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Protein

Anionic trypsin

Gene
N/A
Organism
Canis familiaris (Dog) (Canis lupus familiaris)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at transcript leveli

Functioni

Catalytic activityi

Preferential cleavage: Arg-|-Xaa, Lys-|-Xaa.

Cofactori

Ca2+By similarityNote: Binds 1 Ca2+ ion per subunit.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei63 – 631Charge relay systemBy similarity
Metal bindingi75 – 751CalciumBy similarity
Metal bindingi77 – 771Calcium; via carbonyl oxygenBy similarity
Metal bindingi80 – 801Calcium; via carbonyl oxygenBy similarity
Metal bindingi85 – 851CalciumBy similarity
Active sitei107 – 1071Charge relay systemBy similarity
Sitei194 – 1941Required for specificityBy similarity
Active sitei200 – 2001Charge relay systemBy similarity

GO - Molecular functioni

  1. calcium ion binding Source: UniProtKB
  2. serine-type endopeptidase activity Source: UniProtKB

GO - Biological processi

  1. collagen catabolic process Source: UniProtKB
  2. digestion Source: UniProtKB-KW
  3. proteolysis Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protease, Serine protease

Keywords - Biological processi

Digestion

Keywords - Ligandi

Calcium, Metal-binding

Enzyme and pathway databases

ReactomeiREACT_174078. Cobalamin (Cbl, vitamin B12) transport and metabolism.
REACT_182220. Activation of Matrix Metalloproteinases.

Protein family/group databases

MEROPSiS01.120.

Names & Taxonomyi

Protein namesi
Recommended name:
Anionic trypsin (EC:3.4.21.4)
OrganismiCanis familiaris (Dog) (Canis lupus familiaris)
Taxonomic identifieri9615 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCarnivoraCaniformiaCanidaeCanis
ProteomesiUP000002254: Chromosome 16

Subcellular locationi

GO - Cellular componenti

  1. extracellular region Source: UniProtKB
  2. extracellular space Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1515Add
BLAST
Propeptidei16 – 238Activation peptidePRO_0000028193
Chaini24 – 247224Anionic trypsinPRO_0000028194Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi30 ↔ 160PROSITE-ProRule annotation
Disulfide bondi48 ↔ 64PROSITE-ProRule annotation
Disulfide bondi132 ↔ 233PROSITE-ProRule annotation
Disulfide bondi139 ↔ 206PROSITE-ProRule annotation
Disulfide bondi171 ↔ 185PROSITE-ProRule annotation
Disulfide bondi196 ↔ 220PROSITE-ProRule annotation

Keywords - PTMi

Disulfide bond, Zymogen

Proteomic databases

PaxDbiP06872.
PRIDEiP06872.

Structurei

3D structure databases

ProteinModelPortaliP06872.
SMRiP06872. Positions 24-246.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini24 – 244221Peptidase S1PROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

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

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiCOG5640.
GeneTreeiENSGT00760000118862.
HOGENOMiHOG000251820.
HOVERGENiHBG013304.
InParanoidiP06872.
KOiK01312.
OMAiHPKYSSW.
OrthoDBiEOG75B84T.
TreeFamiTF331065.

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: Complete.

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

P06872-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MNPLLILAFL GAAVATPTDD DDKIVGGYTC EENSVPYQVS LNAGYHFCGG
60 70 80 90 100
SLISDQWVVS AAHCYKSRIQ VRLGEYNIDV LEGNEQFINS AKVIRHPNYN
110 120 130 140 150
SWILDNDIML IKLSSPAVLN ARVATISLPR ACAAPGTQCL ISGWGNTLSS
160 170 180 190 200
GTNYPELLQC LDAPILTQAQ CEASYPGQIT ENMICAGFLE GGKDSCQGDS
210 220 230 240
GGPVVCNGEL QGIVSWGYGC AQKNKPGVYT KVCNFVDWIQ STIAANS
Length:247
Mass (Da):26,423
Last modified:January 1, 1988 - v1
Checksum:i374E9D31D6DB8EAF
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M11589 mRNA. Translation: AAA30899.1.
PIRiA26273. TRDG.
RefSeqiXP_003432104.1. XM_003432056.2.

Genome annotation databases

EnsembliENSCAFT00000022998; ENSCAFP00000021363; ENSCAFG00000014481.
GeneIDi100686744.
KEGGicfa:100686744.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M11589 mRNA. Translation: AAA30899.1.
PIRiA26273. TRDG.
RefSeqiXP_003432104.1. XM_003432056.2.

3D structure databases

ProteinModelPortaliP06872.
SMRiP06872. Positions 24-246.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

MEROPSiS01.120.

Proteomic databases

PaxDbiP06872.
PRIDEiP06872.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSCAFT00000022998; ENSCAFP00000021363; ENSCAFG00000014481.
GeneIDi100686744.
KEGGicfa:100686744.

Phylogenomic databases

eggNOGiCOG5640.
GeneTreeiENSGT00760000118862.
HOGENOMiHOG000251820.
HOVERGENiHBG013304.
InParanoidiP06872.
KOiK01312.
OMAiHPKYSSW.
OrthoDBiEOG75B84T.
TreeFamiTF331065.

Enzyme and pathway databases

ReactomeiREACT_174078. Cobalamin (Cbl, vitamin B12) transport and metabolism.
REACT_182220. Activation of Matrix Metalloproteinases.

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. "Differential regulation of trypsinogen mRNA translation: full-length mRNA sequences encoding two oppositely charged trypsinogen isoenzymes in the dog pancreas."
    Pinsky S.D., Laforge K.S., Scheele G.
    Mol. Cell. Biol. 5:2669-2676(1985) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].

Entry informationi

Entry nameiTRY2_CANFA
AccessioniPrimary (citable) accession number: P06872
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 1, 1988
Last sequence update: January 1, 1988
Last modified: January 7, 2015
This is version 112 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. 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.