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Protein

Angiotensin-converting enzyme

Gene

ACE

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: 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.

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+Note: Binds 2 Zn2+ ions per subunit.
  • chlorideNote: Binds 3 chloride ions per subunit.

Cofactori (for Isoform Testis-specific)

Zn2+Note: Isoform Testis-specific only binds 1 Zn2+ ion per subunit.

Enzyme regulationi

Strongly activated by chloride. Specifically inhibited by lisinopril, captopril and enalaprilat.

Kineticsi

  1. KM=2.51 mM for Hip-His-Leu2 Publications

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei231 – 2311Chloride 1
    Metal bindingi390 – 3901Zinc 1; catalytic1 Publication
    Active sitei391 – 39111
    Metal bindingi394 – 3941Zinc 1; catalytic1 Publication
    Metal bindingi418 – 4181Zinc 1; catalytic1 Publication
    Binding sitei529 – 5291Chloride 1
    Binding sitei791 – 7911Chloride 2
    Binding sitei829 – 8291Chloride 3
    Metal bindingi988 – 9881Zinc 2; catalytic1 Publication
    Active sitei989 – 98912
    Metal bindingi992 – 9921Zinc 2; catalytic1 Publication
    Metal bindingi1016 – 10161Zinc 2; catalytic1 Publication
    Binding sitei1090 – 10901Chloride 2
    Binding sitei1094 – 10941Chloride 2
    Binding sitei1127 – 11271Chloride 3
    Sitei1225 – 12251Not glycosylated

    GO - Molecular functioni

    • actin binding Source: UniProtKB
    • bradykinin receptor binding Source: BHF-UCL
    • carboxypeptidase activity Source: UniProtKB-KW
    • chloride ion binding Source: BHF-UCL
    • drug binding Source: BHF-UCL
    • endopeptidase activity Source: UniProtKB
    • exopeptidase activity Source: BHF-UCL
    • metallopeptidase activity Source: UniProtKB
    • mitogen-activated protein kinase binding Source: BHF-UCL
    • mitogen-activated protein kinase kinase binding Source: BHF-UCL
    • peptidyl-dipeptidase activity Source: UniProtKB
    • tripeptidyl-peptidase activity Source: BHF-UCL
    • zinc ion binding Source: BHF-UCL

    GO - Biological processi

    • angiotensin catabolic process in blood Source: UniProtKB
    • angiotensin maturation Source: Reactome
    • antigen processing and presentation of peptide antigen via MHC class I Source: BHF-UCL
    • arachidonic acid secretion Source: BHF-UCL
    • beta-amyloid metabolic process Source: BHF-UCL
    • blood vessel remodeling Source: BHF-UCL
    • cell proliferation in bone marrow Source: BHF-UCL
    • cellular protein metabolic process Source: Reactome
    • heart contraction Source: BHF-UCL
    • hematopoietic stem cell differentiation Source: BHF-UCL
    • hormone catabolic process Source: BHF-UCL
    • kidney development Source: BHF-UCL
    • mononuclear cell proliferation Source: BHF-UCL
    • negative regulation of gap junction assembly Source: BHF-UCL
    • neutrophil mediated immunity Source: BHF-UCL
    • peptide catabolic process Source: BHF-UCL
    • positive regulation of peptidyl-cysteine S-nitrosylation Source: BHF-UCL
    • positive regulation of peptidyl-tyrosine autophosphorylation Source: BHF-UCL
    • positive regulation of protein tyrosine kinase activity Source: BHF-UCL
    • regulation of angiotensin metabolic process Source: BHF-UCL
    • regulation of blood pressure Source: BHF-UCL
    • regulation of hematopoietic stem cell proliferation Source: BHF-UCL
    • regulation of renal output by angiotensin Source: BHF-UCL
    • regulation of smooth muscle cell migration Source: BHF-UCL
    • regulation of systemic arterial blood pressure by renin-angiotensin Source: UniProtKB
    • regulation of vasoconstriction Source: UniProtKB
    • regulation of vasodilation Source: BHF-UCL
    • spermatogenesis Source: BHF-UCL
    Complete GO annotation...

    Keywords - Molecular functioni

    Carboxypeptidase, Hydrolase, Metalloprotease, Protease

    Keywords - Ligandi

    Metal-binding, Zinc

    Enzyme and pathway databases

    BioCyciMetaCyc:HS08412-MONOMER.
    BRENDAi3.4.15.1. 2681.
    ReactomeiREACT_147707. Metabolism of Angiotensinogen to Angiotensins.
    SABIO-RKP12821.
    SignaLinkiP12821.

    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:DCP, DCP1
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640 Componenti: Chromosome 17

    Organism-specific databases

    HGNCiHGNC:2707. ACE.

    Subcellular locationi

    Topology

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini30 – 12561227ExtracellularSequence AnalysisAdd
    BLAST
    Transmembranei1257 – 127721HelicalSequence AnalysisAdd
    BLAST
    Topological domaini1278 – 130629CytoplasmicSequence AnalysisAdd
    BLAST

    GO - Cellular componenti

    • endosome Source: BHF-UCL
    • external side of plasma membrane Source: BHF-UCL
    • extracellular exosome Source: UniProtKB
    • extracellular region Source: Reactome
    • extracellular space Source: UniProtKB
    • integral component of membrane Source: UniProtKB-KW
    • lysosome Source: BHF-UCL
    • plasma membrane Source: BHF-UCL
    Complete GO annotation...

    Keywords - Cellular componenti

    Cell membrane, Cytoplasm, Membrane, Secreted

    Pathology & Biotechi

    Involvement in diseasei

    Ischemic stroke (ISCHSTR)1 Publication

    Disease susceptibility is associated with variations affecting the gene represented in this entry.

    Disease descriptionA 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.

    See also OMIM:601367
    Renal tubular dysgenesis (RTD)1 Publication

    The disease is caused by mutations affecting the gene represented in this entry.

    Disease descriptionAutosomal 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).

    See also OMIM:267430
    Microvascular complications of diabetes 3 (MVCD3)

    Disease susceptibility is associated with variations affecting the gene represented in this entry.

    Disease descriptionPathological 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.

    See also OMIM:612624
    Intracerebral hemorrhage (ICH)1 Publication

    Disease susceptibility is associated with variations affecting the gene represented in this entry.

    Disease descriptionA 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.

    See also OMIM:614519

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi1299 – 12991S → A: Abolishes phosphorylation and decreases membrane retention. 1 Publication

    Organism-specific databases

    MIMi106180. gene+phenotype.
    267430. phenotype.
    601367. phenotype.
    612624. phenotype.
    614519. phenotype.
    Orphaneti97369. Renal tubular dysgenesis of genetic origin.
    PharmGKBiPA139.

    Chemistry

    DrugBankiDB00542. Benazepril.
    DB00616. Candoxatril.
    DB01197. Captopril.
    DB01340. Cilazapril.
    DB00584. Enalapril.
    DB00492. Fosinopril.
    DB00722. Lisinopril.
    DB00691. Moexipril.
    DB00790. Perindopril.
    DB00881. Quinapril.
    DB00178. Ramipril.
    DB01180. Rescinnamine.
    DB01348. Spirapril.
    DB00519. Trandolapril.

    Polymorphism and mutation databases

    BioMutaiACE.
    DMDMi113045.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 29291 PublicationAdd
    BLAST
    Chaini30 – 13061277Angiotensin-converting enzymePRO_0000028530Add
    BLAST
    Chaini30 – 12321203Angiotensin-converting enzyme, soluble formPRO_0000028531Add
    BLAST
    Propeptidei1233 – 130674Removed in soluble formPRO_0000028532Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi38 – 381N-linked (GlcNAc...)1 Publication
    Glycosylationi54 – 541N-linked (GlcNAc...)2 Publications
    Glycosylationi74 – 741N-linked (GlcNAc...)1 Publication
    Glycosylationi111 – 1111N-linked (GlcNAc...)2 Publications
    Glycosylationi146 – 1461N-linked (GlcNAc...)2 Publications
    Disulfide bondi157 ↔ 1651 Publication
    Glycosylationi160 – 1601N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi318 – 3181N-linked (GlcNAc...)1 Publication
    Glycosylationi445 – 4451N-linked (GlcNAc...)1 Publication
    Glycosylationi509 – 5091N-linked (GlcNAc...)3 Publications
    Glycosylationi677 – 6771N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi695 – 6951N-linked (GlcNAc...) (complex)2 Publications
    Glycosylationi714 – 7141N-linked (GlcNAc...) (complex)3 Publications
    Disulfide bondi757 ↔ 7631 Publication
    Glycosylationi760 – 7601N-linked (GlcNAc...); partial1 Publication
    Glycosylationi942 – 9421N-linked (GlcNAc...); partial1 Publication
    Disulfide bondi957 ↔ 9751 Publication
    Disulfide bondi1143 ↔ 11551 Publication
    Glycosylationi1191 – 11911N-linked (GlcNAc...); partial1 Publication
    Modified residuei1299 – 12991Phosphoserine1 Publication

    Post-translational modificationi

    Phosphorylated by CK2 on Ser-1299; which allows membrane retention.1 Publication

    Keywords - PTMi

    Disulfide bond, Glycoprotein, Phosphoprotein

    Proteomic databases

    MaxQBiP12821.
    PaxDbiP12821.
    PeptideAtlasiP12821.
    PRIDEiP12821.

    PTM databases

    PhosphoSiteiP12821.

    Miscellaneous databases

    PMAP-CutDBP12821.

    Expressioni

    Tissue specificityi

    Ubiquitously expressed, with highest levels in lung, kidney, heart, gastrointestinal system and prostate. Isoform Testis-specific is expressed in spermatocytes and adult testis.4 Publications

    Inductioni

    Up-regulated in failing heart.2 Publications

    Gene expression databases

    BgeeiP12821.
    CleanExiHS_ACE.
    ExpressionAtlasiP12821. baseline and differential.
    GenevestigatoriP12821.

    Organism-specific databases

    HPAiCAB002426.
    CAB002921.
    HPA029298.

    Interactioni

    Protein-protein interaction databases

    BioGridi108004. 7 interactions.
    IntActiP12821. 1 interaction.
    MINTiMINT-127316.
    STRINGi9606.ENSP00000290866.

    Structurei

    Secondary structure

    1
    1306
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi32 – 343Combined sources
    Helixi43 – 7230Combined sources
    Helixi77 – 10529Combined sources
    Turni106 – 1083Combined sources
    Helixi109 – 1113Combined sources
    Helixi115 – 12410Combined sources
    Helixi128 – 1314Combined sources
    Helixi134 – 15320Combined sources
    Beta strandi155 – 1573Combined sources
    Beta strandi159 – 1613Combined sources
    Beta strandi165 – 1673Combined sources
    Turni168 – 1703Combined sources
    Helixi171 – 1788Combined sources
    Helixi182 – 21736Combined sources
    Helixi223 – 2297Combined sources
    Helixi236 – 26631Combined sources
    Turni268 – 2703Combined sources
    Beta strandi281 – 2844Combined sources
    Helixi291 – 2933Combined sources
    Helixi294 – 2974Combined sources
    Helixi309 – 3157Combined sources
    Helixi319 – 33214Combined sources
    Helixi340 – 3456Combined sources
    Beta strandi352 – 3543Combined sources
    Beta strandi362 – 3654Combined sources
    Beta strandi367 – 3704Combined sources
    Beta strandi372 – 3754Combined sources
    Helixi382 – 40120Combined sources
    Helixi406 – 4083Combined sources
    Helixi414 – 42815Combined sources
    Helixi431 – 4366Combined sources
    Helixi447 – 46115Combined sources
    Helixi464 – 47916Combined sources
    Helixi485 – 4873Combined sources
    Helixi488 – 50013Combined sources
    Helixi514 – 5174Combined sources
    Turni519 – 5246Combined sources
    Helixi528 – 54720Combined sources
    Helixi554 – 5563Combined sources
    Helixi563 – 57513Combined sources
    Helixi581 – 5899Combined sources
    Helixi597 – 61620Combined sources
    Turni634 – 6374Combined sources
    Helixi646 – 67530Combined sources
    Helixi680 – 70425Combined sources
    Helixi709 – 7113Combined sources
    Helixi715 – 72410Combined sources
    Helixi728 – 7314Combined sources
    Helixi734 – 75320Combined sources
    Beta strandi755 – 7573Combined sources
    Beta strandi759 – 7613Combined sources
    Beta strandi763 – 7653Combined sources
    Turni766 – 7683Combined sources
    Helixi769 – 7768Combined sources
    Helixi780 – 79314Combined sources
    Helixi795 – 7995Combined sources
    Helixi802 – 81514Combined sources
    Helixi821 – 8277Combined sources
    Helixi834 – 84411Combined sources
    Helixi846 – 86419Combined sources
    Helixi866 – 8683Combined sources
    Beta strandi879 – 8824Combined sources
    Helixi889 – 8913Combined sources
    Helixi892 – 8954Combined sources
    Helixi906 – 9127Combined sources
    Helixi917 – 93014Combined sources
    Helixi938 – 9436Combined sources
    Beta strandi945 – 9473Combined sources
    Beta strandi950 – 9523Combined sources
    Beta strandi960 – 9634Combined sources
    Beta strandi965 – 9684Combined sources
    Beta strandi970 – 9734Combined sources
    Helixi980 – 99819Combined sources
    Turni999 – 10013Combined sources
    Helixi1004 – 10063Combined sources
    Helixi1012 – 102615Combined sources
    Helixi1029 – 10346Combined sources
    Helixi1045 – 107733Combined sources
    Turni1083 – 10853Combined sources
    Helixi1086 – 109813Combined sources
    Helixi1112 – 11154Combined sources
    Turni1117 – 11226Combined sources
    Helixi1126 – 114520Combined sources
    Helixi1152 – 11543Combined sources
    Helixi1161 – 117111Combined sources
    Turni1172 – 11754Combined sources
    Helixi1179 – 11879Combined sources
    Beta strandi1188 – 11914Combined sources
    Helixi1195 – 121521Combined sources

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1O86X-ray2.00A642-1230[»]
    1O8AX-ray2.00A642-1230[»]
    1UZEX-ray1.82A642-1230[»]
    1UZFX-ray2.00A642-1230[»]
    2C6FX-ray3.01A/B30-641[»]
    2C6NX-ray3.00A/B30-641[»]
    2IULX-ray2.01A642-1232[»]
    2IUXX-ray2.80A642-1232[»]
    2OC2X-ray2.25A642-1232[»]
    2XY9X-ray1.97A645-1228[»]
    2XYDX-ray2.15A/B30-639[»]
    2YDMX-ray2.44A642-1230[»]
    3BKKX-ray2.17A642-1232[»]
    3BKLX-ray2.18A642-1232[»]
    3L3NX-ray2.30A642-1232[»]
    3NXQX-ray1.99A/B30-658[»]
    4APHX-ray1.99A642-1230[»]
    4APJX-ray2.60A642-1230[»]
    4BXKX-ray2.20A/B30-657[»]
    4BZRX-ray1.84A642-1230[»]
    4BZSX-ray2.10A/B30-657[»]
    4C2NX-ray2.59A642-1230[»]
    4C2OX-ray1.80A642-1230[»]
    4C2PX-ray1.99A642-1230[»]
    4C2QX-ray2.40A642-1230[»]
    4C2RX-ray2.30A642-1230[»]
    4CA5X-ray1.85A642-1230[»]
    4CA6X-ray1.91A/B30-639[»]
    ProteinModelPortaliP12821.
    SMRiP12821. Positions 30-641, 645-1230.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP12821.

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni30 – 630601Peptidase M2 1Add
    BLAST
    Regioni631 – 1232602Peptidase 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.
    InParanoidiP12821.
    KOiK01283.
    OrthoDBiEOG76HQ13.
    PhylomeDBiP12821.
    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 (4)i

    Sequence statusi: Complete.

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

    This entry describes 4 isoformsi produced by alternative splicing. AlignAdd to basket

    Isoform Somatic-1 (identifier: P12821-1) [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
    MGAASGRRGP GLLLPLPLLL LLPPQPALAL DPGLQPGNFS ADEAGAQLFA
    60 70 80 90 100
    QSYNSSAEQV LFQSVAASWA HDTNITAENA RRQEEAALLS QEFAEAWGQK
    110 120 130 140 150
    AKELYEPIWQ NFTDPQLRRI IGAVRTLGSA NLPLAKRQQY NALLSNMSRI
    160 170 180 190 200
    YSTAKVCLPN KTATCWSLDP DLTNILASSR SYAMLLFAWE GWHNAAGIPL
    210 220 230 240 250
    KPLYEDFTAL SNEAYKQDGF TDTGAYWRSW YNSPTFEDDL EHLYQQLEPL
    260 270 280 290 300
    YLNLHAFVRR ALHRRYGDRY INLRGPIPAH LLGDMWAQSW ENIYDMVVPF
    310 320 330 340 350
    PDKPNLDVTS TMLQQGWNAT HMFRVAEEFF TSLELSPMPP EFWEGSMLEK
    360 370 380 390 400
    PADGREVVCH ASAWDFYNRK DFRIKQCTRV TMDQLSTVHH EMGHIQYYLQ
    410 420 430 440 450
    YKDLPVSLRR GANPGFHEAI GDVLALSVST PEHLHKIGLL DRVTNDTESD
    460 470 480 490 500
    INYLLKMALE KIAFLPFGYL VDQWRWGVFS GRTPPSRYNF DWWYLRTKYQ
    510 520 530 540 550
    GICPPVTRNE THFDAGAKFH VPNVTPYIRY FVSFVLQFQF HEALCKEAGY
    560 570 580 590 600
    EGPLHQCDIY RSTKAGAKLR KVLQAGSSRP WQEVLKDMVG LDALDAQPLL
    610 620 630 640 650
    KYFQPVTQWL QEQNQQNGEV LGWPEYQWHP PLPDNYPEGI DLVTDEAEAS
    660 670 680 690 700
    KFVEEYDRTS QVVWNEYAEA NWNYNTNITT ETSKILLQKN MQIANHTLKY
    710 720 730 740 750
    GTQARKFDVN QLQNTTIKRI IKKVQDLERA ALPAQELEEY NKILLDMETT
    760 770 780 790 800
    YSVATVCHPN GSCLQLEPDL TNVMATSRKY EDLLWAWEGW RDKAGRAILQ
    810 820 830 840 850
    FYPKYVELIN QAARLNGYVD AGDSWRSMYE TPSLEQDLER LFQELQPLYL
    860 870 880 890 900
    NLHAYVRRAL HRHYGAQHIN LEGPIPAHLL GNMWAQTWSN IYDLVVPFPS
    910 920 930 940 950
    APSMDTTEAM LKQGWTPRRM FKEADDFFTS LGLLPVPPEF WNKSMLEKPT
    960 970 980 990 1000
    DGREVVCHAS AWDFYNGKDF RIKQCTTVNL EDLVVAHHEM GHIQYFMQYK
    1010 1020 1030 1040 1050
    DLPVALREGA NPGFHEAIGD VLALSVSTPK HLHSLNLLSS EGGSDEHDIN
    1060 1070 1080 1090 1100
    FLMKMALDKI AFIPFSYLVD QWRWRVFDGS ITKENYNQEW WSLRLKYQGL
    1110 1120 1130 1140 1150
    CPPVPRTQGD FDPGAKFHIP SSVPYIRYFV SFIIQFQFHE ALCQAAGHTG
    1160 1170 1180 1190 1200
    PLHKCDIYQS KEAGQRLATA MKLGFSRPWP EAMQLITGQP NMSASAMLSY
    1210 1220 1230 1240 1250
    FKPLLDWLRT ENELHGEKLG WPQYNWTPNS ARSEGPLPDS GRVSFLGLDL
    1260 1270 1280 1290 1300
    DAQQARVGQW LLLFLGIALL VATLGLSQRL FSIRHRSLHR HSHGPQFGSE

    VELRHS
    Length:1,306
    Mass (Da):149,715
    Last modified:October 1, 1989 - v1
    Checksum:i1B33BCA7301A26AA
    GO
    Isoform Somatic-2 (identifier: P12821-2) [UniParc]FASTAAdd to basket

    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.

    Show »
    Length:1,145
    Mass (Da):131,659
    Checksum:iB7EED12CAB675583
    GO
    Isoform Testis-specific (identifier: P12821-3) [UniParc] [UniParc]FASTAAdd to basket

    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

    Show »
    Length:732
    Mass (Da):83,330
    Checksum:i80E0D19CFA642313
    GO
    Isoform 4 (identifier: P12821-4) [UniParc]FASTAAdd to basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-641: MGAASGRRGP...LPDNYPEGID → MGQGWATAGL...AHQTSAQSPN
         1128-1168: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:691
    Mass (Da):78,694
    Checksum:iF31FE078F52FF0B2
    GO

    Sequence cautioni

    The sequence BAD92208.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti35 – 351Q → E AA sequence (PubMed:2558109).Curated
    Sequence conflicti42 – 421D → R AA sequence (PubMed:2558109).Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti154 – 1541A → T.
    Corresponds to variant rs13306087 [ dbSNP | Ensembl ].
    VAR_029139
    Natural varianti183 – 1831A → T.
    Corresponds to variant rs12720754 [ dbSNP | Ensembl ].
    VAR_029140
    Natural varianti244 – 2441Y → C.
    Corresponds to variant rs3730025 [ dbSNP | Ensembl ].
    VAR_023430
    Natural varianti260 – 2601R → C.
    Corresponds to variant rs4302 [ dbSNP | Ensembl ].
    VAR_054000
    Natural varianti260 – 2601R → L.
    Corresponds to variant rs4303 [ dbSNP | Ensembl ].
    VAR_054001
    Natural varianti261 – 2611A → S.1 Publication
    Corresponds to variant rs4303 [ dbSNP | Ensembl ].
    VAR_011707
    Natural varianti351 – 3511P → L.
    Corresponds to variant rs2229839 [ dbSNP | Ensembl ].
    VAR_023431
    Natural varianti354 – 3541G → R.1 Publication
    Corresponds to variant rs56394458 [ dbSNP | Ensembl ].
    VAR_035434
    Natural varianti379 – 3791R → Q.
    Corresponds to variant rs13306085 [ dbSNP | Ensembl ].
    VAR_029141
    Natural varianti524 – 5241V → A.
    Corresponds to variant rs12720746 [ dbSNP | Ensembl ].
    VAR_029142
    Natural varianti561 – 5611R → W.1 Publication
    Corresponds to variant rs4314 [ dbSNP | Ensembl ].
    VAR_011708
    Natural varianti592 – 5921D → G.
    Corresponds to variant rs12709426 [ dbSNP | Ensembl ].
    VAR_020053
    Natural varianti828 – 8281M → T.
    Corresponds to variant rs13306091 [ dbSNP | Ensembl ].
    VAR_034602
    Natural varianti916 – 9161T → M.
    Corresponds to variant rs3730043 [ dbSNP | Ensembl ].
    VAR_023432
    Natural varianti1018 – 10181I → T.1 Publication
    Corresponds to variant rs4976 [ dbSNP | Ensembl ].
    VAR_014189
    Natural varianti1051 – 10511F → V.1 Publication
    Corresponds to variant rs4977 [ dbSNP | Ensembl ].
    VAR_014190
    Natural varianti1187 – 11871T → M.
    Corresponds to variant rs12709442 [ dbSNP | Ensembl ].
    VAR_023433
    Natural varianti1228 – 12281P → L No effect on activity; increases secretion; rate of solubilization is 2.5-fold higher than wild-type. 3 Publications
    VAR_023434
    Natural varianti1279 – 12791R → Q.1 Publication
    Corresponds to variant rs4980 [ dbSNP | Ensembl ].
    VAR_014191
    Natural varianti1286 – 12861R → S.2 Publications
    Corresponds to variant rs4364 [ dbSNP | Ensembl ].
    VAR_011709
    Natural varianti1296 – 12961Q → P.1 Publication
    Corresponds to variant rs4981 [ dbSNP | Ensembl ].
    VAR_014192
    Isoform Testis-specific (identifier: P12821-3)
    Natural varianti32 – 321S → P.
    Corresponds to variant rs4317 [ dbSNP | Ensembl ].
    Natural varianti49 – 491S → G.
    Corresponds to variant rs4318 [ dbSNP | Ensembl ].

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 641641MGAAS…PEGID → MGQGWATAGLPSLLFLLLCY GHPLLVPSQEASQQVTVTHG TSSQATTSSQTTTHQATAHQ TSAQSPN in isoform 4. 1 PublicationVSP_054836Add
    BLAST
    Alternative sequencei1 – 574574Missing in isoform Testis-specific. 2 PublicationsVSP_035120Add
    BLAST
    Alternative sequencei575 – 64167AGSSR…PEGID → MGQGWATAGLPSLLFLLLCY GHPLLVPSQEASQQVTVTHG TSSQATTSSQTTTHQATAHQ TSAQSPN in isoform Testis-specific. 2 PublicationsVSP_035121Add
    BLAST
    Alternative sequencei1128 – 116841Missing in isoform 4. 1 PublicationVSP_054837Add
    BLAST
    Alternative sequencei1137 – 11459QFHEALCQA → HPFSQHTAA in isoform Somatic-2. 1 PublicationVSP_029932
    Alternative sequencei1146 – 1306161Missing in isoform Somatic-2. 1 PublicationVSP_029933Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    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.
    CCDSiCCDS11637.1. [P12821-1]
    CCDS45755.1. [P12821-3]
    CCDS54155.1. [P12821-4]
    PIRiA31759.
    PW0053.
    S05238.
    RefSeqiNP_000780.1. NM_000789.3. [P12821-1]
    NP_001171528.1. NM_001178057.1. [P12821-4]
    NP_690043.1. NM_152830.2. [P12821-3]
    UniGeneiHs.298469.

    Genome annotation databases

    EnsembliENST00000290863; ENSP00000290863; ENSG00000159640. [P12821-3]
    ENST00000290866; ENSP00000290866; ENSG00000159640. [P12821-1]
    ENST00000413513; ENSP00000392247; ENSG00000159640. [P12821-4]
    GeneIDi1636.
    KEGGihsa:1636.
    UCSCiuc002jau.2. human. [P12821-1]
    uc002jav.2. human. [P12821-3]

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Web resourcesi

    SHMPD

    The Singapore human mutation and polymorphism database

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    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.
    CCDSiCCDS11637.1. [P12821-1]
    CCDS45755.1. [P12821-3]
    CCDS54155.1. [P12821-4]
    PIRiA31759.
    PW0053.
    S05238.
    RefSeqiNP_000780.1. NM_000789.3. [P12821-1]
    NP_001171528.1. NM_001178057.1. [P12821-4]
    NP_690043.1. NM_152830.2. [P12821-3]
    UniGeneiHs.298469.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1O86X-ray2.00A642-1230[»]
    1O8AX-ray2.00A642-1230[»]
    1UZEX-ray1.82A642-1230[»]
    1UZFX-ray2.00A642-1230[»]
    2C6FX-ray3.01A/B30-641[»]
    2C6NX-ray3.00A/B30-641[»]
    2IULX-ray2.01A642-1232[»]
    2IUXX-ray2.80A642-1232[»]
    2OC2X-ray2.25A642-1232[»]
    2XY9X-ray1.97A645-1228[»]
    2XYDX-ray2.15A/B30-639[»]
    2YDMX-ray2.44A642-1230[»]
    3BKKX-ray2.17A642-1232[»]
    3BKLX-ray2.18A642-1232[»]
    3L3NX-ray2.30A642-1232[»]
    3NXQX-ray1.99A/B30-658[»]
    4APHX-ray1.99A642-1230[»]
    4APJX-ray2.60A642-1230[»]
    4BXKX-ray2.20A/B30-657[»]
    4BZRX-ray1.84A642-1230[»]
    4BZSX-ray2.10A/B30-657[»]
    4C2NX-ray2.59A642-1230[»]
    4C2OX-ray1.80A642-1230[»]
    4C2PX-ray1.99A642-1230[»]
    4C2QX-ray2.40A642-1230[»]
    4C2RX-ray2.30A642-1230[»]
    4CA5X-ray1.85A642-1230[»]
    4CA6X-ray1.91A/B30-639[»]
    ProteinModelPortaliP12821.
    SMRiP12821. Positions 30-641, 645-1230.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    BioGridi108004. 7 interactions.
    IntActiP12821. 1 interaction.
    MINTiMINT-127316.
    STRINGi9606.ENSP00000290866.

    Chemistry

    BindingDBiP12821.
    ChEMBLiCHEMBL1808.
    DrugBankiDB00542. Benazepril.
    DB00616. Candoxatril.
    DB01197. Captopril.
    DB01340. Cilazapril.
    DB00584. Enalapril.
    DB00492. Fosinopril.
    DB00722. Lisinopril.
    DB00691. Moexipril.
    DB00790. Perindopril.
    DB00881. Quinapril.
    DB00178. Ramipril.
    DB01180. Rescinnamine.
    DB01348. Spirapril.
    DB00519. Trandolapril.
    GuidetoPHARMACOLOGYi1613.

    Protein family/group databases

    MEROPSiM02.001.

    PTM databases

    PhosphoSiteiP12821.

    Polymorphism and mutation databases

    BioMutaiACE.
    DMDMi113045.

    Proteomic databases

    MaxQBiP12821.
    PaxDbiP12821.
    PeptideAtlasiP12821.
    PRIDEiP12821.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsembliENST00000290863; ENSP00000290863; ENSG00000159640. [P12821-3]
    ENST00000290866; ENSP00000290866; ENSG00000159640. [P12821-1]
    ENST00000413513; ENSP00000392247; ENSG00000159640. [P12821-4]
    GeneIDi1636.
    KEGGihsa:1636.
    UCSCiuc002jau.2. human. [P12821-1]
    uc002jav.2. human. [P12821-3]

    Organism-specific databases

    CTDi1636.
    GeneCardsiGC17P061554.
    HGNCiHGNC:2707. ACE.
    HPAiCAB002426.
    CAB002921.
    HPA029298.
    MIMi106180. gene+phenotype.
    267430. phenotype.
    601367. phenotype.
    612624. phenotype.
    614519. phenotype.
    neXtProtiNX_P12821.
    Orphaneti97369. Renal tubular dysgenesis of genetic origin.
    PharmGKBiPA139.
    GenAtlasiSearch...

    Phylogenomic databases

    eggNOGiNOG71044.
    GeneTreeiENSGT00520000055576.
    HOGENOMiHOG000007838.
    HOVERGENiHBG000264.
    InParanoidiP12821.
    KOiK01283.
    OrthoDBiEOG76HQ13.
    PhylomeDBiP12821.
    TreeFamiTF312861.

    Enzyme and pathway databases

    BioCyciMetaCyc:HS08412-MONOMER.
    BRENDAi3.4.15.1. 2681.
    ReactomeiREACT_147707. Metabolism of Angiotensinogen to Angiotensins.
    SABIO-RKP12821.
    SignaLinkiP12821.

    Miscellaneous databases

    EvolutionaryTraceiP12821.
    GeneWikiiAngiotensin-converting_enzyme.
    GenomeRNAii1636.
    NextBioi6722.
    PMAP-CutDBP12821.
    PROiP12821.
    SOURCEiSearch...

    Gene expression databases

    BgeeiP12821.
    CleanExiHS_ACE.
    ExpressionAtlasiP12821. baseline and differential.
    GenevestigatoriP12821.

    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]
    ProtoNetiSearch...

    Publicationsi

    « Hide 'large scale' publications
    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, IDENTIFICATION BY 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, IDENTIFICATION BY 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. 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.
      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.
      Tissue: Liver.
    25. 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. Cited for: INVOLVEMENT IN SUSCEPTIBILITY TO ICH.
    35. Cited for: INVOLVEMENT IN RTD, VARIANT ARG-354.

    Entry informationi

    Entry nameiACE_HUMAN
    AccessioniPrimary (citable) accession number: P12821
    Secondary accession number(s): B0LPF0
    , B4DXI3, E7EU16, P22966, Q53YX9, Q59GY8, Q7M4L4
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1989
    Last sequence update: October 1, 1989
    Last modified: May 27, 2015
    This is version 196 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny 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.

    Miscellaneousi

    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.

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Human cell differentiation molecules
      CD nomenclature of surface proteins of human leucocytes and list of entries
    2. Glycosyl hydrolases
      Classification of glycosyl hydrolase families and list of entries
    3. Human chromosome 17
      Human chromosome 17: entries, gene names and cross-references to MIM
    4. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    5. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    6. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    7. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    8. Peptidase families
      Classification of peptidase families and list of entries
    9. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3

    Similar proteinsi

    Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
    100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
    90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
    50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.