Reviewed, UniProtKB/Swiss-Prot Q50JE5 (ACE_MESAU)

Names and origin

Protein names

Recommended name:
    Angiotensin-converting enzyme
      Short name=ACE
    EC=3.4.15.1
    EC=3.2.1.-
Alternative name(s):
    Dipeptidyl carboxypeptidase I
    Kininase II
    CD_antigen=CD143
Cleaved into the following chain:
    1- Recommended name:
            Angiotensin-converting enzyme, soluble form

Gene names

Name:	Ace
Synonyms:	Dcp1

Organism

Mesocricetus auratus (Golden hamster)

Taxonomic identifier

10036 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Cricetidae › Cricetinae › Mesocricetus

Protein attributes

Sequence length	1314 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at transcript level.

General annotation (Comments)

Function	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.
Catalytic activity	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.
Cofactor	Binds 2 zinc ions per subunit By similarity. Binds 3 chloride ions per subunit By similarity.
Subcellular location	Angiotensin-converting enzyme, soluble form: Secreted By similarity. Cell membrane; Single-pass type I membrane protein By similarity.
Tissue specificity	Widely expressed with dominant expression in lung and kidney. Ref.1
Post-translational modification	Phosphorylated by CK2 on Ser-1307; which allows membrane retention By similarity.
Sequence similarities	Belongs to the peptidase M2 family.

Ontologies

Keywords
Cellular component	Cell membrane Membrane Secreted
Coding sequence diversity	Alternative splicing
Domain	Repeat Signal Transmembrane
Ligand	Metal-binding Zinc
Molecular function	Carboxypeptidase Hydrolase Metalloprotease Protease
PTM	Disulfide bond Glycoprotein Phosphoprotein
Gene Ontology (GO)
Biological process	proteolysis Inferred from electronic annotation. Source: InterPro
Cellular component	extracellular region Inferred from electronic annotation. Source: UniProtKB-KW integral to membrane Inferred from electronic annotation. Source: UniProtKB-SubCell plasma membrane Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	carboxypeptidase activity Inferred from electronic annotation. Source: UniProtKB-KW metallopeptidase activity Inferred from electronic annotation. Source: UniProtKB-KW peptidyl-dipeptidase activity Inferred from electronic annotation. Source: InterPro zinc ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Select]

Isoform Somatic (identifier: Q50JE5-1)

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.

Isoform Testis-specific (identifier: Q50JE5-2)

Also known as: ACE-T;

The sequence of this isoform is not available.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 35	35	By similarity
	Chain	36 – 1314	1279	Angiotensin-converting enzyme		PRO_0000028536
	Chain	36 – 1238	1203	Angiotensin-converting enzyme, soluble form		PRO_0000028537
	Propeptide	1239 – 1314	76	Removed in secreted form By similarity		PRO_0000028538
Regions
	Topological domain	36 – 1265	1230	Extracellular Potential
	Transmembrane	1266 – 1282	17	Potential
	Topological domain	1283 – 1314	32	Cytoplasmic Potential
	Region	36 – 636	601	Peptidase M2 1
	Region	637 – 1238	602	Peptidase M2 2
Sites
	Active site	397	1	1 By similarity
	Active site	995	1	2 By similarity
	Metal binding	396	1	Zinc 1; catalytic By similarity
	Metal binding	400	1	Zinc 1; catalytic By similarity
	Metal binding	424	1	Zinc 1; catalytic By similarity
	Metal binding	994	1	Zinc 2; catalytic By similarity
	Metal binding	998	1	Zinc 2; catalytic By similarity
	Metal binding	1022	1	Zinc 2; catalytic By similarity
	Binding site	237	1	Chloride 1 By similarity
	Binding site	535	1	Chloride 1 By similarity
	Binding site	797	1	Chloride 2 By similarity
	Binding site	835	1	Chloride 3 By similarity
	Binding site	1096	1	Chloride 2 By similarity
	Binding site	1100	1	Chloride 2 By similarity
	Binding site	1133	1	Chloride 3 By similarity
Amino acid modifications
	Modified residue	1307	1	Phosphoserine By similarity
	Glycosylation	44	1	N-linked (GlcNAc...) Potential
	Glycosylation	60	1	N-linked (GlcNAc...) Potential
	Glycosylation	80	1	N-linked (GlcNAc...) Potential
	Glycosylation	117	1	N-linked (GlcNAc...) Potential
	Glycosylation	166	1	N-linked (GlcNAc...) Potential
	Glycosylation	324	1	N-linked (GlcNAc...) Potential
	Glycosylation	515	1	N-linked (GlcNAc...) Potential
	Glycosylation	683	1	N-linked (GlcNAc...) Potential
	Glycosylation	701	1	N-linked (GlcNAc...) Potential
	Glycosylation	720	1	N-linked (GlcNAc...) Potential
	Glycosylation	766	1	N-linked (GlcNAc...) Potential
	Glycosylation	948	1	N-linked (GlcNAc...) Potential
	Glycosylation	1197	1	N-linked (GlcNAc...) Potential
	Disulfide bond	163 ↔ 171		By similarity
	Disulfide bond	763 ↔ 769		By similarity
	Disulfide bond	963 ↔ 981		By similarity
	Disulfide bond	1149 ↔ 1161		By similarity

Sequences

	Sequence		Length	Mass (Da)
	Isoform Somatic [UniParc]. Last modified June 7, 2005. Version 1. Checksum: 74E29238E87F157E	FASTA	1,314	151,595
	10 20 30 40 50 60 MGAASGQRGQ GPPSPLLLLW LSLLLLLLPP SPAPALDPGL QPGNFSADEI GAHLFAESYN 70 80 90 100 110 120 SSAEQVIFQS TVASWAYDTN MTEENARLQE EAELIWQEFA EVWGKKAKEL FDAIRQNFTD 130 140 150 160 170 180 SKLRRVIETI RTLGPANLPL ARRQQYNSLQ NNMNRIYSTS KVCLPNKTAT CWSLEPELTN 190 200 210 220 230 240 ILASSRSYAK LLFAWESWHD VVGIPLKPLY QDFTALSNEA YKQDGFSDTG AYWRSAYDSP 250 260 270 280 290 300 SFEETLEHLY HQLEPLYLNL HAYVRRALHR RYGDKYINLR GPIPAHLLGD MWAQSWDNIY 310 320 330 340 350 360 DMVVPFPNKP NLDVTNTMVQ KGWNVTHMFR VAEEFFTSMG LSPMPPEFWA ESMLEKPTDG 370 380 390 400 410 420 REVVCHASAW DFFNRKDFRI KQCTRITMEQ LSTVHHEMGH VQYYLQYKDL TVPLRRGANP 430 440 450 460 470 480 GFHEAIGDVL ALSVSTPAHL HKIGLLDRVA NDLESDINYL LKMALEKIAF LPFGYLVDQW 490 500 510 520 530 540 RWGVFSGHTP PSRYNFDWWY FRTKYQGICP PVVRNETHFD AGAKFHIPSG TPYIRYFVSF 550 560 570 580 590 600 ILQFQFHQAL CKEAGHQGPL HQCDIYQSTQ AGAKLQRVLQ AGYSRPWQEV LKEMVGSDTL 610 620 630 640 650 660 DAQALLEYFQ PVIRWLQEQN QRNGEVLGWP EYQWRPPLPD NYPEGIDLVT DETEAERFVE 670 680 690 700 710 720 EYDRTARVLW NEYAEANWQY NTNITLEASK ILLQKNKKVA NHTLKYGTLA KKFDVSNFQN 730 740 750 760 770 780 YTIKRIIKKV QNMDRAVLPP KELEEYNQIL MDMETTYSIA NVCYLNGTCL HLEPDLTNVM 790 800 810 820 830 840 ATSRKYEELL WVWKSWRDKV GRAILPLFPK YVELSNKIAH LNGYADGGDS WRSSYESKSL 850 860 870 880 890 900 EQDLEQLYQE LQPLYLNLHA YVRRSLHRHY GSQHINLDGP IPAHLLGNMW AQTWSNIYDL 910 920 930 940 950 960 VAPFPSAPNL DATEAMIKQG WTPRRIFKEA DDFFTSLGLL PVSEEFWNKS MLEKPGDGRE 970 980 990 1000 1010 1020 VVCHASAWDF YNGKDFRIKQ CTSVNMEDLV IAHHEMGHIQ YFMQYKDLPV TFREGANPGF 1030 1040 1050 1060 1070 1080 HEAIGDVLAL SVSTPKHLHS LNLLSSEGGG YEHDINFLMK MALDKIAFIP FSYLIDQWRW 1090 1100 1110 1120 1130 1140 RVFDGSITKE NYNQEWWSLR LKYQGLCPPV PRSQDDFDPG SKFHVPANVP YIRYFVSFII 1150 1160 1170 1180 1190 1200 QFQFHEALCR AAGHTGPLHK CDIYQSKEAG KLLADTMKMG YSKPWPEAMK LITGQPNMSA 1210 1220 1230 1240 1250 1260 SAMMNYFKPL TEWLVTENRR HGETLGWPEY NWTPNTARSE GPFPESGRVN FLGMYLEPQQ 1270 1280 1290 1300 1310 ARVGQWVLLF LGVSLLVATL GLTHRLFSIR QHGHSLHRPH RGPQFGSEVE LRHS
	Isoform Testis-specific (ACE-T) (Sequence not available).	FASTA	–	–

References

[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: 17343204] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AB212958 mRNA. Translation: BAD98304.1.
3D structure databases
SMR	Q50JE5. Positions 651-1228.
ModBase	Search...
Protein family/group databases
MEROPS	M02.001.
Phylogenomic databases
HOVERGEN	Q50JE5.
Enzyme and pathway databases
BRENDA	3.4.15.1. 824.
Family and domain databases
InterPro	IPR006025. Pept_M_Zn_BS. IPR001548. Peptidase_M2. [Graphical view]
PANTHER	PTHR10514. Peptidase_M2. 1 hit.
Pfam	PF01401. Peptidase_M2. 2 hits. [Graphical view]
PRINTS	PR00791. PEPDIPTASEA.
ProDom	PD004184. Peptidase_M2. 2 hits. [Graphical view] [Entries sharing at least one domain]
PROSITE	PS00142. ZINC_PROTEASE. 2 hits. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

ACE_MESAU

Accession

Primary (citable) accession number: Q50JE5

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 30, 2005
Last sequence update:	June 7, 2005
Last modified:	October 13, 2009
This is version 35 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)