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Q50JE5

- ACE_MESAU

UniProt

Q50JE5 - ACE_MESAU

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Protein

Angiotensin-converting enzyme

Gene

Ace

Organism
Mesocricetus auratus (Golden hamster)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at transcript 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 (By similarity).By similarity

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

Binds 2 zinc ions per subunit.By similarity
Binds 3 chloride ions per subunit.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei237 – 2371Chloride 1By similarity
Metal bindingi396 – 3961Zinc 1; catalyticBy similarity
Active sitei397 – 39711PROSITE-ProRule annotation
Metal bindingi400 – 4001Zinc 1; catalyticBy similarity
Metal bindingi424 – 4241Zinc 1; catalyticBy similarity
Binding sitei535 – 5351Chloride 1By similarity
Binding sitei797 – 7971Chloride 2By similarity
Binding sitei835 – 8351Chloride 3By similarity
Metal bindingi994 – 9941Zinc 2; catalyticBy similarity
Active sitei995 – 99512PROSITE-ProRule annotation
Metal bindingi998 – 9981Zinc 2; catalyticBy similarity
Metal bindingi1022 – 10221Zinc 2; catalyticBy similarity
Binding sitei1096 – 10961Chloride 2By similarity
Binding sitei1100 – 11001Chloride 2By similarity
Binding sitei1133 – 11331Chloride 3By similarity

GO - Molecular functioni

  1. carboxypeptidase activity Source: UniProtKB-KW
  2. metal ion binding Source: UniProtKB-KW
  3. metallopeptidase activity Source: UniProtKB-KW
  4. peptidyl-dipeptidase activity Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Carboxypeptidase, Hydrolase, Metalloprotease, Protease

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

BRENDAi3.4.15.1. 3239.

Protein family/group databases

MEROPSiM02.005.

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
OrganismiMesocricetus auratus (Golden hamster)
Taxonomic identifieri10036 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaCricetidaeCricetinaeMesocricetus

Subcellular locationi

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

GO - Cellular componenti

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

Keywords - Cellular componenti

Cell membrane, Cytoplasm, Membrane, Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 3535By similarityAdd
BLAST
Chaini36 – 13141279Angiotensin-converting enzymePRO_0000028536Add
BLAST
Chaini36 – 12381203Angiotensin-converting enzyme, soluble formPRO_0000028537Add
BLAST
Propeptidei1239 – 131476Removed in secreted formBy similarityPRO_0000028538Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi44 – 441N-linked (GlcNAc...)Sequence Analysis
Glycosylationi60 – 601N-linked (GlcNAc...)Sequence Analysis
Glycosylationi80 – 801N-linked (GlcNAc...)Sequence Analysis
Glycosylationi117 – 1171N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi163 ↔ 171By similarity
Glycosylationi166 – 1661N-linked (GlcNAc...)Sequence Analysis
Glycosylationi324 – 3241N-linked (GlcNAc...)Sequence Analysis
Glycosylationi515 – 5151N-linked (GlcNAc...)Sequence Analysis
Glycosylationi683 – 6831N-linked (GlcNAc...)Sequence Analysis
Glycosylationi701 – 7011N-linked (GlcNAc...)Sequence Analysis
Glycosylationi720 – 7201N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi763 ↔ 769By similarity
Glycosylationi766 – 7661N-linked (GlcNAc...)Sequence Analysis
Glycosylationi948 – 9481N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi963 ↔ 981By similarity
Disulfide bondi1149 ↔ 1161By similarity
Glycosylationi1197 – 11971N-linked (GlcNAc...)Sequence Analysis
Modified residuei1307 – 13071PhosphoserineBy similarity

Post-translational modificationi

Phosphorylated by CK2 on Ser-1307; which allows membrane retention.By similarity

Keywords - PTMi

Disulfide bond, Glycoprotein, Phosphoprotein

Expressioni

Tissue specificityi

Widely expressed with dominant expression in lung and kidney.1 Publication

Structurei

3D structure databases

ProteinModelPortaliQ50JE5.
SMRiQ50JE5. Positions 36-647, 651-1234.
ModBaseiSearch...
MobiDBiSearch...

Topological domain

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini36 – 12651230ExtracellularSequence AnalysisAdd
BLAST
Topological domaini1283 – 131432CytoplasmicSequence AnalysisAdd
BLAST

Transmembrane

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei1266 – 128217HelicalSequence AnalysisAdd
BLAST

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni36 – 636601Peptidase M2 1Add
BLAST
Regioni637 – 1238602Peptidase M2 2Add
BLAST

Sequence similaritiesi

Belongs to the peptidase M2 family.Curated

Keywords - Domaini

Repeat, Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

HOVERGENiHBG000264.

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: Q50JE5) [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
MGAASGQRGQ GPPSPLLLLW LSLLLLLLPP SPAPALDPGL QPGNFSADEI
60 70 80 90 100
GAHLFAESYN SSAEQVIFQS TVASWAYDTN MTEENARLQE EAELIWQEFA
110 120 130 140 150
EVWGKKAKEL FDAIRQNFTD SKLRRVIETI RTLGPANLPL ARRQQYNSLQ
160 170 180 190 200
NNMNRIYSTS KVCLPNKTAT CWSLEPELTN ILASSRSYAK LLFAWESWHD
210 220 230 240 250
VVGIPLKPLY QDFTALSNEA YKQDGFSDTG AYWRSAYDSP SFEETLEHLY
260 270 280 290 300
HQLEPLYLNL HAYVRRALHR RYGDKYINLR GPIPAHLLGD MWAQSWDNIY
310 320 330 340 350
DMVVPFPNKP NLDVTNTMVQ KGWNVTHMFR VAEEFFTSMG LSPMPPEFWA
360 370 380 390 400
ESMLEKPTDG REVVCHASAW DFFNRKDFRI KQCTRITMEQ LSTVHHEMGH
410 420 430 440 450
VQYYLQYKDL TVPLRRGANP GFHEAIGDVL ALSVSTPAHL HKIGLLDRVA
460 470 480 490 500
NDLESDINYL LKMALEKIAF LPFGYLVDQW RWGVFSGHTP PSRYNFDWWY
510 520 530 540 550
FRTKYQGICP PVVRNETHFD AGAKFHIPSG TPYIRYFVSF ILQFQFHQAL
560 570 580 590 600
CKEAGHQGPL HQCDIYQSTQ AGAKLQRVLQ AGYSRPWQEV LKEMVGSDTL
610 620 630 640 650
DAQALLEYFQ PVIRWLQEQN QRNGEVLGWP EYQWRPPLPD NYPEGIDLVT
660 670 680 690 700
DETEAERFVE EYDRTARVLW NEYAEANWQY NTNITLEASK ILLQKNKKVA
710 720 730 740 750
NHTLKYGTLA KKFDVSNFQN YTIKRIIKKV QNMDRAVLPP KELEEYNQIL
760 770 780 790 800
MDMETTYSIA NVCYLNGTCL HLEPDLTNVM ATSRKYEELL WVWKSWRDKV
810 820 830 840 850
GRAILPLFPK YVELSNKIAH LNGYADGGDS WRSSYESKSL EQDLEQLYQE
860 870 880 890 900
LQPLYLNLHA YVRRSLHRHY GSQHINLDGP IPAHLLGNMW AQTWSNIYDL
910 920 930 940 950
VAPFPSAPNL DATEAMIKQG WTPRRIFKEA DDFFTSLGLL PVSEEFWNKS
960 970 980 990 1000
MLEKPGDGRE VVCHASAWDF YNGKDFRIKQ CTSVNMEDLV IAHHEMGHIQ
1010 1020 1030 1040 1050
YFMQYKDLPV TFREGANPGF HEAIGDVLAL SVSTPKHLHS LNLLSSEGGG
1060 1070 1080 1090 1100
YEHDINFLMK MALDKIAFIP FSYLIDQWRW RVFDGSITKE NYNQEWWSLR
1110 1120 1130 1140 1150
LKYQGLCPPV PRSQDDFDPG SKFHVPANVP YIRYFVSFII QFQFHEALCR
1160 1170 1180 1190 1200
AAGHTGPLHK CDIYQSKEAG KLLADTMKMG YSKPWPEAMK LITGQPNMSA
1210 1220 1230 1240 1250
SAMMNYFKPL TEWLVTENRR HGETLGWPEY NWTPNTARSE GPFPESGRVN
1260 1270 1280 1290 1300
FLGMYLEPQQ ARVGQWVLLF LGVSLLVATL GLTHRLFSIR QHGHSLHRPH
1310
RGPQFGSEVE LRHS
Length:1,314
Mass (Da):151,595
Last modified:June 7, 2005 - v1
Checksum:i74E29238E87F157E
GO
Isoform Testis-specific (identifier: Q50JE5-2)

Also known as: ACE-T

Sequence is not available
Length:
Mass (Da):

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AB212958 mRNA. Translation: BAD98304.1.
RefSeqiNP_001268510.1. NM_001281581.1. [Q50JE5-1]

Genome annotation databases

GeneIDi101824864.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AB212958 mRNA. Translation: BAD98304.1 .
RefSeqi NP_001268510.1. NM_001281581.1. [Q50JE5-1 ]

3D structure databases

ProteinModelPortali Q50JE5.
SMRi Q50JE5. Positions 36-647, 651-1234.
ModBasei Search...
MobiDBi Search...

Protein family/group databases

MEROPSi M02.005.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 101824864.

Phylogenomic databases

HOVERGENi HBG000264.

Enzyme and pathway databases

BRENDAi 3.4.15.1. 3239.

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

  1. "cDNA cloning of hamster angiotensin-converting enzyme and mRNA expression."
    Uchide T., Fujimori Y., Fukushima U., Uechi M., Sasaki T., Temma K.
    DNA Seq. 17:319-325(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY.

Entry informationi

Entry nameiACE_MESAU
AccessioniPrimary (citable) accession number: Q50JE5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 30, 2005
Last sequence update: June 7, 2005
Last modified: October 29, 2014
This is version 52 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Documents

  1. Glycosyl hydrolases
    Classification of glycosyl hydrolase families and list of entries
  2. Peptidase families
    Classification of peptidase families and list of entries
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3