P12821 (ACE_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Angiotensin-converting enzyme
Short name=ACE
EC=3.2.1.-
EC=3.4.15.1

Alternative name(s):
Dipeptidyl carboxypeptidase I
Kininase II
CD_antigen=CD143

Cleaved into the following chain:

1. Angiotensin-converting enzyme, soluble form

Gene names

Name:	ACE
Synonyms:	DCP, DCP1

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	1306 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein 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.
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. Isoform Testis-specific only binds 1 zinc ion per subunit. Binds 3 chloride ions per subunit.
Enzyme regulation	Strongly activated by chloride. Specifically inhibited by lisinopril, captopril and enalaprilat.
Subcellular location	Angiotensin-converting enzyme, soluble form: Secreted. Cell membrane; Single-pass type I membrane protein.
Tissue specificity	Ubiquitously expressed, with highest levels in lung, kidney, heart, gastrointestinal system and prostate. Isoform Testis-specific is expressed in spermatocytes and adult testis. Ref.15 Ref.16 Ref.19 Ref.22
Induction	Up-regulated in failing heart. Ref.21 Ref.22
Post-translational modification	Phosphorylated by CK2 on Ser-1299; which allows membrane retention. Ref.18
Involvement in disease	Ischemic stroke (ISCHSTR) [MIM:601367]: A stroke is an acute neurologic event leading to death of neural tissue of the brain and resulting in loss of motor, sensory and/or cognitive function. Ischemic strokes, resulting from vascular occlusion, is considered to be a highly complex disease consisting of a group of heterogeneous disorders with multiple genetic and environmental risk factors. Note: Disease susceptibility is associated with variations affecting the gene represented in this entry. Ref.33 Renal tubular dysgenesis (RTD) [MIM:267430]: Autosomal recessive severe disorder of renal tubular development characterized by persistent fetal anuria and perinatal death, probably due to pulmonary hypoplasia from early-onset oligohydramnios (the Potter phenotype). Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.35 Microvascular complications of diabetes 3 (MVCD3) [MIM:612624]: Pathological conditions that develop in numerous tissues and organs as a consequence of diabetes mellitus. They include diabetic retinopathy, diabetic nephropathy leading to end-stage renal disease, and diabetic neuropathy. Diabetic retinopathy remains the major cause of new-onset blindness among diabetic adults. It is characterized by vascular permeability and increased tissue ischemia and angiogenesis. Note: Disease susceptibility is associated with variations affecting the gene represented in this entry. Intracerebral hemorrhage (ICH) [MIM:614519]: A pathological condition characterized by bleeding into one or both cerebral hemispheres including the basal ganglia and the cerebral cortex. It is often associated with hypertension and craniocerebral trauma. Intracerebral bleeding is a common cause of stroke. Note: Disease susceptibility is associated with variations affecting the gene represented in this entry. Ref.34
Miscellaneous	Inhibitors of ACE are commonly used to treat hypertension and some types of renal and cardiac dysfunction. The glycosidase activity probably uses different active site residues than the metalloprotease activity.
Sequence similarities	Belongs to the peptidase M2 family.
Biophysicochemical properties	Kinetic parameters: KM=2.51 mM for Hip-His-Leu Ref.17 Ref.20
Sequence caution	The sequence BAD92208.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
Cellular component	Cell membrane Membrane Secreted
Coding sequence diversity	Alternative splicing Polymorphism
Domain	Repeat Signal Transmembrane Transmembrane helix
Ligand	Metal-binding Zinc
Molecular function	Carboxypeptidase Hydrolase Metalloprotease Protease
PTM	Disulfide bond Glycoprotein Phosphoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	angiotensin catabolic process in blood Inferred by curator PubMed 1668266. Source: UniProtKB angiotensin maturation Traceable author statement. Source: Reactome arachidonic acid secretion Inferred from direct assay PubMed 17077303. Source: BHF-UCL blood vessel remodeling Inferred by curator PubMed 1668266. Source: BHF-UCL cellular protein metabolic process Traceable author statement. Source: Reactome hematopoietic stem cell differentiation Inferred by curator PubMed 7876104. Source: BHF-UCL hormone catabolic process Inferred from direct assay PubMed 7876104. Source: BHF-UCL kidney development Inferred from mutant phenotype Ref.35. Source: BHF-UCL mononuclear cell proliferation Inferred by curator PubMed 7876104. Source: BHF-UCL peptide catabolic process Inferred from direct assay PubMed 4322742. Source: BHF-UCL proteolysis Inferred from electronic annotation. Source: UniProtKB-KW regulation of renal output by angiotensin Inferred by curator PubMed 1668266. Source: BHF-UCL regulation of smooth muscle cell migration Inferred from sequence or structural similarity. Source: BHF-UCL regulation of vasoconstriction Inferred by curator PubMed 1668266. Source: UniProtKB regulation of vasodilation Inferred by curator PubMed 4322742. Source: BHF-UCL
Cellular_component	endosome Inferred from direct assay PubMed 17077303. Source: BHF-UCL external side of plasma membrane Inferred from direct assay PubMed 9449382. Source: BHF-UCL extracellular space Inferred from direct assay PubMed 15283675. Source: UniProtKB integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW plasma membrane Inferred from direct assay PubMed 16186248. Source: UniProtKB
Molecular_function	actin binding Inferred from direct assay PubMed 16186248. Source: UniProtKB carboxypeptidase activity Inferred from electronic annotation. Source: UniProtKB-KW chloride ion binding Inferred from direct assay Ref.26. Source: BHF-UCL drug binding Inferred from direct assay PubMed 1320019. Source: BHF-UCL endopeptidase activity Inferred from direct assay PubMed 15283675. Source: UniProtKB metallopeptidase activity Inferred from direct assay PubMed 1320019PubMed 1668266PubMed 17077303Ref.1. Source: UniProtKB peptidyl-dipeptidase activity Inferred from direct assay PubMed 1320019PubMed 1668266PubMed 17077303Ref.1. Source: UniProtKB zinc ion binding Inferred from direct assay Ref.26. Source: BHF-UCL
Complete GO annotation...

Alternative products

This entry describes 4 isoforms produced by alternative splicing. [Align] [Select]

Isoform Somatic-1 (identifier: P12821-1)

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 Somatic-2 (identifier: P12821-2)

Also known as: Soluble;

The sequence of this isoform differs from the canonical sequence as follows:
     1137-1145: QFHEALCQA → HPFSQHTAA
     1146-1306: Missing.

Note: Incomplete sequence.

Isoform Testis-specific (identifier: P12821-3)

Also known as: ACE-T;

The sequence of this isoform differs from the canonical sequence as follows:
     1-574: Missing.
     575-641: AGSSRPWQEV...LPDNYPEGID → MGQGWATAGL...AHQTSAQSPN

Isoform 4 (identifier: P12821-4)

The sequence of this isoform differs from the canonical sequence as follows:
     1-67: MGAASGRRGP...EQVLFQSVAA → MGQGWATAGL...AHQTSAQSPN
     68-642: Missing.
     1128-1168: Missing.

Note: No experimental confirmation available.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 29

29

Ref.9

Chain

30 – 1306

1277

Angiotensin-converting enzyme

PRO_0000028530

Chain

30 – 1232

1203

Angiotensin-converting enzyme, soluble form

PRO_0000028531

Propeptide

1233 – 1306

74

Removed in soluble form

PRO_0000028532

Regions

Topological domain

30 – 1256

1227

Extracellular Potential

Transmembrane

1257 – 1277

21

Helical; Potential

Topological domain

1278 – 1306

29

Cytoplasmic Potential

Region

30 – 630

601

Peptidase M2 1

Region

631 – 1232

602

Peptidase M2 2

Sites

Active site

391

1

1

Active site

989

1

2

Metal binding

390

1

Zinc 1; catalytic

Metal binding

394

1

Zinc 1; catalytic

Metal binding

418

1

Zinc 1; catalytic

Metal binding

988

1

Zinc 2; catalytic

Metal binding

992

1

Zinc 2; catalytic

Metal binding

1016

1

Zinc 2; catalytic

Binding site

231

1

Chloride 1

Binding site

529

1

Chloride 1

Binding site

791

1

Chloride 2

Binding site

829

1

Chloride 3

Binding site

1090

1

Chloride 2

Binding site

1094

1

Chloride 2

Binding site

1127

1

Chloride 3

Site

1225

1

Not glycosylated

Amino acid modifications

Modified residue

1299

1

Phosphoserine Ref.18

Glycosylation

38

1

N-linked (GlcNAc...) Probable

Glycosylation

54

1

N-linked (GlcNAc...) Ref.13 Ref.28

Glycosylation

74

1

N-linked (GlcNAc...) Ref.28

Glycosylation

111

1

N-linked (GlcNAc...) Ref.13 Ref.24

Glycosylation

146

1

N-linked (GlcNAc...) Ref.13 Ref.28

Glycosylation

160

1

N-linked (GlcNAc...) Potential

Glycosylation

318

1

N-linked (GlcNAc...) Ref.28

Glycosylation

445

1

N-linked (GlcNAc...) Ref.24

Glycosylation

509

1

N-linked (GlcNAc...) Ref.13 Ref.23 Ref.28

Glycosylation

677

1

N-linked (GlcNAc...) Potential

Glycosylation

695

1

N-linked (GlcNAc...) (complex) Ref.13 Ref.23

Glycosylation

714

1

N-linked (GlcNAc...) (complex) Ref.13 Ref.23 Ref.24

Glycosylation

760

1

N-linked (GlcNAc...); partial Ref.13

Glycosylation

942

1

N-linked (GlcNAc...); partial Ref.13

Glycosylation

1191

1

N-linked (GlcNAc...); partial Ref.13

Disulfide bond

157 ↔ 165

Ref.12

Disulfide bond

757 ↔ 763

Ref.12

Disulfide bond

957 ↔ 975

Ref.12

Disulfide bond

1143 ↔ 1155

Ref.12

Natural variations

Alternative sequence

1 – 574

574

Missing in isoform Testis-specific.

VSP_035120

Alternative sequence

1 – 67

67

MGAAS…QSVAA → MGQGWATAGLPSLLFLLLCY GHPLLVPSQEASQQVTVTHG TSSQATTSSQTTTHQATAHQ TSAQSPN in isoform 4.

VSP_043522

Alternative sequence

68 – 642

575

Missing in isoform 4.

VSP_043523

Alternative sequence

575 – 641

67

AGSSR…PEGID → MGQGWATAGLPSLLFLLLCY GHPLLVPSQEASQQVTVTHG TSSQATTSSQTTTHQATAHQ TSAQSPN in isoform Testis-specific.

VSP_035121

Alternative sequence

1128 – 1168

41

Missing in isoform 4.

VSP_043524

Alternative sequence

1137 – 1145

9

QFHEALCQA → HPFSQHTAA in isoform Somatic-2.

VSP_029932

Alternative sequence

1146 – 1306

161

Missing in isoform Somatic-2.

VSP_029933

Natural variant

154

1

A → T.
Corresponds to variant rs13306087 [ dbSNP | Ensembl ].

VAR_029139

Natural variant

183

1

A → T.
Corresponds to variant rs12720754 [ dbSNP | Ensembl ].

VAR_029140

Natural variant

244

1

Y → C.
Corresponds to variant rs3730025 [ dbSNP | Ensembl ].

VAR_023430

Natural variant

260

1

R → C.
Corresponds to variant rs4302 [ dbSNP | Ensembl ].

VAR_054000

Natural variant

260

1

R → L.
Corresponds to variant rs4303 [ dbSNP | Ensembl ].

VAR_054001

Natural variant

261

1

A → S. Ref.4
Corresponds to variant rs4303 [ dbSNP | Ensembl ].

VAR_011707

Natural variant

351

1

P → L.
Corresponds to variant rs2229839 [ dbSNP | Ensembl ].

VAR_023431

Natural variant

354

1

G → R. Ref.35
Corresponds to variant rs56394458 [ dbSNP | Ensembl ].

VAR_035434

Natural variant

379

1

R → Q.
Corresponds to variant rs13306085 [ dbSNP | Ensembl ].

VAR_029141

Natural variant

524

1

V → A.
Corresponds to variant rs12720746 [ dbSNP | Ensembl ].

VAR_029142

Natural variant

561

1

R → W. Ref.4
Corresponds to variant rs4314 [ dbSNP | Ensembl ].

VAR_011708

Natural variant

592

1

D → G.
Corresponds to variant rs12709426 [ dbSNP | Ensembl ].

VAR_020053

Natural variant

828

1

M → T.
Corresponds to variant rs13306091 [ dbSNP | Ensembl ].

VAR_034602

Natural variant

916

1

T → M.
Corresponds to variant rs3730043 [ dbSNP | Ensembl ].

VAR_023432

Natural variant

1018

1

I → T. Ref.30
Corresponds to variant rs4976 [ dbSNP | Ensembl ].

VAR_014189

Natural variant

1051

1

F → V. Ref.30
Corresponds to variant rs4977 [ dbSNP | Ensembl ].

VAR_014190

Natural variant

1187

1

T → M.
Corresponds to variant rs12709442 [ dbSNP | Ensembl ].

VAR_023433

Natural variant

1228

1

P → L No effect on activity; increases secretion; rate of solubilization is 2.5-fold higher than wild-type. Ref.17 Ref.31 Ref.32

VAR_023434

Natural variant

1279

1

R → Q. Ref.30
Corresponds to variant rs4980 [ dbSNP | Ensembl ].

VAR_014191

Natural variant

1286

1

R → S. Ref.4 Ref.30
Corresponds to variant rs4364 [ dbSNP | Ensembl ].

VAR_011709

Natural variant

1296

1

Q → P. Ref.30
Corresponds to variant rs4981 [ dbSNP | Ensembl ].

VAR_014192

Isoform Testis-specific:

Natural variant

32

1

S → P.
Corresponds to variant rs4317 [ dbSNP | Ensembl ].

Natural variant

49

1

S → G.
Corresponds to variant rs4318 [ dbSNP | Ensembl ].

Experimental info

Mutagenesis

1299

1

S → A: Abolishes phosphorylation and decreases membrane retention. Ref.18

Sequence conflict

35

1

Q → E AA sequence Ref.9

Sequence conflict

42

1

D → R AA sequence Ref.9

Secondary structure

1

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1306

Helix Strand Turn

Details...

Helix

32 – 34

3

Helix

43 – 72

30

Helix

77 – 105

29

Turn

106 – 108

3

Helix

109 – 111

3

Helix

115 – 124

10

Helix

128 – 131

4

Helix

134 – 153

20

Beta strand

155 – 157

3

Beta strand

165 – 167

3

Turn

168 – 170

3

Helix

171 – 178

8

Helix

182 – 216

35

Turn

217 – 219

3

Helix

223 – 229

7

Helix

236 – 266

31

Turn

268 – 270

3

Beta strand

281 – 284

4

Helix

291 – 293

3

Helix

294 – 297

4

Helix

309 – 315

7

Helix

319 – 332

14

Helix

340 – 345

6

Beta strand

352 – 354

3

Beta strand

362 – 365

4

Beta strand

367 – 370

4

Beta strand

372 – 375

4

Helix

382 – 400

19

Helix

406 – 408

3

Helix

414 – 428

15

Helix

431 – 436

6

Helix

447 – 461

15

Turn

462 – 464

3

Helix

465 – 479

15

Helix

485 – 487

3

Helix

488 – 500

13

Helix

514 – 517

4

Turn

519 – 524

6

Helix

528 – 547

20

Helix

554 – 556

3

Helix

563 – 575

13

Helix

581 – 589

9

Helix

597 – 617

21

Turn

634 – 637

4

Helix

646 – 675

30

Helix

680 – 704

25

Helix

709 – 711

3

Helix

715 – 724

10

Helix

728 – 731

4

Helix

734 – 753

20

Beta strand

755 – 757

3

Beta strand

759 – 761

3

Beta strand

763 – 765

3

Turn

766 – 768

3

Helix

769 – 776

8

Helix

780 – 793

14

Helix

795 – 798

4

Turn

799 – 801

3

Helix

802 – 815

14

Helix

821 – 826

6

Helix

827 – 829

3

Helix

834 – 844

11

Helix

846 – 864

19

Turn

866 – 868

3

Beta strand

879 – 882

4

Helix

889 – 891

3

Helix

892 – 895

4

Helix

906 – 912

7

Helix

917 – 930

14

Helix

938 – 943

6

Beta strand

945 – 947

3

Beta strand

950 – 952

3

Beta strand

960 – 963

4

Beta strand

965 – 968

4

Beta strand

970 – 973

4

Helix

980 – 998

19

Turn

999 – 1001

3

Helix

1004 – 1006

3

Helix

1012 – 1026

15

Helix

1029 – 1034

6

Helix

1045 – 1077

33

Turn

1083 – 1085

3

Helix

1086 – 1098

13

Helix

1112 – 1115

4

Turn

1117 – 1122

6

Helix

1126 – 1145

20

Helix

1152 – 1154

3

Helix

1161 – 1171

11

Turn

1172 – 1175

4

Helix

1179 – 1187

9

Beta strand

1188 – 1191

4

Helix

1195 – 1214

20

Sequences

	Sequence		Length	Mass (Da)
	Isoform Somatic-1 [UniParc]. Last modified October 1, 1989. Version 1. Checksum: 1B33BCA7301A26AA	FASTA	1,306	149,715
	10 20 30 40 50 60 MGAASGRRGP GLLLPLPLLL LLPPQPALAL DPGLQPGNFS ADEAGAQLFA QSYNSSAEQV 70 80 90 100 110 120 LFQSVAASWA HDTNITAENA RRQEEAALLS QEFAEAWGQK AKELYEPIWQ NFTDPQLRRI 130 140 150 160 170 180 IGAVRTLGSA NLPLAKRQQY NALLSNMSRI YSTAKVCLPN KTATCWSLDP DLTNILASSR 190 200 210 220 230 240 SYAMLLFAWE GWHNAAGIPL KPLYEDFTAL SNEAYKQDGF TDTGAYWRSW YNSPTFEDDL 250 260 270 280 290 300 EHLYQQLEPL YLNLHAFVRR ALHRRYGDRY INLRGPIPAH LLGDMWAQSW ENIYDMVVPF 310 320 330 340 350 360 PDKPNLDVTS TMLQQGWNAT HMFRVAEEFF TSLELSPMPP EFWEGSMLEK PADGREVVCH 370 380 390 400 410 420 ASAWDFYNRK DFRIKQCTRV TMDQLSTVHH EMGHIQYYLQ YKDLPVSLRR GANPGFHEAI 430 440 450 460 470 480 GDVLALSVST PEHLHKIGLL DRVTNDTESD INYLLKMALE KIAFLPFGYL VDQWRWGVFS 490 500 510 520 530 540 GRTPPSRYNF DWWYLRTKYQ GICPPVTRNE THFDAGAKFH VPNVTPYIRY FVSFVLQFQF 550 560 570 580 590 600 HEALCKEAGY EGPLHQCDIY RSTKAGAKLR KVLQAGSSRP WQEVLKDMVG LDALDAQPLL 610 620 630 640 650 660 KYFQPVTQWL QEQNQQNGEV LGWPEYQWHP PLPDNYPEGI DLVTDEAEAS KFVEEYDRTS 670 680 690 700 710 720 QVVWNEYAEA NWNYNTNITT ETSKILLQKN MQIANHTLKY GTQARKFDVN QLQNTTIKRI 730 740 750 760 770 780 IKKVQDLERA ALPAQELEEY NKILLDMETT YSVATVCHPN GSCLQLEPDL TNVMATSRKY 790 800 810 820 830 840 EDLLWAWEGW RDKAGRAILQ FYPKYVELIN QAARLNGYVD AGDSWRSMYE TPSLEQDLER 850 860 870 880 890 900 LFQELQPLYL NLHAYVRRAL HRHYGAQHIN LEGPIPAHLL GNMWAQTWSN IYDLVVPFPS 910 920 930 940 950 960 APSMDTTEAM LKQGWTPRRM FKEADDFFTS LGLLPVPPEF WNKSMLEKPT DGREVVCHAS 970 980 990 1000 1010 1020 AWDFYNGKDF RIKQCTTVNL EDLVVAHHEM GHIQYFMQYK DLPVALREGA NPGFHEAIGD 1030 1040 1050 1060 1070 1080 VLALSVSTPK HLHSLNLLSS EGGSDEHDIN FLMKMALDKI AFIPFSYLVD QWRWRVFDGS 1090 1100 1110 1120 1130 1140 ITKENYNQEW WSLRLKYQGL CPPVPRTQGD FDPGAKFHIP SSVPYIRYFV SFIIQFQFHE 1150 1160 1170 1180 1190 1200 ALCQAAGHTG PLHKCDIYQS KEAGQRLATA MKLGFSRPWP EAMQLITGQP NMSASAMLSY 1210 1220 1230 1240 1250 1260 FKPLLDWLRT ENELHGEKLG WPQYNWTPNS ARSEGPLPDS GRVSFLGLDL DAQQARVGQW 1270 1280 1290 1300 LLLFLGIALL VATLGLSQRL FSIRHRSLHR HSHGPQFGSE VELRHS
	Isoform Somatic-2 (Soluble) [UniParc]. Checksum: B7EED12CAB675583	FASTA	1,145	131,659
	10 20 30 40 50 60 MGAASGRRGP GLLLPLPLLL LLPPQPALAL DPGLQPGNFS ADEAGAQLFA QSYNSSAEQV 70 80 90 100 110 120 LFQSVAASWA HDTNITAENA RRQEEAALLS QEFAEAWGQK AKELYEPIWQ NFTDPQLRRI 130 140 150 160 170 180 IGAVRTLGSA NLPLAKRQQY NALLSNMSRI YSTAKVCLPN KTATCWSLDP DLTNILASSR 190 200 210 220 230 240 SYAMLLFAWE GWHNAAGIPL KPLYEDFTAL SNEAYKQDGF TDTGAYWRSW YNSPTFEDDL 250 260 270 280 290 300 EHLYQQLEPL YLNLHAFVRR ALHRRYGDRY INLRGPIPAH LLGDMWAQSW ENIYDMVVPF 310 320 330 340 350 360 PDKPNLDVTS TMLQQGWNAT HMFRVAEEFF TSLELSPMPP EFWEGSMLEK PADGREVVCH 370 380 390 400 410 420 ASAWDFYNRK DFRIKQCTRV TMDQLSTVHH EMGHIQYYLQ YKDLPVSLRR GANPGFHEAI 430 440 450 460 470 480 GDVLALSVST PEHLHKIGLL DRVTNDTESD INYLLKMALE KIAFLPFGYL VDQWRWGVFS 490 500 510 520 530 540 GRTPPSRYNF DWWYLRTKYQ GICPPVTRNE THFDAGAKFH VPNVTPYIRY FVSFVLQFQF 550 560 570 580 590 600 HEALCKEAGY EGPLHQCDIY RSTKAGAKLR KVLQAGSSRP WQEVLKDMVG LDALDAQPLL 610 620 630 640 650 660 KYFQPVTQWL QEQNQQNGEV LGWPEYQWHP PLPDNYPEGI DLVTDEAEAS KFVEEYDRTS 670 680 690 700 710 720 QVVWNEYAEA NWNYNTNITT ETSKILLQKN MQIANHTLKY GTQARKFDVN QLQNTTIKRI 730 740 750 760 770 780 IKKVQDLERA ALPAQELEEY NKILLDMETT YSVATVCHPN GSCLQLEPDL TNVMATSRKY 790 800 810 820 830 840 EDLLWAWEGW RDKAGRAILQ FYPKYVELIN QAARLNGYVD AGDSWRSMYE TPSLEQDLER 850 860 870 880 890 900 LFQELQPLYL NLHAYVRRAL HRHYGAQHIN LEGPIPAHLL GNMWAQTWSN IYDLVVPFPS 910 920 930 940 950 960 APSMDTTEAM LKQGWTPRRM FKEADDFFTS LGLLPVPPEF WNKSMLEKPT DGREVVCHAS 970 980 990 1000 1010 1020 AWDFYNGKDF RIKQCTTVNL EDLVVAHHEM GHIQYFMQYK DLPVALREGA NPGFHEAIGD 1030 1040 1050 1060 1070 1080 VLALSVSTPK HLHSLNLLSS EGGSDEHDIN FLMKMALDKI AFIPFSYLVD QWRWRVFDGS 1090 1100 1110 1120 1130 1140 ITKENYNQEW WSLRLKYQGL CPPVPRTQGD FDPGAKFHIP SSVPYIRYFV SFIIQFHPFS QHTAA
	Isoform Testis-specific (ACE-T) [UniParc] [UniParc]. Checksum: 80E0D19CFA642313	FASTA	732	83,330
	10 20 30 40 50 60 MGQGWATAGL PSLLFLLLCY GHPLLVPSQE ASQQVTVTHG TSSQATTSSQ TTTHQATAHQ 70 80 90 100 110 120 TSAQSPNLVT DEAEASKFVE EYDRTSQVVW NEYAEANWNY NTNITTETSK ILLQKNMQIA 130 140 150 160 170 180 NHTLKYGTQA RKFDVNQLQN TTIKRIIKKV QDLERAALPA QELEEYNKIL LDMETTYSVA 190 200 210 220 230 240 TVCHPNGSCL QLEPDLTNVM ATSRKYEDLL WAWEGWRDKA GRAILQFYPK YVELINQAAR 250 260 270 280 290 300 LNGYVDAGDS WRSMYETPSL EQDLERLFQE LQPLYLNLHA YVRRALHRHY GAQHINLEGP 310 320 330 340 350 360 IPAHLLGNMW AQTWSNIYDL VVPFPSAPSM DTTEAMLKQG WTPRRMFKEA DDFFTSLGLL 370 380 390 400 410 420 PVPPEFWNKS MLEKPTDGRE VVCHASAWDF YNGKDFRIKQ CTTVNLEDLV VAHHEMGHIQ 430 440 450 460 470 480 YFMQYKDLPV ALREGANPGF HEAIGDVLAL SVSTPKHLHS LNLLSSEGGS DEHDINFLMK 490 500 510 520 530 540 MALDKIAFIP FSYLVDQWRW RVFDGSITKE NYNQEWWSLR LKYQGLCPPV PRTQGDFDPG 550 560 570 580 590 600 AKFHIPSSVP YIRYFVSFII QFQFHEALCQ AAGHTGPLHK CDIYQSKEAG QRLATAMKLG 610 620 630 640 650 660 FSRPWPEAMQ LITGQPNMSA SAMLSYFKPL LDWLRTENEL HGEKLGWPQY NWTPNSARSE 670 680 690 700 710 720 GPLPDSGRVS FLGLDLDAQQ ARVGQWLLLF LGIALLVATL GLSQRLFSIR HRSLHRHSHG 730 PQFGSEVELR HS
	Isoform 4 [UniParc]. Checksum: C7FED633D33129B0	FASTA	690	78,581
	10 20 30 40 50 60 MGQGWATAGL PSLLFLLLCY GHPLLVPSQE ASQQVTVTHG TSSQATTSSQ TTTHQATAHQ 70 80 90 100 110 120 TSAQSPNVTD EAEASKFVEE YDRTSQVVWN EYAEANWNYN TNITTETSKI LLQKNMQIAN 130 140 150 160 170 180 HTLKYGTQAR KFDVNQLQNT TIKRIIKKVQ DLERAALPAQ ELEEYNKILL DMETTYSVAT 190 200 210 220 230 240 VCHPNGSCLQ LEPDLTNVMA TSRKYEDLLW AWEGWRDKAG RAILQFYPKY VELINQAARL 250 260 270 280 290 300 NGYVDAGDSW RSMYETPSLE QDLERLFQEL QPLYLNLHAY VRRALHRHYG AQHINLEGPI 310 320 330 340 350 360 PAHLLGNMWA QTWSNIYDLV VPFPSAPSMD TTEAMLKQGW TPRRMFKEAD DFFTSLGLLP 370 380 390 400 410 420 VPPEFWNKSM LEKPTDGREV VCHASAWDFY NGKDFRIKQC TTVNLEDLVV AHHEMGHIQY 430 440 450 460 470 480 FMQYKDLPVA LREGANPGFH EAIGDVLALS VSTPKHLHSL NLLSSEGGSD EHDINFLMKM 490 500 510 520 530 540 ALDKIAFIPF SYLVDQWRWR VFDGSITKEN YNQEWWSLRL KYQGLCPPVP RTQGDFDPGA 550 560 570 580 590 600 KFHIPSSVPY IRTAMKLGFS RPWPEAMQLI TGQPNMSASA MLSYFKPLLD WLRTENELHG 610 620 630 640 650 660 EKLGWPQYNW TPNSARSEGP LPDSGRVSFL GLDLDAQQAR VGQWLLLFLG IALLVATLGL 670 680 690 SQRLFSIRHR SLHRHSHGPQ FGSEVELRHS

References

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[1]	"Two putative active centers in human angiotensin I-converting enzyme revealed by molecular cloning." Soubrier F., Alhenc-Gelas F., Hubert C., Allegrini J., John M., Tregear G., Corbol P. Proc. Natl. Acad. Sci. U.S.A. 85:9386-9390(1988) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM SOMATIC-1).
[2]	"The testicular transcript of the angiotensin I-converting enzyme encodes for the ancestral, non-duplicated form of the enzyme." Lattion A.L., Soubrier F., Allegrini J., Hubert C., Corvol P., Alhenc-Gelas F. FEBS Lett. 252:99-104(1989) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM TESTIS-SPECIFIC).
[3]	"Molecular cloning of human testicular angiotensin-converting enzyme: the testis isozyme is identical to the C-terminal half of endothelial angiotensin-converting enzyme." Ehlers M.R.W., Fox E.A., Strydom D.J., Riordan J.F. Proc. Natl. Acad. Sci. U.S.A. 86:7741-7745(1989) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM TESTIS-SPECIFIC).
[4]	"Sequence variation in the human angiotensin converting enzyme." Rieder M.J., Taylor S.L., Clark A.G., Nickerson D.A. Nat. Genet. 22:59-62(1999) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS SER-261; TRP-561 AND SER-1286.
[5]	"Complete sequencing and characterization of 21,243 full-length human cDNAs." Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S. Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4). Tissue: Testis.
[6]	NHLBI resequencing and genotyping service (RS&G) Submitted (DEC-2007) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[7]	Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S., Ohara O., Nagase T., Kikuno R.F. Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-1239 (ISOFORM SOMATIC-1). Tissue: Brain.
[8]	"DNA sequence of human chromosome 17 and analysis of rearrangement in the human lineage." Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R., Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A., Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J., Chang J.L. , Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J., DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S., Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E., Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K., LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J., Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A., Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K., Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D., Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A., Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C. Nature 440:1045-1049(2006) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[9]	"Purification of human lung angiotensin-converting enzyme by high-performance liquid chromatography: properties and N-terminal amino acid sequence." Takeuchi K., Shimizu T., Ohishi N., Seyama Y., Takaku F., Yotsumoto H. J. Biochem. 106:442-445(1989) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 30-46. Tissue: Lung.
[10]	"Alternative splicing of the mRNA coding for the human endothelial angiotensin-converting enzyme: a new mechanism for solubilization." Sugimura K., Tian X.-L., Hoffmann S., Ganten D., Bader M. Biochem. Biophys. Res. Commun. 247:466-472(1998) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1114-1306 (ISOFORM SOMATIC-2), ALTERNATIVE SPLICING. Tissue: Umbilical vein endothelial cell.
[11]	"Angiotensin-converting enzyme: zinc- and inhibitor-binding stoichiometries of the somatic and testis isozymes." Ehlers M.R.W., Riordan J.F. Biochemistry 30:7118-7126(1991) [PubMed] [Europe PMC] [Abstract] Cited for: ZINC-BINDING.
[12]	"Assignment of free and disulfide-bonded cysteine residues in testis angiotensin-converting enzyme: functional implications." Sturrock E.D., Yu X.C., Wu Z., Biemann K., Riordan J.F. Biochemistry 35:9560-9566(1996) [PubMed] [Europe PMC] [Abstract] Cited for: DISULFIDE BONDS.
[13]	"Identification of N-linked glycosylation sites in human testis angiotensin-converting enzyme and expression of an active deglycosylated form." Yu X.C., Sturrock E.D., Wu Z., Biemann K., Ehlers M.R.W., Riordan J.F. J. Biol. Chem. 272:3511-3519(1997) [PubMed] [Europe PMC] [Abstract] Cited for: GLYCOSYLATION AT ASN-38; ASN-54; ASN-111; ASN-146; ASN-509; ASN-695; ASN-714; ASN-760; ASN-942 AND ASN-1191, MASS SPECTROMETRY.
[14]	"Shedding of somatic angiotensin-converting enzyme (ACE) is inefficient compared with testis ACE despite cleavage at identical stalk sites." Woodman Z.L., Oppong S.Y., Cook S., Hooper N.M., Schwager S.L.U., Brandt W.F., Ehlers M.R.W., Sturrock E.D. Biochem. J. 347:711-718(2000) [PubMed] [Europe PMC] [Abstract] Cited for: CLEAVAGE SITE, MASS SPECTROMETRY.
[15]	"A novel angiotensin-converting enzyme-related carboxypeptidase (ACE2) converts angiotensin I to angiotensin 1-9." Donoghue M., Hsieh F., Baronas E., Godbout K., Gosselin M., Stagliano N., Donovan M., Woolf B., Robison K., Jeyaseelan R., Breitbart R.E., Acton S. Circ. Res. 87:E1-E9(2000) [PubMed] [Europe PMC] [Abstract] Cited for: TISSUE SPECIFICITY.
[16]	"A human homolog of angiotensin-converting enzyme. Cloning and functional expression as a captopril-insensitive carboxypeptidase." Tipnis S.R., Hooper N.M., Hyde R., Karran E., Christie G., Turner A.J. J. Biol. Chem. 275:33238-33243(2000) [PubMed] [Europe PMC] [Abstract] Cited for: TISSUE SPECIFICITY.
[17]	"Increased shedding of angiotensin-converting enzyme by a mutation identified in the stalk region." Eyries M., Michaud A., Deinum J., Agrapart M., Chomilier J., Kramers C., Soubrier F. J. Biol. Chem. 276:5525-5532(2001) [PubMed] [Europe PMC] [Abstract] Cited for: BIOPHYSICOCHEMICAL PROPERTIES, CHARACTERIZATION OF VARIANT LEU-1228.
[18]	"CK2 phosphorylates the angiotensin-converting enzyme and regulates its retention in the endothelial cell plasma membrane." Kohlstedt K., Shoghi F., Mueller-Esterl W., Busse R., Fleming I. Circ. Res. 91:749-756(2002) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION AT SER-1299, MUTAGENESIS OF SER-1299.
[19]	"Quantitative mRNA expression profiling of ACE 2, a novel homologue of angiotensin converting enzyme." Harmer D., Gilbert M., Borman R., Clark K.L. FEBS Lett. 532:107-110(2002) [PubMed] [Europe PMC] [Abstract] Cited for: TISSUE SPECIFICITY.
[20]	"Deglycosylation, processing and crystallization of human testis angiotensin-converting enzyme." Gordon K., Redelinghuys P., Schwager S.L.U., Ehlers M.R.W., Papageorgiou A.C., Natesh R., Acharya K.R., Sturrock E.D. Biochem. J. 371:437-442(2003) [PubMed] [Europe PMC] [Abstract] Cited for: BIOPHYSICOCHEMICAL PROPERTIES, CLEAVAGE SITE.
[21]	"ACE2 gene expression is up-regulated in the human failing heart." Goulter A.B., Goddard M.J., Allen J.C., Clark K.L. BMC Med. 2:19-19(2004) [PubMed] [Europe PMC] [Abstract] Cited for: INDUCTION.
[22]	"Myocardial infarction increases ACE2 expression in rat and humans." Burrell L.M., Risvanis J., Kubota E., Dean R.G., MacDonald P.S., Lu S., Tikellis C., Grant S.L., Lew R.A., Smith A.I., Cooper M.E., Johnston C.I. Eur. Heart J. 26:369-375(2005) [PubMed] [Europe PMC] [Abstract] Cited for: TISSUE SPECIFICITY, INDUCTION.
[23]	"Human plasma N-glycoproteome analysis by immunoaffinity subtraction, hydrazide chemistry, and mass spectrometry." Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E., Moore R.J., Smith R.D. J. Proteome Res. 4:2070-2080(2005) [PubMed] [Europe PMC] [Abstract] Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-509; ASN-695 AND ASN-714, MASS SPECTROMETRY. Tissue: Plasma.
[24]	"Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry." Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H. J. Proteome Res. 8:651-661(2009) [PubMed] [Europe PMC] [Abstract] Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-111; ASN-445 AND ASN-714, MASS SPECTROMETRY. Tissue: Liver.
[25]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[26]	"Crystal structure of the human angiotensin-converting enzyme-lisinopril complex." Natesh R., Schwager S.L.U., Sturrock E.D., Acharya K.R. Nature 421:551-554(2003) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 642-1230, X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 642-1230 IN COMPLEX WITH LISINOPRIL.
[27]	"Structural details on the binding of antihypertensive drugs captopril and enalaprilat to human testicular angiotensin I-converting enzyme." Natesh R., Schwager S.L.U., Evans H.R., Sturrock E.D., Acharya K.R. Biochemistry 43:8718-8724(2004) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 642-1230 IN COMPLEX WITH ENALAPRILAT, X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 642-1230 IN COMPLEX WITH CAPTOPRIL.
[28]	"Crystal structure of the N domain of human somatic angiotensin I-converting enzyme provides a structural basis for domain-specific inhibitor design." Corradi H.R., Schwager S.L.U., Nchinda A.T., Sturrock E.D., Acharya K.R. J. Mol. Biol. 357:964-974(2006) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 30-641 IN COMPLEX WITH LISINOPRIL; ZINC AND CHLORIDE IONS, GLYCOSYLATION AT ASN-54; ASN-74; ASN-146; ASN-318 AND ASN-509.
[29]	"The DD genotype of the ACE gene polymorphism is associated with progression of diabetic nephropathy to end stage renal failure in IDDM." Vleming L.J., van der Pijl J.W., Lemkes H.H.P.J., Westendorp R.G.J., Maassen J.A., Daha M.R., van Es L.A., van Kooten C. Clin. Nephrol. 51:133-140(1999) [PubMed] [Europe PMC] [Abstract] Cited for: INVOLVEMENT IN DIABETIC NEPHROPATHY SUSCEPTIBILITY.
[30]	"Patterns of single-nucleotide polymorphisms in candidate genes for blood-pressure homeostasis." Halushka M.K., Fan J.-B., Bentley K., Hsie L., Shen N., Weder A., Cooper R., Lipshutz R., Chakravarti A. Nat. Genet. 22:239-247(1999) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS THR-1018; VAL-1051; GLN-1279; SER-1286 AND PRO-1296.
[31]	"Point mutation in the stalk of angiotensin-converting enzyme causes a dramatic increase in serum angiotensin-converting enzyme but no cardiovascular disease." Kramers C., Danilov S.M., Deinum J., Balyasnikova I.V., Scharenborg N., Looman M., Boomsma F., de Keijzer M.H., van Duijn C., Martin S., Soubrier F., Adema G.J. Circulation 104:1236-1240(2001) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT LEU-1228, ASSOCIATION WITH BENIGN SERUM INCREASE OF ANGIOTENSIN-CONVERTING ENZYME.
[32]	"Hereditary elevation of angiotensin converting enzyme suggesting neurosarcoidosis." Linnebank M., Kesper K., Jeub M., Urbach H., Wuellner U., Klockgether T., Schmidt S. Neurology 61:1819-1820(2003) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT LEU-1228, ASSOCIATION WITH BENIGN SERUM INCREASE OF ANGIOTENSIN-CONVERTING ENZYME.
[33]	"Meta-analysis of genetic studies in ischemic stroke: thirty-two genes involving approximately 18,000 cases and 58,000 controls." Casas J.P., Hingorani A.D., Bautista L.E., Sharma P. Arch. Neurol. 61:1652-1661(2004) [PubMed] [Europe PMC] [Abstract] Cited for: INVOLVEMENT IN SUSCEPTIBILITY TO ISCHSTR.
[34]	"DD genotype of ACE gene is a risk factor for intracerebral hemorrhage." Slowik A., Turaj W., Dziedzic T., Haefele A., Pera J., Malecki M.T., Glodzik-Sobanska L., Szermer P., Figlewicz D.A., Szczudlik A. Neurology 63:359-361(2004) [PubMed] [Europe PMC] [Abstract] Cited for: INVOLVEMENT IN SUSCEPTIBILITY TO ICH.
[35]	"Mutations in genes in the renin-angiotensin system are associated with autosomal recessive renal tubular dysgenesis." Gribouval O., Gonzales M., Neuhaus T., Aziza J., Bieth E., Laurent N., Bouton J.M., Feuillet F., Makni S., Ben Amar H., Laube G., Delezoide A.-L., Bouvier R., Dijoud F., Ollagnon-Roman E., Roume J., Joubert M., Antignac C., Gubler M.-C. Nat. Genet. 37:964-968(2005) [PubMed] [Europe PMC] [Abstract] Cited for: INVOLVEMENT IN RTD, VARIANT ARG-354.
+	Additional computationally mapped references.

Web resources

GeneReviews

SHMPD

The Singapore human mutation and polymorphism database

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

J04144 mRNA. Translation: AAA51684.1.
M26657 mRNA. Translation: AAA60611.1.
X16295 mRNA. Translation: CAA34362.1.
AF118569 Genomic DNA. Translation: AAD28560.1.
AY436326 Genomic DNA. Translation: AAR03504.1.
AK301988 mRNA. Translation: BAG63395.1.
EU332840 Genomic DNA. Translation: ABY87529.1.
AB208971 mRNA. Translation: BAD92208.1. Different initiation.
AC113554 Genomic DNA. No translation available.

IPI

IPI00028147.
IPI00437751.
IPI00877100.
IPI00909226.

PIR

A31759.
PW0053.
S05238.

RefSeq

NP_000780.1. NM_000789.3.
NP_001171528.1. NM_001178057.1.
NP_690043.1. NM_152830.2.

UniGene

Hs.298469.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1O86	X-ray	2.00	A	642-1230	[»]
1O8A	X-ray	2.00	A	642-1230	[»]
1UZE	X-ray	1.82	A	642-1230	[»]
1UZF	X-ray	2.00	A	642-1230	[»]
2C6F	X-ray	3.01	A/B	30-641	[»]
2C6N	X-ray	3.00	A/B	30-641	[»]
2IUL	X-ray	2.01	A	642-1232	[»]
2IUX	X-ray	2.80	A	642-1232	[»]
2OC2	X-ray	2.25	A	642-1232	[»]
2XY9	X-ray	1.97	A	645-1228	[»]
2XYD	X-ray	2.15	A/B	30-639	[»]
2YDM	X-ray	2.44	A	642-1230	[»]
3BKK	X-ray	2.17	A	642-1232	[»]
3BKL	X-ray	2.18	A	642-1232	[»]
3L3N	X-ray	2.30	A	642-1232	[»]
3NXQ	X-ray	1.99	A/B	30-657	[»]
4APH	X-ray	1.99	A	642-1230	[»]
4APJ	X-ray	2.60	A	642-1230	[»]

ProteinModelPortal

P12821.

ModBase

Search...

Protein-protein interaction databases

MINT

MINT-127316.

STRING

9606.ENSP00000290866.

Protein family/group databases

MEROPS

M02.001.

PTM databases

PhosphoSite

P12821.

Polymorphism databases

DMDM

113045.

Proteomic databases

PaxDb

P12821.

PeptideAtlas

P12821.

PRIDE

P12821.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000290863; ENSP00000290863; ENSG00000159640.
ENST00000290866; ENSP00000290866; ENSG00000159640.
ENST00000413513; ENSP00000392247; ENSG00000159640.
ENST00000428043; ENSP00000397593; ENSG00000159640.

GeneID

1636.

KEGG

hsa:1636.

UCSC

uc002jau.2. human.
uc002jav.2. human.
uc010wpj.2. human.

Organism-specific databases

CTD

1636.

GeneCards

GC17P061554.

HGNC

HGNC:2707. ACE.

HPA

CAB002426.
CAB002921.
HPA029298.

MIM

106180. gene+phenotype.
267430. phenotype.
601367. phenotype.
612624. phenotype.
614519. phenotype.

neXtProt

NX_P12821.

Orphanet

97369. Renal tubular dysgenesis of genetic origin.

PharmGKB

PA139.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG71044.

HOGENOM

HOG000292210.

HOVERGEN

HBG000264.

InParanoid

P12821.

KO

K01283.

OMA

MEQLFTV.

OrthoDB

EOG495ZQZ.

PhylomeDB

P12821.

Enzyme and pathway databases

BioCyc

MetaCyc:HS08412-MONOMER.

BRENDA

3.4.15.1. 2681.

Reactome

REACT_17015. Metabolism of proteins.

SABIO-RK

P12821.

SignaLink

P12821.

Gene expression databases

ArrayExpress

P12821.

Bgee

P12821.

CleanEx

HS_ACE.

Genevestigator

P12821.

GermOnline

ENSG00000159640. Homo sapiens.

Family and domain databases

InterPro

IPR001548. Peptidase_M2.
[Graphical view]

PANTHER

PTHR10514. PTHR10514. 1 hit.

Pfam

PF01401. Peptidase_M2. 2 hits.
[Graphical view]

PRINTS

PR00791. PEPDIPTASEA.

PROSITE

PS00142. ZINC_PROTEASE. 2 hits.
[Graphical view]

ProtoNet

Search...

Other

BindingDB

P12821.

ChEMBL

CHEMBL1808.

DrugBank

DB00542. Benazepril.
DB01197. Captopril.
DB01089. Deserpidine.
DB00584. Enalapril.
DB00492. Fosinopril.
DB00722. Lisinopril.
DB00691. Moexipril.
DB00790. Perindopril.
DB00881. Quinapril.
DB00178. Ramipril.
DB01180. Rescinnamine.
DB01348. Spirapril.
DB00519. Trandolapril.

EvolutionaryTrace

P12821.

GenomeRNAi

1636.

NextBio

6722.

PMAP-CutDB

P12821.

SOURCE

Search...

Entry information

Entry name

ACE_HUMAN

Accession

Primary (citable) accession number: P12821
Secondary accession number(s): B0LPF0 , B4DXI3, E7EU16, P22966, Q53YX9, Q59GY8, Q7M4L4

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1989
Last sequence update:	October 1, 1989
Last modified:	May 29, 2013
This is version 174 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.