenti: Unplaced

Organism-specific databases

RGDi620022. Gzmm.

Subcellular locationi

Secreted. Cytoplasmic granule
Note: Granules of large granular lymphocytes.

GO - Cellular componenti

  1. extracellular region Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Propeptidei? – 20Activation peptide1 PublicationPRO_0000027423
Signal peptidei‹1 – ?Sequence Analysis
Chaini21 – 258238Granzyme MPRO_0000027424Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi46 ↔ 62PROSITE-ProRule annotation
Disulfide bondi142 ↔ 210PROSITE-ProRule annotation
Disulfide bondi173 ↔ 189PROSITE-ProRule annotation
Glycosylationi174 – 1741N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi200 ↔ 226PROSITE-ProRule annotation
Glycosylationi225 – 2251N-linked (GlcNAc...)Sequence Analysis

Keywords - PTMi

Disulfide bond, Glycoprotein, Zymogen

Proteomic databases

PRIDEiQ03238.

Expressioni

Gene expression databases

GenevestigatoriQ03238.

Interactioni

Protein-protein interaction databases

IntActiQ03238. 1 interaction.
STRINGi10116.ENSRNOP00000011086.

Structurei

3D structure databases

ProteinModelPortaliQ03238.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini21 – 250230Peptidase S1PROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the peptidase S1 family. Granzyme subfamily.PROSITE-ProRule annotation
Contains 1 peptidase S1 domain.PROSITE-ProRule annotation

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiCOG5640.
HOGENOMiHOG000251820.
HOVERGENiHBG013304.
InParanoidiQ03238.
PhylomeDBiQ03238.

Family and domain databases

InterProiIPR001254. Peptidase_S1.
IPR018114. Peptidase_S1_AS.
IPR001314. Peptidase_S1A.
IPR009003. Trypsin-like_Pept_dom.
[Graphical view]
PfamiPF00089. Trypsin. 1 hit.
[Graphical view]
PRINTSiPR00722. CHYMOTRYPSIN.
SMARTiSM00020. Tryp_SPc. 1 hit.
[Graphical view]
SUPFAMiSSF50494. SSF50494. 1 hit.
PROSITEiPS50240. TRYPSIN_DOM. 1 hit.
PS00134. TRYPSIN_HIS. 1 hit.
PS00135. TRYPSIN_SER. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Fragment.

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

Q03238-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
LLLLLALKTL WAVGNRFEAQ IIGGREAVPH SRPYMVSLQN TKSHMCGGVL
60 70 80 90 100
VHQKWVLTAA HCLSEPLQQL KLVFGLHSLH DPQDPGLTFY IKQAIKHPGY
110 120 130 140 150
NLKYENDLAL LKLDGRVKPS KNVKPLALPR KPRDKPAEGS RCSTAGWGIT
160 170 180 190 200
HQRGQLAKSL QELDLRLLDT RMCNNSRFWN GVLTDSMLCL KAGAKGQAPC
210 220 230 240 250
KGDSGGPLVC GKGKVDGILS FSSKNCTDIF KPTVATAVAP YSSWIRKVIG

RWSPQPLT
Length:258
Mass (Da):28,339
Last modified:June 1, 1994 - v1
Checksum:iB89DC10EF54DF495
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Non-terminal residuei1 – 11

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L05175 mRNA. Translation: AAA42056.1.
PIRiA45161.
UniGeneiRn.9838.

Genome annotation databases

UCSCiRGD:620022. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L05175 mRNA. Translation: AAA42056.1.
PIRiA45161.
UniGeneiRn.9838.

3D structure databases

ProteinModelPortaliQ03238.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ03238. 1 interaction.
STRINGi10116.ENSRNOP00000011086.

Protein family/group databases

MEROPSiS01.139.

Proteomic databases

PRIDEiQ03238.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

UCSCiRGD:620022. rat.

Organism-specific databases

RGDi620022. Gzmm.

Phylogenomic databases

eggNOGiCOG5640.
HOGENOMiHOG000251820.
HOVERGENiHBG013304.
InParanoidiQ03238.
PhylomeDBiQ03238.

Enzyme and pathway databases

BRENDAi3.4.21.B2. 5301.

Miscellaneous databases

PROiQ03238.

Gene expression databases

GenevestigatoriQ03238.

Family and domain databases

InterProiIPR001254. Peptidase_S1.
IPR018114. Peptidase_S1_AS.
IPR001314. Peptidase_S1A.
IPR009003. Trypsin-like_Pept_dom.
[Graphical view]
PfamiPF00089. Trypsin. 1 hit.
[Graphical view]
PRINTSiPR00722. CHYMOTRYPSIN.
SMARTiSM00020. Tryp_SPc. 1 hit.
[Graphical view]
SUPFAMiSSF50494. SSF50494. 1 hit.
PROSITEiPS50240. TRYPSIN_DOM. 1 hit.
PS00134. TRYPSIN_HIS. 1 hit.
PS00135. TRYPSIN_SER. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "Purification and cloning of a novel serine protease, RNK-Met-1, from the granules of a rat natural killer cell leukemia."
    Smyth M.J., Wiltrout T., Trapani J.A., Ottaway K.S., Sowder R., Henderson L.E., Kam C.-M., Powers J.C., Young H.A., Sayers T.J.
    J. Biol. Chem. 267:24418-24425(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 21-44.

Entry informationi

Entry nameiGRAM_RAT
AccessioniPrimary (citable) accession number: Q03238
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 1, 1994
Last sequence update: June 1, 1994
Last modified: April 1, 2015
This is version 103 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. Peptidase families
    Classification of peptidase families and list of entries
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.