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Protein

Amiloride-sensitive amine oxidase [copper-containing]

Gene

AOC1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the degradation of compounds such as putrescine, histamine, spermine, and spermidine, substances involved in allergic and immune responses, cell proliferation, tissue differentiation, tumor formation, and possibly apoptosis. Placental DAO is thought to play a role in the regulation of the female reproductive function.

Catalytic activityi

Histamine + H2O + O2 = (imidazol-4-yl)acetaldehyde + NH3 + H2O2.1 Publication

Cofactori

Protein has several cofactor binding sites:

Enzyme regulationi

Inhibited by isoniazid, cimetidine, clonidine, pentamidine, berenil and pentamidine.1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei373Proton acceptor1 Publication1
Active sitei461Schiff-base intermediate with substrate; via topaquinoneCombined sources1 Publication1
Metal bindingi510Copper; via tele nitrogenCombined sources1 Publication1
Metal bindingi512Copper; via tele nitrogenCombined sources1 Publication1
Metal bindingi519Calcium 1Combined sources1 Publication1
Metal bindingi520Calcium 1; via carbonyl oxygenCombined sources1 Publication1
Metal bindingi521Calcium 1Combined sources1 Publication1
Metal bindingi562Calcium 2Combined sources1 Publication1
Metal bindingi653Calcium 2; via carbonyl oxygenCombined sources1 Publication1
Metal bindingi656Calcium 2Combined sources1 Publication1
Metal bindingi658Calcium 2Combined sources1 Publication1
Metal bindingi664Calcium 1Combined sources1 Publication1
Metal bindingi665Calcium 1; via carbonyl oxygenCombined sources1 Publication1
Metal bindingi675Copper; via pros nitrogenCombined sources1 Publication1

GO - Molecular functioni

  • calcium ion binding Source: UniProtKB
  • copper ion binding Source: UniProtKB
  • diamine oxidase activity Source: UniProtKB
  • drug binding Source: UniProtKB
  • heparin binding Source: UniProtKB
  • histamine oxidase activity Source: Reactome
  • methylputrescine oxidase activity Source: UniProtKB-EC
  • primary amine oxidase activity Source: UniProtKB
  • propane-1,3-diamine oxidase activity Source: UniProtKB-EC
  • protein complex binding Source: UniProtKB
  • protein homodimerization activity Source: UniProtKB
  • quinone binding Source: UniProtKB
  • receptor activity Source: UniProtKB
  • zinc ion binding Source: UniProtKB

GO - Biological processi

  • amine metabolic process Source: InterPro
  • cellular response to azide Source: UniProtKB
  • cellular response to copper ion Source: UniProtKB
  • cellular response to copper ion starvation Source: UniProtKB
  • cellular response to heparin Source: UniProtKB
  • cellular response to histamine Source: UniProtKB
  • oxidation-reduction process Source: UniProtKB
  • response to antibiotic Source: UniProtKB
  • response to drug Source: UniProtKB
  • xenobiotic metabolic process Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

Calcium, Copper, Heparin-binding, Metal-binding

Enzyme and pathway databases

BioCyciMetaCyc:HS00083-MONOMER.
ZFISH:HS00083-MONOMER.
BRENDAi1.4.3.22. 2681.
ReactomeiR-HSA-211945. Phase 1 - Functionalization of compounds.
R-HSA-6798695. Neutrophil degranulation.

Names & Taxonomyi

Protein namesi
Recommended name:
Amiloride-sensitive amine oxidase [copper-containing] (EC:1.4.3.221 Publication)
Short name:
DAO
Short name:
Diamine oxidase
Alternative name(s):
Amiloride-binding protein 1
Amine oxidase copper domain-containing protein 1
Histaminase
Kidney amine oxidase
Short name:
KAO
Gene namesi
Name:AOC1
Synonyms:ABP1, DAO1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 7

Organism-specific databases

HGNCiHGNC:80. AOC1.

Subcellular locationi

GO - Cellular componenti

  • bicellular tight junction Source: UniProtKB
  • extracellular exosome Source: UniProtKB
  • extracellular space Source: UniProtKB
  • peroxisome Source: UniProtKB
  • plasma membrane Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Organism-specific databases

DisGeNETi26.
OpenTargetsiENSG00000002726.
PharmGKBiPA24416.

Chemistry databases

ChEMBLiCHEMBL2118.
DrugBankiDB00594. Amiloride.

Polymorphism and mutation databases

DMDMi251757489.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 191 PublicationAdd BLAST19
ChainiPRO_000003566620 – 751Amiloride-sensitive amine oxidase [copper-containing]Add BLAST732

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi110N-linked (GlcNAc...)Combined sources1 Publication1
Glycosylationi168N-linked (GlcNAc...)PROSITE-ProRule annotation1
Disulfide bondi177 ↔ 181Combined sources1 Publication
Disulfide bondi391 ↔ 417Combined sources1 Publication
Modified residuei4612',4',5'-topaquinoneBy similarity1
Glycosylationi538N-linked (GlcNAc...)Combined sources1 Publication1
Disulfide bondi736InterchainCombined sources1 Publication
Glycosylationi745N-linked (GlcNAc...)Combined sources1 Publication1

Post-translational modificationi

Topaquinone (TPQ) is generated by copper-dependent autoxidation of a specific tyrosyl residue.By similarity

Keywords - PTMi

Disulfide bond, Glycoprotein, TPQ

Proteomic databases

PaxDbiP19801.
PeptideAtlasiP19801.
PRIDEiP19801.
TopDownProteomicsiP19801-1. [P19801-1]

PTM databases

iPTMnetiP19801.
PhosphoSitePlusiP19801.

Expressioni

Tissue specificityi

Placenta and kidney.

Gene expression databases

BgeeiENSG00000002726.
CleanExiHS_ABP1.
ExpressionAtlasiP19801. baseline and differential.
GenevisibleiP19801. HS.

Organism-specific databases

HPAiHPA031032.
HPA031033.

Interactioni

Subunit structurei

Homodimer; disulfide-linked.1 Publication

GO - Molecular functioni

  • protein complex binding Source: UniProtKB
  • protein homodimerization activity Source: UniProtKB

Protein-protein interaction databases

BioGridi106544. 1 interactor.
STRINGi9606.ENSP00000354193.

Chemistry databases

BindingDBiP19801.

Structurei

Secondary structure

1751
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi29 – 33Combined sources5
Helixi38 – 49Combined sources12
Helixi52 – 54Combined sources3
Beta strandi64 – 75Combined sources12
Helixi79 – 88Combined sources10
Beta strandi96 – 103Combined sources8
Beta strandi105 – 108Combined sources4
Beta strandi110 – 117Combined sources8
Beta strandi119 – 121Combined sources3
Beta strandi124 – 129Combined sources6
Helixi137 – 140Combined sources4
Helixi145 – 158Combined sources14
Helixi160 – 162Combined sources3
Helixi163 – 170Combined sources8
Beta strandi173 – 176Combined sources4
Beta strandi178 – 186Combined sources9
Beta strandi191 – 193Combined sources3
Beta strandi198 – 205Combined sources8
Helixi210 – 212Combined sources3
Beta strandi214 – 222Combined sources9
Beta strandi225 – 227Combined sources3
Helixi228 – 230Combined sources3
Beta strandi232 – 238Combined sources7
Helixi246 – 254Combined sources9
Beta strandi301 – 303Combined sources3
Beta strandi309 – 313Combined sources5
Beta strandi316 – 320Combined sources5
Beta strandi322 – 329Combined sources8
Turni330 – 332Combined sources3
Beta strandi333 – 341Combined sources9
Beta strandi344 – 359Combined sources16
Helixi364 – 368Combined sources5
Beta strandi370 – 372Combined sources3
Helixi373 – 376Combined sources4
Helixi378 – 380Combined sources3
Turni387 – 389Combined sources3
Beta strandi395 – 405Combined sources11
Beta strandi410 – 422Combined sources13
Beta strandi427 – 433Combined sources7
Beta strandi435 – 445Combined sources11
Beta strandi448 – 456Combined sources9
Beta strandi458 – 469Combined sources12
Beta strandi475 – 483Combined sources9
Beta strandi487 – 489Combined sources3
Helixi492 – 496Combined sources5
Beta strandi497 – 502Combined sources6
Beta strandi505 – 508Combined sources4
Beta strandi510 – 520Combined sources11
Beta strandi524 – 540Combined sources17
Beta strandi547 – 559Combined sources13
Helixi562 – 565Combined sources4
Beta strandi569 – 571Combined sources3
Beta strandi575 – 584Combined sources10
Beta strandi590 – 598Combined sources9
Helixi610 – 619Combined sources10
Beta strandi621 – 626Combined sources6
Helixi629 – 631Combined sources3
Turni637 – 641Combined sources5
Beta strandi643 – 645Combined sources3
Helixi652 – 655Combined sources4
Beta strandi661 – 675Combined sources15
Helixi679 – 681Combined sources3
Beta strandi691 – 704Combined sources14
Helixi706 – 709Combined sources4
Beta strandi714 – 717Combined sources4
Beta strandi720 – 723Combined sources4
Beta strandi725 – 727Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3HI7X-ray1.80A/B21-751[»]
3HIGX-ray2.09A/B21-751[»]
3HIIX-ray2.15A/B21-751[»]
3K5TX-ray2.11A21-751[»]
3MPHX-ray2.05A/B21-751[»]
ProteinModelPortaliP19801.
SMRiP19801.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP19801.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni371 – 381Substrate bindingCombined sources1 PublicationAdd BLAST11
Regioni458 – 463Substrate bindingCombined sources1 Publication6
Regioni568 – 575Heparin-bindingBy similarity8

Sequence similaritiesi

Belongs to the copper/topaquinone oxidase family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiKOG1186. Eukaryota.
COG3733. LUCA.
GeneTreeiENSGT00510000046461.
HOGENOMiHOG000233919.
HOVERGENiHBG004164.
InParanoidiP19801.
KOiK11182.
OMAiFNSNFKG.
OrthoDBiEOG091G0C1O.
PhylomeDBiP19801.
TreeFamiTF314750.

Family and domain databases

Gene3Di2.70.98.20. 1 hit.
InterProiIPR000269. Cu_amine_oxidase.
IPR015798. Cu_amine_oxidase_C.
IPR016182. Cu_amine_oxidase_N-reg.
IPR015800. Cu_amine_oxidase_N2.
IPR015802. Cu_amine_oxidase_N3.
[Graphical view]
PANTHERiPTHR10638. PTHR10638. 1 hit.
PfamiPF01179. Cu_amine_oxid. 1 hit.
PF02727. Cu_amine_oxidN2. 1 hit.
PF02728. Cu_amine_oxidN3. 1 hit.
[Graphical view]
PRINTSiPR00766. CUDAOXIDASE.
SUPFAMiSSF49998. SSF49998. 1 hit.
SSF54416. SSF54416. 2 hits.
PROSITEiPS01164. COPPER_AMINE_OXID_1. 1 hit.
PS01165. COPPER_AMINE_OXID_2. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

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

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: P19801-1) [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
MPALGWAVAA ILMLQTAMAE PSPGTLPRKA GVFSDLSNQE LKAVHSFLWS
60 70 80 90 100
KKELRLQPSS TTTMAKNTVF LIEMLLPKKY HVLRFLDKGE RHPVREARAV
110 120 130 140 150
IFFGDQEHPN VTEFAVGPLP GPCYMRALSP RPGYQSSWAS RPISTAEYAL
160 170 180 190 200
LYHTLQEATK PLHQFFLNTT GFSFQDCHDR CLAFTDVAPR GVASGQRRSW
210 220 230 240 250
LIIQRYVEGY FLHPTGLELL VDHGSTDAGH WAVEQVWYNG KFYGSPEELA
260 270 280 290 300
RKYADGEVDV VVLEDPLPGG KGHDSTEEPP LFSSHKPRGD FPSPIHVSGP
310 320 330 340 350
RLVQPHGPRF RLEGNAVLYG GWSFAFRLRS SSGLQVLNVH FGGERIAYEV
360 370 380 390 400
SVQEAVALYG GHTPAGMQTK YLDVGWGLGS VTHELAPGID CPETATFLDT
410 420 430 440 450
FHYYDADDPV HYPRALCLFE MPTGVPLRRH FNSNFKGGFN FYAGLKGQVL
460 470 480 490 500
VLRTTSTVYN YDYIWDFIFY PNGVMEAKMH ATGYVHATFY TPEGLRHGTR
510 520 530 540 550
LHTHLIGNIH THLVHYRVDL DVAGTKNSFQ TLQMKLENIT NPWSPRHRVV
560 570 580 590 600
QPTLEQTQYS WERQAAFRFK RKLPKYLLFT SPQENPWGHK RTYRLQIHSM
610 620 630 640 650
ADQVLPPGWQ EEQAITWARY PLAVTKYRES ELCSSSIYHQ NDPWHPPVVF
660 670 680 690 700
EQFLHNNENI ENEDLVAWVT VGFLHIPHSE DIPNTATPGN SVGFLLRPFN
710 720 730 740 750
FFPEDPSLAS RDTVIVWPRD NGPNYVQRWI PEDRDCSMPP PFSYNGTYRP

V
Length:751
Mass (Da):85,378
Last modified:July 7, 2009 - v4
Checksum:i37114CD0D446639C
GO
Isoform 2 (identifier: P19801-2) [UniParc]FASTAAdd to basket
Also known as: DAO2

The sequence of this isoform differs from the canonical sequence as follows:
     618-618: A → ARTEGGQPRALSQAASPVPG

Show »
Length:770
Mass (Da):87,239
Checksum:iCA4864D23DB6D7CC
GO

Sequence cautioni

The sequence AAA58358 differs from that shown. Reason: Frameshift at positions 266, 284, 328, 494, 497, 514, 707 and 729.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti28R → A AA sequence (PubMed:8144586).Curated1
Sequence conflicti280P → A in AAA58358 (PubMed:2217167).Curated1
Sequence conflicti290D → T in AAA58358 (PubMed:2217167).Curated1
Sequence conflicti572K → R in AAA58358 (PubMed:2217167).Curated1
Sequence conflicti592T → S in AAA58358 (PubMed:2217167).Curated1
Sequence conflicti592T → S in CAA55046 (PubMed:8182053).Curated1
Sequence conflicti592T → S in AAC50270 (PubMed:8595053).Curated1
Sequence conflicti592T → S in AAB60381 (PubMed:8595053).Curated1
Sequence conflicti592T → S in AAH14093 (PubMed:15489334).Curated1
Isoform 2 (identifier: P19801-2)
Sequence conflicti632A → R in AAB60381 (PubMed:8595053).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_02507816T → M.1 PublicationCorresponds to variant rs10156191dbSNPEnsembl.1
Natural variantiVAR_025079332S → F.2 PublicationsCorresponds to variant rs1049742dbSNPEnsembl.1
Natural variantiVAR_025080479M → I.1 PublicationCorresponds to variant rs45558339dbSNPEnsembl.1
Natural variantiVAR_007542645H → D.4 PublicationsCorresponds to variant rs1049793dbSNPEnsembl.1
Natural variantiVAR_025081659N → H.1 PublicationCorresponds to variant rs35070995dbSNPEnsembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_055190618A → ARTEGGQPRALSQAASPVPG in isoform 2. 1 Publication1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M55602 mRNA. Translation: AAA58358.1. Frameshift.
X78212 Genomic DNA. Translation: CAA55046.1.
U11862 mRNA. Translation: AAC50270.1.
U11863 mRNA. Translation: AAB60381.1.
AY948960 Genomic DNA. Translation: AAX81409.1.
AC006343 Genomic DNA. No translation available.
AC006479 Genomic DNA. No translation available.
BC014093 mRNA. Translation: AAH14093.1.
CCDSiCCDS43679.1. [P19801-1]
CCDS64797.1. [P19801-2]
PIRiA54053.
RefSeqiNP_001082.2. NM_001091.3. [P19801-1]
NP_001259001.1. NM_001272072.1. [P19801-2]
XP_016867433.1. XM_017011944.1. [P19801-2]
XP_016867434.1. XM_017011945.1. [P19801-2]
XP_016867435.1. XM_017011946.1. [P19801-2]
XP_016867436.1. XM_017011947.1. [P19801-1]
UniGeneiHs.647097.
Hs.733889.

Genome annotation databases

EnsembliENST00000360937; ENSP00000354193; ENSG00000002726. [P19801-1]
ENST00000416793; ENSP00000411613; ENSG00000002726. [P19801-2]
ENST00000467291; ENSP00000418328; ENSG00000002726. [P19801-1]
ENST00000493429; ENSP00000418614; ENSG00000002726. [P19801-1]
GeneIDi26.
KEGGihsa:26.
UCSCiuc003whz.3. human. [P19801-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Web resourcesi

NIEHS-SNPs

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M55602 mRNA. Translation: AAA58358.1. Frameshift.
X78212 Genomic DNA. Translation: CAA55046.1.
U11862 mRNA. Translation: AAC50270.1.
U11863 mRNA. Translation: AAB60381.1.
AY948960 Genomic DNA. Translation: AAX81409.1.
AC006343 Genomic DNA. No translation available.
AC006479 Genomic DNA. No translation available.
BC014093 mRNA. Translation: AAH14093.1.
CCDSiCCDS43679.1. [P19801-1]
CCDS64797.1. [P19801-2]
PIRiA54053.
RefSeqiNP_001082.2. NM_001091.3. [P19801-1]
NP_001259001.1. NM_001272072.1. [P19801-2]
XP_016867433.1. XM_017011944.1. [P19801-2]
XP_016867434.1. XM_017011945.1. [P19801-2]
XP_016867435.1. XM_017011946.1. [P19801-2]
XP_016867436.1. XM_017011947.1. [P19801-1]
UniGeneiHs.647097.
Hs.733889.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3HI7X-ray1.80A/B21-751[»]
3HIGX-ray2.09A/B21-751[»]
3HIIX-ray2.15A/B21-751[»]
3K5TX-ray2.11A21-751[»]
3MPHX-ray2.05A/B21-751[»]
ProteinModelPortaliP19801.
SMRiP19801.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi106544. 1 interactor.
STRINGi9606.ENSP00000354193.

Chemistry databases

BindingDBiP19801.
ChEMBLiCHEMBL2118.
DrugBankiDB00594. Amiloride.

PTM databases

iPTMnetiP19801.
PhosphoSitePlusiP19801.

Polymorphism and mutation databases

DMDMi251757489.

Proteomic databases

PaxDbiP19801.
PeptideAtlasiP19801.
PRIDEiP19801.
TopDownProteomicsiP19801-1. [P19801-1]

Protocols and materials databases

DNASUi26.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000360937; ENSP00000354193; ENSG00000002726. [P19801-1]
ENST00000416793; ENSP00000411613; ENSG00000002726. [P19801-2]
ENST00000467291; ENSP00000418328; ENSG00000002726. [P19801-1]
ENST00000493429; ENSP00000418614; ENSG00000002726. [P19801-1]
GeneIDi26.
KEGGihsa:26.
UCSCiuc003whz.3. human. [P19801-1]

Organism-specific databases

CTDi26.
DisGeNETi26.
GeneCardsiAOC1.
H-InvDBHIX0007216.
HGNCiHGNC:80. AOC1.
HPAiHPA031032.
HPA031033.
MIMi104610. gene.
neXtProtiNX_P19801.
OpenTargetsiENSG00000002726.
PharmGKBiPA24416.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG1186. Eukaryota.
COG3733. LUCA.
GeneTreeiENSGT00510000046461.
HOGENOMiHOG000233919.
HOVERGENiHBG004164.
InParanoidiP19801.
KOiK11182.
OMAiFNSNFKG.
OrthoDBiEOG091G0C1O.
PhylomeDBiP19801.
TreeFamiTF314750.

Enzyme and pathway databases

BioCyciMetaCyc:HS00083-MONOMER.
ZFISH:HS00083-MONOMER.
BRENDAi1.4.3.22. 2681.
ReactomeiR-HSA-211945. Phase 1 - Functionalization of compounds.
R-HSA-6798695. Neutrophil degranulation.

Miscellaneous databases

EvolutionaryTraceiP19801.
GenomeRNAii26.
PROiP19801.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000002726.
CleanExiHS_ABP1.
ExpressionAtlasiP19801. baseline and differential.
GenevisibleiP19801. HS.

Family and domain databases

Gene3Di2.70.98.20. 1 hit.
InterProiIPR000269. Cu_amine_oxidase.
IPR015798. Cu_amine_oxidase_C.
IPR016182. Cu_amine_oxidase_N-reg.
IPR015800. Cu_amine_oxidase_N2.
IPR015802. Cu_amine_oxidase_N3.
[Graphical view]
PANTHERiPTHR10638. PTHR10638. 1 hit.
PfamiPF01179. Cu_amine_oxid. 1 hit.
PF02727. Cu_amine_oxidN2. 1 hit.
PF02728. Cu_amine_oxidN3. 1 hit.
[Graphical view]
PRINTSiPR00766. CUDAOXIDASE.
SUPFAMiSSF49998. SSF49998. 1 hit.
SSF54416. SSF54416. 2 hits.
PROSITEiPS01164. COPPER_AMINE_OXID_1. 1 hit.
PS01165. COPPER_AMINE_OXID_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiAOC1_HUMAN
AccessioniPrimary (citable) accession number: P19801
Secondary accession number(s): C9J690
, Q16683, Q16684, Q56II4, Q6GU42
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1991
Last sequence update: July 7, 2009
Last modified: November 30, 2016
This is version 174 of the entry and version 4 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

Inhibited by amiloride in a competitive manner.By similarity

Keywords - Technical termi

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

Documents

  1. Human chromosome 7
    Human chromosome 7: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

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 one 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.