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P97321

- SEPR_MOUSE

UniProt

P97321 - SEPR_MOUSE

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Protein

Prolyl endopeptidase FAP

Gene

Fap

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

Cell surface glycoprotein serine protease that participates in extracellular matrix degradation and involved in many cellular processes including tissue remodeling, fibrosis, wound healing, inflammation and tumor growth. Both plasma membrane and soluble forms exhibit post-proline cleaving endopeptidase activity, with a marked preference for Ala/Ser-Gly-Pro-Ser/Asn/Ala consensus sequences, on substrate such as alpha-2-antiplasmin SERPINF2 and SPRY2. Degrade also gelatin, heat-denatured type I collagen, but not native collagen type I and IV, vibronectin, tenascin, laminin, fibronectin, fibrin or casein. Have also dipeptidyl peptidase activity, exhibiting the ability to hydrolyze the prolyl bond two residues from the N-terminus of synthetic dipeptide substrates provided that the penultimate residue is proline, with a preference for Ala-Pro, Ile-Pro, Gly-Pro, Arg-Pro and Pro-Pro. Natural neuropeptide hormones for dipeptidyl peptidase are the neuropeptide Y (NPY), peptide YY (PYY), substance P (TAC1) and brain natriuretic peptide 32 (NPPB). The plasma membrane form, in association with either DPP4, PLAUR or integrins, is involved in the pericellular proteolysis of the extracellular matrix (ECM), and hence promotes cell adhesion, migration and invasion through the ECM. Plays a role in tissue remodeling during development and wound healing. Participates in the cell invasiveness towards the ECM in malignant melanoma cancers. Enhances tumor growth progression by increasing angiogenesis, collagen fiber degradation and apoptosis and by reducing antitumor response of the immune system. Promotes glioma cell invasion through the brain parenchyma by degrading the proteoglycan brevican. Acts as a tumor suppressor in melanocytic cells through regulation of cell proliferation and survival in a serine protease activity-independent manner.7 Publications

Catalytic activityi

Hydrolysis of Pro-|-Xaa >> Ala-|-Xaa in oligopeptides.1 Publication
Release of an N-terminal dipeptide, Xaa-Yaa-|-Zaa-, from a polypeptide, preferentially when Yaa is Pro, provided Zaa is neither Pro nor hydroxyproline.4 PublicationsPROSITE-ProRule annotation

Enzyme regulationi

Gelatinase activity is inhibited by serine-protease inhibitors, such as phenylmethylsulfonyl fluoride (PMSF), 4-(2-aminoethyl)-benzenesulfonyl fluoride hydrochloride (AEBSF), 4-amidino phenylsulfonyl fluoride (APSF) and diisopropyl fluorophosphate (DFP), N-ethylmaleimide (NEM) and phenylmethylsulfonyl fluoride (PMSF). Dipeptidyl peptidase activity is inhibited by 2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid), diisopropylfluorophosphate (DFP). Prolyl endopeptidase activity is inhibited by the boronic acid peptide Ac-Gly-BoroPro, Ac-Gly-Pro-chloromethyl ketone and Thr-Ser-Gly-chloromethyl ketone.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei23 – 242CleavageBy similarity
Binding sitei203 – 2031SubstrateBy similarity
Binding sitei204 – 2041SubstrateBy similarity
Active sitei624 – 6241Charge relay systemBy similarityPROSITE-ProRule annotation
Active sitei702 – 7021Charge relay systemBy similarity
Active sitei734 – 7341Charge relay systemBy similarity

GO - Molecular functioni

  1. dipeptidyl-peptidase activity Source: UniProtKB
  2. peptidase activity Source: MGI
  3. protein homodimerization activity Source: UniProtKB
  4. serine-type endopeptidase activity Source: UniProtKB
  5. serine-type peptidase activity Source: UniProtKB

GO - Biological processi

  1. endothelial cell migration Source: UniProtKB
  2. melanocyte apoptotic process Source: UniProtKB
  3. melanocyte proliferation Source: UniProtKB
  4. mitotic cell cycle arrest Source: UniProtKB
  5. negative regulation of cell proliferation involved in contact inhibition Source: UniProtKB
  6. negative regulation of extracellular matrix disassembly Source: UniProtKB
  7. negative regulation of extracellular matrix organization Source: UniProtKB
  8. positive regulation of cell cycle arrest Source: UniProtKB
  9. positive regulation of execution phase of apoptosis Source: UniProtKB
  10. proteolysis Source: UniProtKB
  11. proteolysis involved in cellular protein catabolic process Source: UniProtKB
  12. regulation of collagen catabolic process Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protease, Serine protease

Keywords - Biological processi

Angiogenesis, Apoptosis, Cell adhesion

Protein family/group databases

MEROPSiS09.007.

Names & Taxonomyi

Protein namesi
Recommended name:
Prolyl endopeptidase FAPBy similarity (EC:3.4.21.261 Publication)
Alternative name(s):
Dipeptidyl peptidase FAPBy similarity (EC:3.4.14.54 Publications)
Fibroblast activation protein alphaBy similarity
Short name:
FAPalpha1 Publication
Gelatine degradation protease FAPBy similarity (EC:3.4.21.-By similarity)
Integral membrane serine proteaseBy similarity
Post-proline cleaving enzymeCurated
Serine integral membrane proteaseBy similarity
Short name:
SIMPBy similarity
Surface-expressed proteaseBy similarity
Short name:
SepraseBy similarity
Cleaved into the following chain:
Antiplasmin-cleaving enzyme FAP, soluble formBy similarity (EC:3.4.14.5By similarity, EC:3.4.21.-By similarity, EC:3.4.21.26By similarity)
Short name:
APCEBy similarity
Gene namesi
Name:FapImported
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 2

Organism-specific databases

MGIiMGI:109608. Fap.

Subcellular locationi

Chain Prolyl endopeptidase FAP : Cell surface 1 Publication. Cell membrane By similarity; Single-pass type II membrane protein Sequence Analysis. Cell projectionlamellipodium membrane By similarity; Single-pass type II membrane protein Sequence Analysis. Cell projectioninvadopodium membrane By similarity; Single-pass type II membrane protein Sequence Analysis. Cell projectionruffle membrane By similarity; Single-pass type II membrane protein Sequence Analysis. Membrane By similarity; Single-pass type II membrane protein Sequence Analysis
Note: Localized on cell surface with lamellipodia and invadopodia membranes and on shed vesicles. Colocalized with DPP4 at invadopodia and lamellipodia membranes of migratory activated endothelial cells in collagenous matrix. Colocalized with DPP4 on endothelial cells of capillary-like microvessels but not large vessels within invasive breast ductal carcinoma. Anchored and enriched preferentially by integrin alpha-3/beta-1 at invadopodia, plasma membrane protrusions that correspond to sites of cell invasion, in a collagen-dependent manner. Localized at plasma and ruffle membranes in a collagen-independent manner. Colocalized with PLAUR preferentially at the cell surface of invadopodia membranes in a cytoskeleton-, integrin- and vitronectin-dependent manner. Concentrated at invadopodia membranes, specialized protrusions of the ventral plasma membrane in a fibrobectin-dependent manner. Colocalizes with extracellular components (ECM), such as collagen fibers and fibronectin.By similarity
Chain Antiplasmin-cleaving enzyme FAP, soluble form : Secreted 1 Publication
Note: Found in blood plasma and serum.1 Publication

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 44CytoplasmicBy similaritySequence Analysis
Transmembranei5 – 2521Helical; Signal-anchor for type II membrane proteinSequence AnalysisAdd
BLAST
Topological domaini26 – 761736ExtracellularBy similaritySequence AnalysisAdd
BLAST

GO - Cellular componenti

  1. apical part of cell Source: MGI
  2. basal part of cell Source: MGI
  3. cell junction Source: UniProtKB-KW
  4. cell surface Source: UniProtKB
  5. extracellular space Source: Ensembl
  6. integral component of membrane Source: UniProtKB-KW
  7. invadopodium membrane Source: UniProtKB
  8. lamellipodium Source: UniProtKB
  9. plasma membrane Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

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

Pathology & Biotechi

Disruption phenotypei

No visible phenotype. Mice are viable and fertile and display no overt developmental defects and no general change in cancer susceptibiliy.1 Publication

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi624 – 6241S → A: Localized at the cell surface, inhibits gelatinase and dipeptidyl peptidase activities and stimulates tumor suppression activity. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 761761Prolyl endopeptidase FAPBy similarityPRO_0000122425Add
BLAST
Chaini24 – 761738Antiplasmin-cleaving enzyme FAP, soluble formBy similarityPRO_0000430644Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi49 – 491N-linked (GlcNAc...)By similarityPROSITE-ProRule annotation
Glycosylationi92 – 921N-linked (GlcNAc...)By similarityPROSITE-ProRule annotation
Glycosylationi99 – 991N-linked (GlcNAc...)By similarityPROSITE-ProRule annotation
Glycosylationi227 – 2271N-linked (GlcNAc...)By similarityPROSITE-ProRule annotation
Glycosylationi314 – 3141N-linked (GlcNAc...)By similarityPROSITE-ProRule annotation
Disulfide bondi321 ↔ 332By similarity
Disulfide bondi438 ↔ 441By similarity
Disulfide bondi448 ↔ 466By similarity
Disulfide bondi643 ↔ 756By similarity
Glycosylationi679 – 6791N-linked (GlcNAc...)PROSITE-ProRule annotation

Post-translational modificationi

N-glycosylated.By similarity
The N-terminus may be blocked.By similarity

Keywords - PTMi

Cleavage on pair of basic residues, Disulfide bond, Glycoprotein

Proteomic databases

PaxDbiP97321.
PRIDEiP97321.

PTM databases

PhosphoSiteiP97321.

Expressioni

Tissue specificityi

Expressed strongly in uterus, pancreas, submaxillary gland and skin, less in lymph node, ovary, skeletal muscle, adrenal and bone marrow. Expressed in reactive stromal fibroblast in epithelial cancers. Expressed in melanocytes but not melanomas (at protein level). Detected in fibroblasts, in placenta, uterus, embryos from day 7-19 and in newborn mice (P1).3 Publications

Developmental stagei

Expressed in developing myotubes at 11.5 dpc. Expressed in the dermomyotome component of the somites at 12.5 dpc. Expressed in fibroblasts at 13 dpc. Expressed in the perichondrial mesenchymal cells from the cartilage primordium of the ribs and in the scattered developing intercostal muscle fibs at 16.5 dpc (at protein level). Expressed in the primitive mesenchymal condensation adjacent to the eye and in primitive mesenchymal cells surrounding the cartilaginous primordia of the bones at 13.5 dpc.2 Publications

Gene expression databases

BgeeiP97321.
CleanExiMM_FAP.
ExpressionAtlasiP97321. baseline and differential.
GenevestigatoriP97321.

Interactioni

Subunit structurei

Homodimer; homodimerization is required for activity of both plasma membrane and soluble forms. The monomer is inactive. Heterodimer with DPP4. Interacts with PLAUR; the interaction occurs at the cell surface of invadopodia membranes. Interacts with ITGB1. Interacts with ITGA3. Associates with integrin alpha-3/beta-1; the association occurs in a collagen-dependent manner at the cell surface of invadopodia membranes.By similarity

Protein-protein interaction databases

MINTiMINT-4997001.

Structurei

3D structure databases

ProteinModelPortaliP97321.
SMRiP97321. Positions 40-758.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase S9B family.Curated

Keywords - Domaini

Signal-anchor, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiCOG1506.
GeneTreeiENSGT00760000119233.
HOGENOMiHOG000231875.
HOVERGENiHBG005527.
InParanoidiP97321.
KOiK08674.
OMAiQYYTARF.
OrthoDBiEOG761BT2.
PhylomeDBiP97321.
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.

Sequences (3)i

Sequence statusi: Complete.

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

This entry describes 3 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: P97321-1) [UniParc]FASTAAdd to Basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MKTWLKTVFG VTTLAALALV VICIVLRPSR VYKPEGNTKR ALTLKDILNG
60 70 80 90 100
TFSYKTYFPN WISEQEYLHQ SEDDNIVFYN IETRESYIIL SNSTMKSVNA
110 120 130 140 150
TDYGLSPDRQ FVYLESDYSK LWRYSYTATY YIYDLQNGEF VRGYELPRPI
160 170 180 190 200
QYLCWSPVGS KLAYVYQNNI YLKQRPGDPP FQITYTGREN RIFNGIPDWV
210 220 230 240 250
YEEEMLATKY ALWWSPDGKF LAYVEFNDSD IPIIAYSYYG DGQYPRTINI
260 270 280 290 300
PYPKAGAKNP VVRVFIVDTT YPHHVGPMEV PVPEMIASSD YYFSWLTWVS
310 320 330 340 350
SERVCLQWLK RVQNVSVLSI CDFREDWHAW ECPKNQEHVE ESRTGWAGGF
360 370 380 390 400
FVSTPAFSQD ATSYYKIFSD KDGYKHIHYI KDTVENAIQI TSGKWEAIYI
410 420 430 440 450
FRVTQDSLFY SSNEFEGYPG RRNIYRISIG NSPPSKKCVT CHLRKERCQY
460 470 480 490 500
YTASFSYKAK YYALVCYGPG LPISTLHDGR TDQEIQVLEE NKELENSLRN
510 520 530 540 550
IQLPKVEIKK LKDGGLTFWY KMILPPQFDR SKKYPLLIQV YGGPCSQSVK
560 570 580 590 600
SVFAVNWITY LASKEGIVIA LVDGRGTAFQ GDKFLHAVYR KLGVYEVEDQ
610 620 630 640 650
LTAVRKFIEM GFIDEERIAI WGWSYGGYVS SLALASGTGL FKCGIAVAPV
660 670 680 690 700
SSWEYYASIY SERFMGLPTK DDNLEHYKNS TVMARAEYFR NVDYLLIHGT
710 720 730 740 750
ADDNVHFQNS AQIAKALVNA QVDFQAMWYS DQNHGISSGR SQNHLYTHMT
760
HFLKQCFSLS D
Length:761
Mass (Da):87,945
Last modified:May 1, 1997 - v1
Checksum:i9174C3AEDA213B25
GO
Isoform 2 (identifier: P97321-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     31-35: Missing.

Show »
Length:756
Mass (Da):87,328
Checksum:iBE2A232BCEFD0C64
GO
Isoform 3 (identifier: P97321-3) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     31-63: Missing.

Show »
Length:728
Mass (Da):84,096
Checksum:i4436F2EC1C4B1BDA
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti737 – 7371S → L in AAH19190. (PubMed:15489334)Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei31 – 6333Missing in isoform 3. 1 PublicationVSP_005369Add
BLAST
Alternative sequencei31 – 355Missing in isoform 2. 1 PublicationVSP_005368

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Y10007 mRNA. Translation: CAA71116.1.
BC019190 mRNA. Translation: AAH19190.1.
CCDSiCCDS16067.1. [P97321-1]
RefSeqiNP_032012.1. NM_007986.3. [P97321-1]
XP_006498809.1. XM_006498746.1. [P97321-1]
UniGeneiMm.41816.

Genome annotation databases

EnsembliENSMUST00000000402; ENSMUSP00000000402; ENSMUSG00000000392. [P97321-3]
ENSMUST00000102732; ENSMUSP00000099793; ENSMUSG00000000392. [P97321-1]
ENSMUST00000174448; ENSMUSP00000134386; ENSMUSG00000000392. [P97321-2]
GeneIDi14089.
KEGGimmu:14089.
UCSCiuc008jvk.1. mouse. [P97321-1]
uc008jvl.1. mouse. [P97321-3]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Y10007 mRNA. Translation: CAA71116.1 .
BC019190 mRNA. Translation: AAH19190.1 .
CCDSi CCDS16067.1. [P97321-1 ]
RefSeqi NP_032012.1. NM_007986.3. [P97321-1 ]
XP_006498809.1. XM_006498746.1. [P97321-1 ]
UniGenei Mm.41816.

3D structure databases

ProteinModelPortali P97321.
SMRi P97321. Positions 40-758.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

MINTi MINT-4997001.

Chemistry

BindingDBi P97321.
ChEMBLi CHEMBL5769.

Protein family/group databases

MEROPSi S09.007.

PTM databases

PhosphoSitei P97321.

Proteomic databases

PaxDbi P97321.
PRIDEi P97321.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000000402 ; ENSMUSP00000000402 ; ENSMUSG00000000392 . [P97321-3 ]
ENSMUST00000102732 ; ENSMUSP00000099793 ; ENSMUSG00000000392 . [P97321-1 ]
ENSMUST00000174448 ; ENSMUSP00000134386 ; ENSMUSG00000000392 . [P97321-2 ]
GeneIDi 14089.
KEGGi mmu:14089.
UCSCi uc008jvk.1. mouse. [P97321-1 ]
uc008jvl.1. mouse. [P97321-3 ]

Organism-specific databases

CTDi 2191.
MGIi MGI:109608. Fap.

Phylogenomic databases

eggNOGi COG1506.
GeneTreei ENSGT00760000119233.
HOGENOMi HOG000231875.
HOVERGENi HBG005527.
InParanoidi P97321.
KOi K08674.
OMAi QYYTARF.
OrthoDBi EOG761BT2.
PhylomeDBi P97321.
TreeFami TF313309.

Miscellaneous databases

NextBioi 285126.
PROi P97321.
SOURCEi Search...

Gene expression databases

Bgeei P97321.
CleanExi MM_FAP.
ExpressionAtlasi P97321. baseline and differential.
Genevestigatori P97321.

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.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Mouse fibroblast activation protein: molecular cloning, alternative splicing and expression in the reactive stroma of epithelial cancers."
    Niedermeyer J., Scanlan M.J., Garin-Chesa P., Daiber C., Fiebig H.H., Old L.J., Rettig W.J., Schnapp A.
    Int. J. Cancer 71:383-389(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2 AND 3).
    Strain: BALB/c.
    Tissue: Embryo.
  2. "Mouse fibroblast-activation protein--conserved Fap gene organization and biochemical function as a serine protease."
    Niedermeyer J., Enenkel B., Park J.E., Lenter M., Rettig W.J., Damm K., Schnapp A.
    Eur. J. Biochem. 254:650-654(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], FUNCTION, CATALYTIC ACTIVITY.
  3. "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] (ISOFORM 1).
    Tissue: Mammary gland.
  4. Cited for: FUNCTION, DISRUPTION PHENOTYPE, CATALYTIC ACTIVITY, DEVELOPMENTAL STAGE.
  5. "Expression of the fibroblast activation protein during mouse embryo development."
    Niedermeyer J., Garin-Chesa P., Kriz M., Hilberg F., Mueller E., Bamberger U., Rettig W.J., Schnapp A.
    Int. J. Dev. Biol. 45:445-447(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, CATALYTIC ACTIVITY, DEVELOPMENTAL STAGE.
  6. "FAPalpha, a surface peptidase expressed during wound healing, is a tumor suppressor."
    Ramirez-Montagut T., Blachere N.E., Sviderskaya E.V., Bennett D.C., Rettig W.J., Garin-Chesa P., Houghton A.N.
    Oncogene 23:5435-5446(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, CATALYTIC ACTIVITY, TISSUE SPECIFICITY, MUTAGENESIS OF SER-624.
  7. "Suppression of antitumor immunity by stromal cells expressing fibroblast activation protein-alpha."
    Kraman M., Bambrough P.J., Arnold J.N., Roberts E.W., Magiera L., Jones J.O., Gopinathan A., Tuveson D.A., Fearon D.T.
    Science 330:827-830(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, TISSUE SPECIFICITY.
  8. "Short hairpin RNA targeting of fibroblast activation protein inhibits tumor growth and improves the tumor microenvironment in a mouse model."
    Cai F., Li Z., Wang C., Xian S., Xu G., Peng F., Wei Y., Lu Y.
    BMB Rep. 46:252-257(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  9. Cited for: FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.

Entry informationi

Entry nameiSEPR_MOUSE
AccessioniPrimary (citable) accession number: P97321
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 5, 2002
Last sequence update: May 1, 1997
Last modified: November 26, 2014
This is version 127 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. 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