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P35750

- CAN1_PIG

UniProt

P35750 - CAN1_PIG

Protein

Calpain-1 catalytic subunit

Gene

CAPN1

Organism
Sus scrofa (Pig)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 125 (01 Oct 2014)
      Sequence version 3 (11 Jan 2001)
      Previous versions | rss
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    Functioni

    Calcium-regulated non-lysosomal thiol-protease which catalyze limited proteolysis of substrates involved in cytoskeletal remodeling and signal transduction.

    Catalytic activityi

    Broad endopeptidase specificity.

    Cofactori

    Binds 4 calcium ions.By similarity

    Enzyme regulationi

    Activated by micromolar concentrations of calcium and inhibited by calpastatin.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sitei15 – 162Cleavage; for 78 kDa formBy similarity
    Sitei27 – 282Cleavage; for 75 kDa formBy similarity
    Active sitei115 – 1151By similarity
    Active sitei272 – 2721By similarity
    Active sitei296 – 2961By similarity

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Calcium bindingi99 – 10681PROSITE-ProRule annotation
    Calcium bindingi302 – 333322PROSITE-ProRule annotationAdd
    BLAST
    Calcium bindingi598 – 609123PROSITE-ProRule annotationAdd
    BLAST
    Calcium bindingi628 – 639124PROSITE-ProRule annotationAdd
    BLAST

    GO - Molecular functioni

    1. calcium-dependent cysteine-type endopeptidase activity Source: UniProtKB
    2. calcium ion binding Source: InterPro

    GO - Biological processi

    1. proteolysis Source: UniProtKB
    2. receptor catabolic process Source: Ensembl

    Keywords - Molecular functioni

    Hydrolase, Protease, Thiol protease

    Keywords - Ligandi

    Calcium, Metal-binding

    Enzyme and pathway databases

    BRENDAi3.4.22.52. 6170.
    ReactomeiREACT_227832. Degradation of the extracellular matrix.

    Protein family/group databases

    MEROPSiC02.001.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Calpain-1 catalytic subunit (EC:3.4.22.52)
    Alternative name(s):
    Calcium-activated neutral proteinase 1
    Short name:
    CANP 1
    Calpain mu-type
    Calpain-1 large subunit
    Micromolar-calpain
    Short name:
    muCANP
    Gene namesi
    Name:CAPN1
    OrganismiSus scrofa (Pig)
    Taxonomic identifieri9823 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaSuinaSuidaeSus
    ProteomesiUP000008227: Chromosome 2

    Subcellular locationi

    Cytoplasm By similarity. Cell membrane By similarity
    Note: Translocates to the plasma membrane upon Ca2+ binding.By similarity

    GO - Cellular componenti

    1. cytoplasm Source: RefGenome
    2. plasma membrane Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cell membrane, Cytoplasm, Membrane

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11RemovedBy similarity
    Chaini2 – 714713Calpain-1 catalytic subunitPRO_0000207697Add
    BLAST

    Post-translational modificationi

    Undergoes calcium-induced successive autoproteolytic cleavages that generate a membrane-bound 78 kDa active form and an intracellular 75 kDa active form. Calpastatin reduces with high efficiency the transition from 78 kDa to 75 kDa calpain forms By similarity.By similarity

    Keywords - PTMi

    Autocatalytic cleavage

    Proteomic databases

    PaxDbiP35750.
    PRIDEiP35750.

    Expressioni

    Tissue specificityi

    Ubiquitous.

    Interactioni

    Subunit structurei

    Forms a heterodimer with a small (regulatory) subunit (CAPNS1).

    Structurei

    3D structure databases

    ProteinModelPortaliP35750.
    SMRiP35750. Positions 13-713.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini55 – 354300Calpain catalyticPROSITE-ProRule annotationAdd
    BLAST
    Domaini585 – 61834EF-hand 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini615 – 65036EF-hand 2PROSITE-ProRule annotationAdd
    BLAST
    Domaini680 – 71435EF-hand 3PROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni355 – 526172Domain IIIAdd
    BLAST
    Regioni527 – 54216LinkerAdd
    BLAST
    Regioni543 – 713171Domain IVAdd
    BLAST

    Sequence similaritiesi

    Belongs to the peptidase C2 family.Curated
    Contains 1 calpain catalytic domain.PROSITE-ProRule annotation
    Contains 3 EF-hand domains.PROSITE-ProRule annotation

    Keywords - Domaini

    Repeat

    Phylogenomic databases

    eggNOGiNOG327523.
    GeneTreeiENSGT00750000117643.
    HOGENOMiHOG000232035.
    HOVERGENiHBG012645.
    KOiK01367.
    OMAiPQSLGYK.
    OrthoDBiEOG7RV9FM.
    TreeFamiTF314748.

    Family and domain databases

    Gene3Di1.10.238.10. 1 hit.
    InterProiIPR022684. Calpain_cysteine_protease.
    IPR022682. Calpain_domain_III.
    IPR022683. Calpain_III.
    IPR011992. EF-hand-dom_pair.
    IPR018247. EF_Hand_1_Ca_BS.
    IPR002048. EF_hand_dom.
    IPR000169. Pept_cys_AS.
    IPR001300. Peptidase_C2_calpain_cat.
    [Graphical view]
    PfamiPF01067. Calpain_III. 1 hit.
    PF13405. EF-hand_6. 1 hit.
    PF00648. Peptidase_C2. 1 hit.
    [Graphical view]
    PRINTSiPR00704. CALPAIN.
    SMARTiSM00720. calpain_III. 1 hit.
    SM00230. CysPc. 1 hit.
    SM00054. EFh. 3 hits.
    [Graphical view]
    SUPFAMiSSF49758. SSF49758. 1 hit.
    PROSITEiPS50203. CALPAIN_CAT. 1 hit.
    PS00018. EF_HAND_1. 2 hits.
    PS50222. EF_HAND_2. 3 hits.
    PS00139. THIOL_PROTEASE_CYS. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    P35750-1 [UniParc]FASTAAdd to Basket

    « Hide

    MAEEVITPVY CTGVSAQVQK LRAKELGLGR HENAIKYLGQ DYEQLRAHCL    50
    QSGSLFRDEA FPPVPQSLGF KELGPNSSKT YGVKWKRPTE LFSNPQFIVD 100
    GATRTDICQG ALGDCWLLAA IASLTLNDTL LHRVVPHGQS FQNGYAGIFH 150
    FQLWQFGEWV DVVVDDLLPT KDGKLVFVHS AQGNEFWSAL LEKAYAKVNG 200
    SYEALSGGST SEGFEDFTGG VTEWYELRKA PSDLYSIILK ALERGSLLGC 250
    SIDISSVLDM EAVTFKKLVK GHAYSVTGAK QVNYQGQMVN LIRMRNPWGE 300
    VEWTGAWSDG SSEWNGVDPY QRDQLRVRME DGEFWMSFRD FLREFTRLEI 350
    CNLTPDALKS QRVRNWNTTL YEGTWRRGST AGGCRNYPAT FWVNPQFKIR 400
    LEETDDPEDD YGGRESGCSF VLALMQKHRR RERRFGRDME TIGFAVYEVP 450
    PELVGQPVHL KRDFFLANAS RARSEQFINL REVSTRFRLP PGEYVVVPST 500
    FEPNKEGDFV LRFFSEKKAG TQELDDQVQA ILPDEQVLSE EEIDENFKAL 550
    FRQLAGEDME ISVRELRTIL NRIISKHKDL RTKGFSLESC RSMVNLMDRD 600
    GNGKLGLVEF NILWNRIRNY LSIFRKFDLD KSGSMSAYEM RMAIESAGFK 650
    LNKKLFELII TRYSEPDLAV DFDNFVCCLV RLETMFRFFK TLDTDLDGVV 700
    TFDLFKWLQL TMFA 714
    Length:714
    Mass (Da):81,739
    Last modified:January 11, 2001 - v3
    Checksum:i0BB31DE4FC56363A
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti528 – 5281V → I in AAA65125. (PubMed:8312396)Curated
    Sequence conflicti531 – 5311I → N in AAA65125. (PubMed:8312396)Curated
    Sequence conflicti541 – 5411E → G in AAA65125. (PubMed:8312396)Curated
    Sequence conflicti622 – 6221S → A in AAA65125. (PubMed:8312396)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF263610 mRNA. Translation: AAF73444.1.
    F14611 mRNA. Translation: CAA23154.1.
    U01180 mRNA. Translation: AAA65125.1.
    RefSeqiXP_005660758.1. XM_005660701.1.
    XP_005660759.1. XM_005660702.1.
    UniGeneiSsc.42541.

    Genome annotation databases

    EnsembliENSSSCT00000014210; ENSSSCP00000013824; ENSSSCG00000012999.
    GeneIDi397027.
    KEGGissc:397027.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF263610 mRNA. Translation: AAF73444.1 .
    F14611 mRNA. Translation: CAA23154.1 .
    U01180 mRNA. Translation: AAA65125.1 .
    RefSeqi XP_005660758.1. XM_005660701.1.
    XP_005660759.1. XM_005660702.1.
    UniGenei Ssc.42541.

    3D structure databases

    ProteinModelPortali P35750.
    SMRi P35750. Positions 13-713.
    ModBasei Search...
    MobiDBi Search...

    Chemistry

    BindingDBi P35750.
    ChEMBLi CHEMBL4062.

    Protein family/group databases

    MEROPSi C02.001.

    Proteomic databases

    PaxDbi P35750.
    PRIDEi P35750.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSSSCT00000014210 ; ENSSSCP00000013824 ; ENSSSCG00000012999 .
    GeneIDi 397027.
    KEGGi ssc:397027.

    Organism-specific databases

    CTDi 823.

    Phylogenomic databases

    eggNOGi NOG327523.
    GeneTreei ENSGT00750000117643.
    HOGENOMi HOG000232035.
    HOVERGENi HBG012645.
    KOi K01367.
    OMAi PQSLGYK.
    OrthoDBi EOG7RV9FM.
    TreeFami TF314748.

    Enzyme and pathway databases

    BRENDAi 3.4.22.52. 6170.
    Reactomei REACT_227832. Degradation of the extracellular matrix.

    Family and domain databases

    Gene3Di 1.10.238.10. 1 hit.
    InterProi IPR022684. Calpain_cysteine_protease.
    IPR022682. Calpain_domain_III.
    IPR022683. Calpain_III.
    IPR011992. EF-hand-dom_pair.
    IPR018247. EF_Hand_1_Ca_BS.
    IPR002048. EF_hand_dom.
    IPR000169. Pept_cys_AS.
    IPR001300. Peptidase_C2_calpain_cat.
    [Graphical view ]
    Pfami PF01067. Calpain_III. 1 hit.
    PF13405. EF-hand_6. 1 hit.
    PF00648. Peptidase_C2. 1 hit.
    [Graphical view ]
    PRINTSi PR00704. CALPAIN.
    SMARTi SM00720. calpain_III. 1 hit.
    SM00230. CysPc. 1 hit.
    SM00054. EFh. 3 hits.
    [Graphical view ]
    SUPFAMi SSF49758. SSF49758. 1 hit.
    PROSITEi PS50203. CALPAIN_CAT. 1 hit.
    PS00018. EF_HAND_1. 2 hits.
    PS50222. EF_HAND_2. 3 hits.
    PS00139. THIOL_PROTEASE_CYS. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Rapid communication: nucleotide sequences of two isoforms of porcine micromolar calcium-activated neutral protease 1 cDNA."
      Smith T.P.L., Simmen F.A., Zhao G., Vallet J.L.
      J. Anim. Sci. 79:552-553(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    2. "Evaluation and characterization of a porcine small intestine cDNA library: analysis of 839 clones."
      Winteroe A.K., Fredholm M., Davies W.
      Mamm. Genome 7:509-517(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 326-415.
      Tissue: Small intestine.
    3. "Cloning the partial cDNAs of mu-calpain and m-calpain from porcine skeletal muscle."
      Sun W., Ji S.Q., Ebert P.J., Bidwell C.A., Hancock D.L.
      Biochimie 75:931-936(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 528-623.
      Tissue: Skeletal muscle.

    Entry informationi

    Entry nameiCAN1_PIG
    AccessioniPrimary (citable) accession number: P35750
    Secondary accession number(s): Q29600, Q9N0M6
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: June 1, 1994
    Last sequence update: January 11, 2001
    Last modified: October 1, 2014
    This is version 125 of the entry and version 3 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