Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

P09470

- ACE_MOUSE

UniProt

P09470 - ACE_MOUSE

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

Angiotensin-converting enzyme

Gene

Ace

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

Functioni

Converts angiotensin I to angiotensin II by release of the terminal His-Leu, this results in an increase of the vasoconstrictor activity of angiotensin. Also able to inactivate bradykinin, a potent vasodilator. Has also a glycosidase activity which releases GPI-anchored proteins from the membrane by cleaving the mannose linkage in the GPI moiety. This GPIase activity seems to be crucial for the egg-binding ability of the sperm.3 Publications

Catalytic activityi

Release of a C-terminal dipeptide, oligopeptide-|-Xaa-Yaa, when Xaa is not Pro, and Yaa is neither Asp nor Glu. Thus, conversion of angiotensin I to angiotensin II, with increase in vasoconstrictor activity, but no action on angiotensin II.

Cofactori

Protein has several cofactor binding sites:
  • Zn2+By similarityNote: Binds 2 Zn(2+) ions per subunit. Isoform Testis-specific only binds 1 Zn(2+) ion per subunit.By similarity
  • chlorideBy similarityNote: Binds 3 chloride ions per subunit.By similarity

Enzyme regulationi

Peptidase activity is specifically inhibited by lisinopril, captopril and enalaprilat. In contrast, GPIase activity is nearly insensitive to captopril.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei236 – 2361Chloride 1By similarity
Metal bindingi395 – 3951Zinc 1; catalyticBy similarity
Active sitei396 – 39611PROSITE-ProRule annotation
Metal bindingi399 – 3991Zinc 1; catalyticBy similarity
Metal bindingi423 – 4231Zinc 1; catalyticBy similarity
Binding sitei534 – 5341Chloride 1By similarity
Binding sitei796 – 7961Chloride 2By similarity
Binding sitei834 – 8341Chloride 3By similarity
Metal bindingi993 – 9931Zinc 2; catalytic
Active sitei994 – 99412
Metal bindingi997 – 9971Zinc 2; catalytic
Metal bindingi1021 – 10211Zinc 2; catalyticBy similarity
Binding sitei1095 – 10951Chloride 2By similarity
Binding sitei1099 – 10991Chloride 2By similarity
Binding sitei1132 – 11321Chloride 3By similarity

GO - Molecular functioni

  1. carboxypeptidase activity Source: UniProtKB-KW
  2. metal ion binding Source: UniProtKB-KW
  3. metallopeptidase activity Source: UniProtKB
  4. peptidase activity Source: MGI
  5. peptidyl-dipeptidase activity Source: UniProtKB

GO - Biological processi

  1. heart contraction Source: MGI
  2. hormone catabolic process Source: BHF-UCL
  3. kidney development Source: MGI
  4. neutrophil mediated immunity Source: MGI
  5. positive regulation of systemic arterial blood pressure Source: MGI
  6. regulation of blood pressure Source: BHF-UCL
  7. spermatogenesis Source: MGI
Complete GO annotation...

Keywords - Molecular functioni

Carboxypeptidase, Hydrolase, Metalloprotease, Protease

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

ReactomeiREACT_196539. Metabolism of Angiotensinogen to Angiotensins.

Protein family/group databases

MEROPSiM02.001.

Names & Taxonomyi

Protein namesi
Recommended name:
Angiotensin-converting enzyme (EC:3.2.1.-, EC:3.4.15.1)
Short name:
ACE
Alternative name(s):
Dipeptidyl carboxypeptidase I
Kininase II
CD_antigen: CD143
Cleaved into the following chain:
Gene namesi
Name:Ace
Synonyms:Dcp1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 11

Organism-specific databases

MGIiMGI:87874. Ace.

Subcellular locationi

Cell membrane 1 Publication; Single-pass type I membrane protein 1 Publication. Cytoplasm 1 Publication
Note: Detected in both cell membrane and cytoplasm in neurons.

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini35 – 12641230ExtracellularSequence AnalysisAdd
BLAST
Transmembranei1265 – 128117HelicalSequence AnalysisAdd
BLAST
Topological domaini1282 – 131231CytoplasmicSequence AnalysisAdd
BLAST

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB
  2. extracellular region Source: UniProtKB-KW
  3. integral component of membrane Source: UniProtKB-KW
  4. plasma membrane Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cytoplasm, Membrane, Secreted

Pathology & Biotechi

Disruption phenotypei

Low blood pressure, elevated serum potassium, anemia, and renal defects. Male mice have reduced fertility.1 Publication

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi993 – 9931H → K: Abolishes peptidase activity but no effect on GPIase activity; when associated to K-997. 1 Publication
Mutagenesisi994 – 9941E → D: Abolishes peptidase activity but no effect on GPIase activity. 1 Publication
Mutagenesisi997 – 9971H → K: Abolishes peptidase activity but no effect on GPIase activity; when associated to K-993. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 34341 PublicationAdd
BLAST
Chaini35 – 13121278Angiotensin-converting enzymePRO_0000028539Add
BLAST
Chaini35 – 12371203Angiotensin-converting enzyme, soluble formPRO_0000028540Add
BLAST
Propeptidei1238 – 131275Removed in secreted formBy similarityPRO_0000028541Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi59 – 591N-linked (GlcNAc...)Sequence Analysis
Glycosylationi79 – 791N-linked (GlcNAc...)Sequence Analysis
Glycosylationi116 – 1161N-linked (GlcNAc...)Sequence Analysis
Glycosylationi151 – 1511N-linked (GlcNAc...)1 Publication
Disulfide bondi162 ↔ 170By similarity
Glycosylationi165 – 1651N-linked (GlcNAc...)Sequence Analysis
Glycosylationi323 – 3231N-linked (GlcNAc...)Sequence Analysis
Glycosylationi514 – 5141N-linked (GlcNAc...)Sequence Analysis
Glycosylationi682 – 6821N-linked (GlcNAc...)Sequence Analysis
Glycosylationi700 – 7001N-linked (GlcNAc...) (complex)By similarity
Glycosylationi719 – 7191N-linked (GlcNAc...) (complex)By similarity
Disulfide bondi762 ↔ 768By similarity
Glycosylationi765 – 7651N-linked (GlcNAc...)Sequence Analysis
Glycosylationi947 – 9471N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi962 ↔ 980By similarity
Disulfide bondi1148 ↔ 1160By similarity
Glycosylationi1196 – 11961N-linked (GlcNAc...)Sequence Analysis
Modified residuei1305 – 13051PhosphoserineBy similarity

Post-translational modificationi

Phosphorylated by CK2 on Ser-1305; which allows membrane retention.By similarity

Keywords - PTMi

Disulfide bond, Glycoprotein, Phosphoprotein

Proteomic databases

MaxQBiP09470.
PaxDbiP09470.
PRIDEiP09470.

PTM databases

PhosphoSiteiP09470.

Expressioni

Tissue specificityi

Testis-specific isoform is expressed in spermatocytes, adult testis.

Inductioni

Expression is thought to be subject to hormonal regulation by androgens.

Gene expression databases

BgeeiP09470.
ExpressionAtlasiP09470. baseline and differential.
GenevestigatoriP09470.

Interactioni

Protein-protein interaction databases

BioGridi197920. 1 interaction.
IntActiP09470. 3 interactions.
MINTiMINT-4086662.

Structurei

3D structure databases

ProteinModelPortaliP09470.
SMRiP09470. Positions 35-646, 650-1235.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni35 – 635601Peptidase M2 1Add
BLAST
Regioni636 – 1237602Peptidase M2 2Add
BLAST

Sequence similaritiesi

Belongs to the peptidase M2 family.Curated

Keywords - Domaini

Repeat, Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG71044.
GeneTreeiENSGT00520000055576.
HOGENOMiHOG000007838.
HOVERGENiHBG000264.
InParanoidiP09470.
KOiK01283.
OMAiMEQLFTV.
OrthoDBiEOG76HQ13.
PhylomeDBiP09470.
TreeFamiTF312861.

Family and domain databases

InterProiIPR001548. Peptidase_M2.
[Graphical view]
PANTHERiPTHR10514. PTHR10514. 1 hit.
PfamiPF01401. Peptidase_M2. 2 hits.
[Graphical view]
PRINTSiPR00791. PEPDIPTASEA.
PROSITEiPS00142. ZINC_PROTEASE. 2 hits.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

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

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform Somatic (identifier: P09470-1) [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
MGAASGQRGR WPLSPPLLML SLLVLLLQPS PAPALDPGLQ PGNFSPDEAG
60 70 80 90 100
AQLFAESYNS SAEVVMFQST VASWAHDTNI TEENARRQEE AALVSQEFAE
110 120 130 140 150
VWGKKAKELY ESIWQNFTDS KLRRIIGSIR TLGPANLPLA QRQQYNSLLS
160 170 180 190 200
NMSRIYSTGK VCFPNKTATC WSLDPELTNI LASSRSYAKL LFAWEGWHDA
210 220 230 240 250
VGIPLKPLYQ DFTAISNEAY RQDDFSDTGA FWRSWYESPS FEESLEHIYH
260 270 280 290 300
QLEPLYLNLH AYVRRALHRR YGDKYVNLRG PIPAHLLGDM WAQSWENIYD
310 320 330 340 350
MVVPFPDKPN LDVTSTMVQK GWNATHMFRV SEEFFTSLGL SPMPPEFWAE
360 370 380 390 400
SMLEKPTDGR EVVCHASAWD FYNRKDFRIK QCTRVTMEQL ATVHHEMGHV
410 420 430 440 450
QYYLQYKDLH VSLRRGANPG FHEAIGDVLA LSVSTPAHLH KIGLLDHVTN
460 470 480 490 500
DIESDINYLL KMALEKIAFL PFGYLVDQWR WGVFSGRTPP SRYNFDWWYL
510 520 530 540 550
RTKYQGICPP VARNETHFDA GAKFHIPNVT PYIRYFVSFV LQFQFHQALC
560 570 580 590 600
KEAGHQGPLH QCDIYQSAQA GAKLKQVLQA GCSRPWQEVL KDLVGSDALD
610 620 630 640 650
AKALLEYFQP VSQWLEEQNQ RNGEVLGWPE NQWRPPLPDN YPEGIDLETD
660 670 680 690 700
EAKADRFVEE YDRTAQVLLN EYAEANWQYN TNITIEGSKI LLEKSTEVSN
710 720 730 740 750
HTLKYGTRAK TFDVSNFQNS SIKRIIKKLQ NLDRAVLPPK ELEEYNQILL
760 770 780 790 800
DMETTYSLSN ICYTNGTCMP LEPDLTNMMA TSRKYEELLW AWKSWRDKVG
810 820 830 840 850
RAILPFFPKY VEFSNKIAKL NGYTDAGDSW RSLYESDNLE QDLEKLYQEL
860 870 880 890 900
QPLYLNLHAY VRRSLHRHYG SEYINLDGPI PAHLLGNMWA QTWSNIYDLV
910 920 930 940 950
APFPSAPNID ATEAMIKQGW TPRRIFKEAD NFFTSLGLLP VPPEFWNKSM
960 970 980 990 1000
LEKPTDGREV VCHPSAWDFY NGKDFRIKQC TSVNMEDLVI AHHEMGHIQY
1010 1020 1030 1040 1050
FMQYKDLPVT FREGANPGFH EAIGDIMALS VSTPKHLYSL NLLSTEGSGY
1060 1070 1080 1090 1100
EYDINFLMKM ALDKIAFIPF SYLIDQWRWR VFDGSITKEN YNQEWWSLRL
1110 1120 1130 1140 1150
KYQGLCPPVP RSQGDFDPGS KFHVPANVPY VRYFVSFIIQ FQFHEALCRA
1160 1170 1180 1190 1200
AGHTGPLHKC DIYQSKEAGK LLADAMKLGY SKPWPEAMKL ITGQPNMSAS
1210 1220 1230 1240 1250
AMMNYFKPLT EWLVTENRRH GETLGWPEYN WAPNTARAEG STAESNRVNF
1260 1270 1280 1290 1300
LGLYLEPQQA RVGQWVLLFL GVALLVATVG LAHRLYNIRN HHSLRRPHRG
1310
PQFGSEVELR HS
Length:1,312
Mass (Da):150,918
Last modified:August 30, 2005 - v3
Checksum:i7DF9F5BE91762DFF
GO
Isoform Testis-specific (identifier: P09470-2) [UniParc] [UniParc]FASTAAdd to Basket

Also known as: ACE-T

The sequence of this isoform differs from the canonical sequence as follows:
     1-580: Missing.
     581-646: GCSRPWQEVL...LPDNYPEGID → MGQGWATPGL...TIDQTTQIPN

Show »
Length:732
Mass (Da):84,047
Checksum:i16C817E7FBD09BD9
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti568 – 5681A → T in AAA37147. (PubMed:2545691)Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 580580Missing in isoform Testis-specific. 1 PublicationVSP_037638Add
BLAST
Alternative sequencei581 – 64666GCSRP…PEGID → MGQGWATPGLPSFLFLLLCC GHHLLVLSQVATDHVTANQG ITNQATTRSQTTTHQATIDQ TTQIPN in isoform Testis-specific. 1 PublicationVSP_037639Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J04946 mRNA. Translation: AAA37147.1.
J04947 mRNA. Translation: AAA37148.1.
M55333 mRNA. Translation: AAA37149.1.
M61094 Genomic DNA. Translation: AAA37150.1.
BC040404 mRNA. Translation: AAH40404.1.
J03940 mRNA. Translation: AAA37146.1.
CCDSiCCDS25543.1. [P09470-1]
CCDS25544.1. [P09470-2]
PIRiA34171.
A35655.
RefSeqiNP_033728.1. NM_009598.2. [P09470-2]
NP_997507.1. NM_207624.5. [P09470-1]
UniGeneiMm.754.

Genome annotation databases

EnsembliENSMUST00000001963; ENSMUSP00000001963; ENSMUSG00000020681. [P09470-1]
ENSMUST00000001964; ENSMUSP00000001964; ENSMUSG00000020681. [P09470-2]
GeneIDi11421.
KEGGimmu:11421.
UCSCiuc007lxu.2. mouse. [P09470-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J04946 mRNA. Translation: AAA37147.1 .
J04947 mRNA. Translation: AAA37148.1 .
M55333 mRNA. Translation: AAA37149.1 .
M61094 Genomic DNA. Translation: AAA37150.1 .
BC040404 mRNA. Translation: AAH40404.1 .
J03940 mRNA. Translation: AAA37146.1 .
CCDSi CCDS25543.1. [P09470-1 ]
CCDS25544.1. [P09470-2 ]
PIRi A34171.
A35655.
RefSeqi NP_033728.1. NM_009598.2. [P09470-2 ]
NP_997507.1. NM_207624.5. [P09470-1 ]
UniGenei Mm.754.

3D structure databases

ProteinModelPortali P09470.
SMRi P09470. Positions 35-646, 650-1235.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 197920. 1 interaction.
IntActi P09470. 3 interactions.
MINTi MINT-4086662.

Chemistry

BindingDBi P09470.
ChEMBLi CHEMBL2994.

Protein family/group databases

MEROPSi M02.001.

PTM databases

PhosphoSitei P09470.

Proteomic databases

MaxQBi P09470.
PaxDbi P09470.
PRIDEi P09470.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000001963 ; ENSMUSP00000001963 ; ENSMUSG00000020681 . [P09470-1 ]
ENSMUST00000001964 ; ENSMUSP00000001964 ; ENSMUSG00000020681 . [P09470-2 ]
GeneIDi 11421.
KEGGi mmu:11421.
UCSCi uc007lxu.2. mouse. [P09470-1 ]

Organism-specific databases

CTDi 1636.
MGIi MGI:87874. Ace.

Phylogenomic databases

eggNOGi NOG71044.
GeneTreei ENSGT00520000055576.
HOGENOMi HOG000007838.
HOVERGENi HBG000264.
InParanoidi P09470.
KOi K01283.
OMAi MEQLFTV.
OrthoDBi EOG76HQ13.
PhylomeDBi P09470.
TreeFami TF312861.

Enzyme and pathway databases

Reactomei REACT_196539. Metabolism of Angiotensinogen to Angiotensins.

Miscellaneous databases

NextBioi 278668.
PROi P09470.
SOURCEi Search...

Gene expression databases

Bgeei P09470.
ExpressionAtlasi P09470. baseline and differential.
Genevestigatori P09470.

Family and domain databases

InterProi IPR001548. Peptidase_M2.
[Graphical view ]
PANTHERi PTHR10514. PTHR10514. 1 hit.
Pfami PF01401. Peptidase_M2. 2 hits.
[Graphical view ]
PRINTSi PR00791. PEPDIPTASEA.
PROSITEi PS00142. ZINC_PROTEASE. 2 hits.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Mouse angiotensin-converting enzyme is a protein composed of two homologous domains."
    Bernstein K.E., Martin B.M., Edwards A.S., Bernstein E.A.
    J. Biol. Chem. 264:11945-11951(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM SOMATIC).
  2. "Transcription of testicular angiotensin-converting enzyme (ACE) is initiated within the 12th intron of the somatic ACE gene."
    Howard T.E., Shai S.-Y., Langford K.G., Martin B.M., Bernstein K.E.
    Mol. Cell. Biol. 10:4294-4302(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM TESTIS-SPECIFIC), PARTIAL NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  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 SOMATIC).
    Strain: FVB/N.
    Tissue: Mammary gland.
  4. "The isolation of angiotensin-converting enzyme cDNA."
    Bernstein K.E., Martin B.M., Bernstein E.A., Linton J., Striker L., Striker G.
    J. Biol. Chem. 263:11021-11024(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-332 (ISOFORM SOMATIC), PARTIAL PROTEIN SEQUENCE.
  5. "Partial protein sequence of mouse and bovine kidney angiotensin converting enzyme."
    Bernstein K.E., Martin B.M., Striker L., Striker G.
    Kidney Int. 33:652-655(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 35-54.
    Tissue: Kidney.
  6. "Male-female differences in fertility and blood pressure in ACE-deficient mice."
    Krege J.H., John S.W., Langenbach L.L., Hodgin J.B., Hagaman J.R., Bachman E.S., Jennette J.C., O'Brien D.A., Smithies O.
    Nature 375:146-148(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  7. "Mice lacking angiotensin-converting enzyme have low blood pressure, renal pathology, and reduced male fertility."
    Esther C.R. Jr., Howard T.E., Marino E.M., Goddard J.M., Capecchi M.R., Bernstein K.E.
    Lab. Invest. 74:953-965(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, DISRUPTION PHENOTYPE.
  8. "Angiotensin-converting enzyme is a GPI-anchored protein releasing factor crucial for fertilization."
    Kondoh G., Tojo H., Nakatani Y., Komazawa N., Murata C., Yamagata K., Maeda Y., Kinoshita T., Okabe M., Taguchi R., Takeda J.
    Nat. Med. 11:160-166(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, ENZYME REGULATION, MUTAGENESIS OF HIS-993; GLU-994 AND HIS-997.
  9. "Proteome-wide characterization of N-glycosylation events by diagonal chromatography."
    Ghesquiere B., Van Damme J., Martens L., Vandekerckhove J., Gevaert K.
    J. Proteome Res. 5:2438-2447(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-151.
    Strain: C57BL/6.
    Tissue: Plasma.
  10. "Qualitative and quantitative analyses of protein phosphorylation in naive and stimulated mouse synaptosomal preparations."
    Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F., Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D., Gerrits B., Panse C., Schlapbach R., Mansuy I.M.
    Mol. Cell. Proteomics 6:283-293(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain cortex.
  11. "Angiotensin II regulates ACE and ACE2 in neurons through p38 mitogen-activated protein kinase and extracellular signal-regulated kinase 1/2 signaling."
    Xiao L., Haack K.K., Zucker I.H.
    Am. J. Physiol. 304:C1073-C1079(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION.

Entry informationi

Entry nameiACE_MOUSE
AccessioniPrimary (citable) accession number: P09470
Secondary accession number(s): P22967, Q6GTS2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: August 30, 2005
Last modified: November 26, 2014
This is version 147 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. Glycosyl hydrolases
    Classification of glycosyl hydrolase families and list of entries
  2. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  3. Peptidase families
    Classification of peptidase families and list of entries
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3