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P28843

- DPP4_MOUSE

UniProt

P28843 - DPP4_MOUSE

Protein

Dipeptidyl peptidase 4

Gene

Dpp4

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 138 (01 Oct 2014)
      Sequence version 3 (01 Feb 1996)
      Previous versions | rss
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    Functioni

    Cell surface glycoprotein receptor involved in the costimulatory signal essential for T-cell receptor (TCR)-mediated T-cell activation. Acts as a positive regulator of T-cell coactivation, by binding at least ADA, CAV1, IGF2R, and PTPRC. Its binding to CAV1 and CARD11 induces T-cell proliferation and NF-kappa-B activation in a T-cell receptor/CD3-dependent manner. Its interaction with ADA also regulates lymphocyte-epithelial cell adhesion. In association with FAP is involved in the pericellular proteolysis of the extracellular matrix (ECM), the migration and invasion of endothelial cells into the ECM. May be involved in the promotion of lymphatic endothelial cells adhesion, migration and tube formation. When overexpressed, enhanced cell proliferation, a process inhibited by GPC3. Acts also as a serine exopeptidase with a dipeptidyl peptidase activity that regulates various physiological processes by cleaving peptides in the circulation, including many chemokines, mitogenic growth factors, neuropeptides and peptide hormones. Removes N-terminal dipeptides sequentially from polypeptides having unsubstituted N-termini provided that the penultimate residue is proline By similarity.By similarity

    Catalytic activityi

    Release of an N-terminal dipeptide, Xaa-Yaa-|-Zaa-, from a polypeptide, preferentially when Yaa is Pro, provided Zaa is neither Pro nor hydroxyproline.PROSITE-ProRule annotation

    Enzyme regulationi

    Inhibited by GPC3 and diprotin A.By similarity

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei624 – 6241Charge relay systemPROSITE-ProRule annotation
    Active sitei702 – 7021Charge relay systemPROSITE-ProRule annotation
    Active sitei734 – 7341Charge relay systemPROSITE-ProRule annotation

    GO - Molecular functioni

    1. dipeptidyl-peptidase activity Source: UniProtKB
    2. protease binding Source: UniProtKB
    3. protein homodimerization activity Source: UniProtKB
    4. receptor binding Source: UniProtKB
    5. serine-type endopeptidase activity Source: InterPro

    GO - Biological processi

    1. cell adhesion Source: UniProtKB-KW
    2. endothelial cell migration Source: UniProtKB
    3. negative regulation of extracellular matrix disassembly Source: UniProtKB
    4. positive regulation of cell proliferation Source: UniProtKB
    5. regulation of cell-cell adhesion mediated by integrin Source: Ensembl
    6. response to hypoxia Source: Ensembl
    7. T cell activation Source: Ensembl
    8. T cell costimulation Source: UniProtKB

    Keywords - Molecular functioni

    Aminopeptidase, Hydrolase, Protease, Receptor, Serine protease

    Keywords - Biological processi

    Cell adhesion

    Protein family/group databases

    MEROPSiS09.003.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Dipeptidyl peptidase 4 (EC:3.4.14.5)
    Alternative name(s):
    Dipeptidyl peptidase IV
    Short name:
    DPP IV
    T-cell activation antigen CD26
    Thymocyte-activating molecule
    Short name:
    THAM
    CD_antigen: CD26
    Cleaved into the following 2 chains:
    Alternative name(s):
    Dipeptidyl peptidase IV membrane form
    Alternative name(s):
    Dipeptidyl peptidase IV soluble form
    Gene namesi
    Name:Dpp4
    Synonyms:Cd26
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 2

    Organism-specific databases

    MGIiMGI:94919. Dpp4.

    Subcellular locationi

    Chain Dipeptidyl peptidase 4 soluble form : Secreted
    Note: Detected in the serum and the seminal fluid.By similarity
    Cell membrane; Single-pass type II membrane protein. Apical cell membrane By similarity; Single-pass type II membrane protein By similarity. Cell projectioninvadopodium membrane By similarity; Single-pass type II membrane protein By similarity. Cell projectionlamellipodium membrane By similarity; Single-pass type II membrane protein By similarity. Cell junction By similarity. Membrane raft By similarity
    Note: Translocated to the apical membrane through the concerted action of N- and O-Glycans and its association with lipid microdomains containing cholesterol and sphingolipids. Redistributed to membrane rafts in T-cell in a interleukin-12-dependent activation. Its interaction with CAV1 is necessary for its translocation to membrane rafts. Colocalized with PTPRC in membrane rafts. Colocalized with FAP in invadopodia and lamellipodia of migratory activated endothelial cells in collagenous matrix. Colocalized with FAP on endothelial cells of capillary-like microvessels but not large vessels within invasive breast ductal carcinoma. Colocalized with ADA at the cell junction in lymphocyte-epithelial cell adhesion. Colocalized with IGF2R in internalized cytoplasmic vesicles adjacent to the cell surface By similarity.By similarity

    GO - Cellular componenti

    1. apical plasma membrane Source: UniProtKB-SubCell
    2. cell surface Source: UniProtKB
    3. endocytic vesicle Source: UniProtKB
    4. extracellular vesicular exosome Source: Ensembl
    5. integral component of membrane Source: UniProtKB-KW
    6. intercellular canaliculus Source: MGI
    7. invadopodium membrane Source: UniProtKB
    8. lamellipodium Source: UniProtKB
    9. lamellipodium membrane Source: UniProtKB-SubCell
    10. lysosomal membrane Source: Ensembl
    11. membrane raft Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cell junction, Cell membrane, Cell projection, Membrane, Secreted

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 760760Dipeptidyl peptidase 4 membrane formPRO_0000027215Add
    BLAST
    Chaini37 – 760724Dipeptidyl peptidase 4 soluble formBy similarityPRO_0000027216Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi83 – 831N-linked (GlcNAc...)By similarity
    Glycosylationi90 – 901N-linked (GlcNAc...)By similarity
    Glycosylationi145 – 1451N-linked (GlcNAc...); atypical1 Publication
    Glycosylationi213 – 2131N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi223 – 2231N-linked (GlcNAc...)By similarity
    Glycosylationi315 – 3151N-linked (GlcNAc...)By similarity
    Disulfide bondi322 ↔ 333By similarity
    Glycosylationi328 – 3281N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi379 ↔ 388By similarity
    Disulfide bondi438 ↔ 441By similarity
    Disulfide bondi448 ↔ 466By similarity
    Glycosylationi514 – 5141N-linked (GlcNAc...)1 Publication
    Disulfide bondi643 ↔ 756By similarity
    Glycosylationi679 – 6791N-linked (GlcNAc...)By similarity

    Post-translational modificationi

    The soluble form (Dipeptidyl peptidase 4 soluble form also named SDPP) derives from the membrane form (Dipeptidyl peptidase 4 membrane form also named MDPP) by proteolytic processing.By similarity
    N- and O-Glycosylated.By similarity
    Phosphorylated. Mannose 6-phosphate residues in the carbohydrate moiety are necessary for interaction with IGF2R in activated T-cells. Mannose 6-phosphorylation is induced during T-cell activation By similarity.By similarity

    Keywords - PTMi

    Disulfide bond, Glycoprotein

    Proteomic databases

    MaxQBiP28843.
    PaxDbiP28843.
    PRIDEiP28843.

    PTM databases

    PhosphoSiteiP28843.

    Expressioni

    Gene expression databases

    BgeeiP28843.
    CleanExiMM_DPP4.
    GenevestigatoriP28843.

    Interactioni

    Subunit structurei

    Monomer. Heterodimer with Seprase (FAP). Requires homodimerization for optimal dipeptidyl peptidase activity and T-cell costimulation. Found in a membrane raft complex, at least composed of BCL10, CARD11, DPP4 and IKBKB. Associates with collagen. Interacts with PTPRC; the interaction is enhanced in a interleukin-12-dependent manner in activated lymphocytes. Interacts (extracellular domain) with ADA; does not inhibit its dipeptidyl peptidase activity. Interacts with CAV1 (via the N-terminus); the interaction is direct. Interacts (via cytoplasmic tail) with CARD11 (via PDZ domain); its homodimerization is necessary for interaction with CARD11. Interacts with IGF2R; the interaction is direct. Interacts with GPC3 By similarity. Homodimer.By similarity

    Protein-protein interaction databases

    BioGridi199300. 1 interaction.
    IntActiP28843. 5 interactions.
    MINTiMINT-1857814.
    STRINGi10090.ENSMUSP00000044050.

    Structurei

    3D structure databases

    ProteinModelPortaliP28843.
    SMRiP28843. Positions 39-759.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini1 – 66CytoplasmicSequence Analysis
    Topological domaini29 – 760732ExtracellularSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei7 – 2822Helical; Signal-anchor for type II membrane proteinSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi295 – 466172Cys-richAdd
    BLAST

    Sequence similaritiesi

    Belongs to the peptidase S9B family. DPPIV subfamily.Curated

    Keywords - Domaini

    Signal-anchor, Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiCOG1506.
    GeneTreeiENSGT00740000115496.
    HOGENOMiHOG000231875.
    HOVERGENiHBG005527.
    InParanoidiP28843.
    KOiK01278.
    OMAiETKFWYQ.
    OrthoDBiEOG761BT2.
    PhylomeDBiP28843.
    TreeFamiTF313309.

    Family and domain databases

    Gene3Di2.140.10.30. 1 hit.
    3.40.50.1820. 1 hit.
    InterProiIPR029058. AB_hydrolase.
    IPR002471. Pept_S9_AS.
    IPR001375. Peptidase_S9.
    IPR002469. Peptidase_S9B.
    [Graphical view]
    PfamiPF00930. DPPIV_N. 1 hit.
    PF00326. Peptidase_S9. 1 hit.
    [Graphical view]
    SUPFAMiSSF53474. SSF53474. 1 hit.
    PROSITEiPS00708. PRO_ENDOPEP_SER. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    P28843-1 [UniParc]FASTAAdd to Basket

    « Hide

    MKTPWKVLLG LLGVAALVTI ITVPIVLLSK DEAAADSRRT YSLADYLKST    50
    FRVKSYSLWW VSDFEYLYKQ ENNILLLNAE HGNSSIFLEN STFESFGYHS 100
    VSPDRLFVLL EYNYVKQWRH SYTASYNIYD VNKRQLITEE KIPNNTQWIT 150
    WSPEGHKLAY VWKNDIYVKV EPHLPSHRIT STGEENVIYN GITDWVYEEE 200
    VFGAYSALWW SPNNTFLAYA QFNDTGVPLI EYSFYSDESL QYPKTVWIPY 250
    PKAGAVNPTV KFFIVNIDSL SSSSSAAPIQ IPAPASVARG DHYLCDVVWA 300
    TEERISLQWL RRIQNYSVMA ICDYDKINLT WNCPSEQQHV EMSTTGWVGR 350
    FRPAEPHFTS DGSSFYKIIS DKDGYKHICH FPKDKKDCTF ITKGAWEVIS 400
    IEALTSDYLY YISNQYKEMP GGRNLYKIQL TDHTNVKCLS CDLNPERCQY 450
    YAVSFSKEAK YYQLGCWGPG LPLYTLHRST DHKELRVLED NSALDRMLQD 500
    VQMPSKKLDF IVLNETRFWY QMILPPHFDK SKKYPLLLDV YAGPCSQKAD 550
    ASFRLNWATY LASTENIIVA SFDGRGSGYQ GDKIMHAINR RLGTLEVEDQ 600
    IEAARQFVKM GFVDSKRVAI WGWSYGGYVT SMVLGSGSGV FKCGIAVAPV 650
    SRWEYYDSVY TERYMGLPIP EDNLDHYRNS TVMSRAEHFK QVEYLLIHGT 700
    ADDNVHFQQS AQISKALVDA GVDFQAMWYT DEDHGIASST AHQHIYSHMS 750
    HFLQQCFSLH 760
    Length:760
    Mass (Da):87,437
    Last modified:February 1, 1996 - v3
    Checksum:iA5F644B46E4A3DF8
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X58384 mRNA. Translation: CAA41274.1.
    U12620
    , U12599, U12600, U12601, U12602, U12603, U12604, U12605, U12606, U12607, U12608, U12609, U12610, U12611, U12612, U12613, U12614, U12615, U12616, U12617, U12618, U12619 Genomic DNA. Translation: AAA82213.1.
    AK085370 mRNA. Translation: BAC39434.1.
    AK153939 mRNA. Translation: BAE32266.1.
    BC022183 mRNA. Translation: AAH22183.1.
    CCDSiCCDS16065.1.
    PIRiS23752.
    RefSeqiNP_001153015.1. NM_001159543.1.
    NP_034204.1. NM_010074.3.
    XP_006498753.1. XM_006498690.1.
    UniGeneiMm.1151.

    Genome annotation databases

    EnsembliENSMUST00000047812; ENSMUSP00000044050; ENSMUSG00000035000.
    GeneIDi13482.
    KEGGimmu:13482.
    UCSCiuc008jvg.2. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X58384 mRNA. Translation: CAA41274.1 .
    U12620
    , U12599 , U12600 , U12601 , U12602 , U12603 , U12604 , U12605 , U12606 , U12607 , U12608 , U12609 , U12610 , U12611 , U12612 , U12613 , U12614 , U12615 , U12616 , U12617 , U12618 , U12619 Genomic DNA. Translation: AAA82213.1 .
    AK085370 mRNA. Translation: BAC39434.1 .
    AK153939 mRNA. Translation: BAE32266.1 .
    BC022183 mRNA. Translation: AAH22183.1 .
    CCDSi CCDS16065.1.
    PIRi S23752.
    RefSeqi NP_001153015.1. NM_001159543.1.
    NP_034204.1. NM_010074.3.
    XP_006498753.1. XM_006498690.1.
    UniGenei Mm.1151.

    3D structure databases

    ProteinModelPortali P28843.
    SMRi P28843. Positions 39-759.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 199300. 1 interaction.
    IntActi P28843. 5 interactions.
    MINTi MINT-1857814.
    STRINGi 10090.ENSMUSP00000044050.

    Chemistry

    BindingDBi P28843.
    ChEMBLi CHEMBL3883.

    Protein family/group databases

    MEROPSi S09.003.

    PTM databases

    PhosphoSitei P28843.

    Proteomic databases

    MaxQBi P28843.
    PaxDbi P28843.
    PRIDEi P28843.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000047812 ; ENSMUSP00000044050 ; ENSMUSG00000035000 .
    GeneIDi 13482.
    KEGGi mmu:13482.
    UCSCi uc008jvg.2. mouse.

    Organism-specific databases

    CTDi 1803.
    MGIi MGI:94919. Dpp4.

    Phylogenomic databases

    eggNOGi COG1506.
    GeneTreei ENSGT00740000115496.
    HOGENOMi HOG000231875.
    HOVERGENi HBG005527.
    InParanoidi P28843.
    KOi K01278.
    OMAi ETKFWYQ.
    OrthoDBi EOG761BT2.
    PhylomeDBi P28843.
    TreeFami TF313309.

    Miscellaneous databases

    ChiTaRSi DPP4. mouse.
    NextBioi 283979.
    PROi P28843.
    SOURCEi Search...

    Gene expression databases

    Bgeei P28843.
    CleanExi MM_DPP4.
    Genevestigatori P28843.

    Family and domain databases

    Gene3Di 2.140.10.30. 1 hit.
    3.40.50.1820. 1 hit.
    InterProi IPR029058. AB_hydrolase.
    IPR002471. Pept_S9_AS.
    IPR001375. Peptidase_S9.
    IPR002469. Peptidase_S9B.
    [Graphical view ]
    Pfami PF00930. DPPIV_N. 1 hit.
    PF00326. Peptidase_S9. 1 hit.
    [Graphical view ]
    SUPFAMi SSF53474. SSF53474. 1 hit.
    PROSITEi PS00708. PRO_ENDOPEP_SER. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "cDNA cloning for mouse thymocyte-activating molecule. A multifunctional ecto-dipeptidyl peptidase IV (CD26) included in a subgroup of serine proteases."
      Marguet D.A., Bernard A.-M., Vivier I., Darmoul D., Naquet P., Pierres M.
      J. Biol. Chem. 267:2200-2208(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Strain: Swiss.
      Tissue: Thymus.
    2. Marguet D.A.
      Submitted (SEP-1994) to the EMBL/GenBank/DDBJ databases
      Cited for: SEQUENCE REVISION.
    3. "Structure of the mouse dipeptidyl peptidase IV (CD26) gene."
      Bernard A.-M., Mattei M.-G., Pierres M., Marguet D.
      Biochemistry 33:15204-15214(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: B10.A.
      Tissue: Liver.
    4. "The transcriptional landscape of the mammalian genome."
      Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
      , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
      Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: C57BL/6J and NOD.
      Tissue: Kidney and Thymus.
    5. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    6. "Evidence that thymocyte-activating molecule is mouse CD26 (dipeptidyl peptidase IV)."
      Vivier I., Marguet D.A., Naquet P., Bonicel J., Black D., Li C.X.-Y., Bernard A.-M., Gorvel J.-P., Pierres M.
      J. Immunol. 147:447-454(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 1-20.
    7. "Mass-spectrometric identification and relative quantification of N-linked cell surface glycoproteins."
      Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M., Schiess R., Aebersold R., Watts J.D.
      Nat. Biotechnol. 27:378-386(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-145 AND ASN-514.

    Entry informationi

    Entry nameiDPP4_MOUSE
    AccessioniPrimary (citable) accession number: P28843
    Secondary accession number(s): Q3U514
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 1, 1992
    Last sequence update: February 1, 1996
    Last modified: October 1, 2014
    This is version 138 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, Direct protein sequencing, Reference proteome

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. Peptidase families
      Classification of peptidase families and list of entries
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3