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Protein

Carbonic anhydrase 9

Gene

CA9

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

Functioni

Reversible hydration of carbon dioxide. Participates in pH regulation. May be involved in the control of cell proliferation and transformation. Appears to be a novel specific biomarker for a cervical neoplasia.1 Publication

Catalytic activityi

H2CO3 = CO2 + H2O.

Cofactori

Zn2+1 Publication

Enzyme regulationi

Inhibited by coumarins, saccharin, sulfonamide derivatives such as acetazolamide (AZA) and Foscarnet (phosphonoformate trisodium salt).4 Publications

pH dependencei

Optimum pH is 6.5.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei200 – 2001Proton acceptorBy similarity
Metal bindingi226 – 2261Zinc; catalytic1 Publication
Metal bindingi228 – 2281Zinc; catalytic1 Publication
Metal bindingi251 – 2511Zinc; catalytic1 Publication

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Lyase

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

BRENDAi4.2.1.1. 2681.
ReactomeiR-HSA-1234158. Regulation of gene expression by Hypoxia-inducible Factor.
R-HSA-1475029. Reversible hydration of carbon dioxide.
SIGNORiQ16790.

Names & Taxonomyi

Protein namesi
Recommended name:
Carbonic anhydrase 9 (EC:4.2.1.1)
Alternative name(s):
Carbonate dehydratase IX
Carbonic anhydrase IX
Short name:
CA-IX
Short name:
CAIX
Membrane antigen MN
P54/58N
Renal cell carcinoma-associated antigen G250
Short name:
RCC-associated antigen G250
pMW1
Gene namesi
Name:CA9
Synonyms:G250, MN
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 9

Organism-specific databases

HGNCiHGNC:1383. CA9.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini38 – 414377ExtracellularAdd
BLAST
Transmembranei415 – 43521HelicalSequence analysisAdd
BLAST
Topological domaini436 – 45924CytoplasmicAdd
BLAST

GO - Cellular componenti

  • basolateral plasma membrane Source: Ensembl
  • integral component of membrane Source: ProtInc
  • microvillus membrane Source: UniProtKB-SubCell
  • nucleolus Source: UniProtKB-SubCell
  • plasma membrane Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cell projection, Membrane, Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA25998.

Chemistry

ChEMBLiCHEMBL2095180.
DrugBankiDB00562. Benzthiazide.
DB00999. Hydrochlorothiazide.
DB00774. Hydroflumethiazide.
DB00909. Zonisamide.

Polymorphism and mutation databases

BioMutaiCA9.
DMDMi83300925.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 37371 PublicationAdd
BLAST
Chaini38 – 459422Carbonic anhydrase 9PRO_0000004243Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi115 – 1151O-linked (GlcNAc...)1 Publication
Disulfide bondi156 ↔ 3361 Publication
Disulfide bondi174 – 174Interchain1 Publication
Glycosylationi346 – 3461N-linked (GlcNAc...)2 Publications
Modified residuei449 – 4491Phosphotyrosine1 Publication

Post-translational modificationi

Asn-346 bears high-mannose type glycan structures.

Keywords - PTMi

Disulfide bond, Glycoprotein, Phosphoprotein

Proteomic databases

MaxQBiQ16790.
PaxDbiQ16790.
PeptideAtlasiQ16790.
PRIDEiQ16790.

PTM databases

iPTMnetiQ16790.
PhosphoSiteiQ16790.

Expressioni

Tissue specificityi

Expressed primarily in carcinoma cells lines. Expression is restricted to very few normal tissues and the most abundant expression is found in the epithelial cells of gastric mucosa.

Inductioni

By hypoxia.1 Publication

Gene expression databases

BgeeiENSG00000107159.
CleanExiHS_CA9.
ExpressionAtlasiQ16790. baseline and differential.
GenevisibleiQ16790. HS.

Organism-specific databases

HPAiCAB005100.
CAB017107.
HPA055207.

Interactioni

Subunit structurei

Forms oligomers linked by disulfide bonds.3 Publications

Protein-protein interaction databases

BioGridi107223. 30 interactions.
DIPiDIP-48973N.
STRINGi9606.ENSP00000367608.

Chemistry

BindingDBiQ16790.

Structurei

Secondary structure

1
459
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Turni137 – 1393Combined sources
Beta strandi145 – 1473Combined sources
Helixi149 – 1524Combined sources
Helixi154 – 1574Combined sources
Beta strandi170 – 1734Combined sources
Beta strandi181 – 1844Combined sources
Beta strandi193 – 1975Combined sources
Beta strandi202 – 2054Combined sources
Beta strandi211 – 2155Combined sources
Beta strandi219 – 22911Combined sources
Beta strandi238 – 2414Combined sources
Beta strandi247 – 25610Combined sources
Helixi262 – 2654Combined sources
Beta strandi271 – 28111Combined sources
Helixi287 – 2937Combined sources
Turni294 – 2963Combined sources
Helixi297 – 2993Combined sources
Beta strandi305 – 3084Combined sources
Helixi313 – 3164Combined sources
Beta strandi324 – 3307Combined sources
Beta strandi338 – 34710Combined sources
Beta strandi349 – 3513Combined sources
Helixi353 – 3619Combined sources
Beta strandi387 – 3893Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2HKFX-ray2.01P83-91[»]
3IAIX-ray2.20A/B/C/D137-391[»]
5FL4X-ray1.82A/B/C/D137-391[»]
5FL5X-ray2.05A/B/C/D137-391[»]
5FL6X-ray1.95A/B/C/D137-391[»]
ProteinModelPortaliQ16790.
SMRiQ16790. Positions 139-391.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ16790.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini139 – 390252Alpha-carbonic anhydrasePROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni38 – 11275Proteoglycan-like (PG)Add
BLAST
Regioni113 – 414302CatalyticAdd
BLAST
Regioni332 – 3332Substrate bindingBy similarity

Sequence similaritiesi

Belongs to the alpha-carbonic anhydrase family.Curated
Contains 1 alpha-carbonic anhydrase domain.PROSITE-ProRule annotation

Keywords - Domaini

Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG0382. Eukaryota.
COG3338. LUCA.
GeneTreeiENSGT00760000118915.
HOGENOMiHOG000112637.
HOVERGENiHBG002837.
InParanoidiQ16790.
KOiK01672.
OMAiSRYFRYE.
OrthoDBiEOG091G0XFM.
PhylomeDBiQ16790.
TreeFamiTF316425.

Family and domain databases

Gene3Di3.10.200.10. 1 hit.
InterProiIPR018429. CA9.
IPR001148. Carbonic_anhydrase_a.
IPR023561. Carbonic_anhydrase_a-class.
IPR018338. Carbonic_anhydrase_a-class_CS.
[Graphical view]
PANTHERiPTHR18952. PTHR18952. 1 hit.
PTHR18952:SF18. PTHR18952:SF18. 1 hit.
PfamiPF00194. Carb_anhydrase. 1 hit.
[Graphical view]
SMARTiSM01057. Carb_anhydrase. 1 hit.
[Graphical view]
SUPFAMiSSF51069. SSF51069. 1 hit.
PROSITEiPS00162. ALPHA_CA_1. 1 hit.
PS51144. ALPHA_CA_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

Q16790-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAPLCPSPWL PLLIPAPAPG LTVQLLLSLL LLVPVHPQRL PRMQEDSPLG
60 70 80 90 100
GGSSGEDDPL GEEDLPSEED SPREEDPPGE EDLPGEEDLP GEEDLPEVKP
110 120 130 140 150
KSEEEGSLKL EDLPTVEAPG DPQEPQNNAH RDKEGDDQSH WRYGGDPPWP
160 170 180 190 200
RVSPACAGRF QSPVDIRPQL AAFCPALRPL ELLGFQLPPL PELRLRNNGH
210 220 230 240 250
SVQLTLPPGL EMALGPGREY RALQLHLHWG AAGRPGSEHT VEGHRFPAEI
260 270 280 290 300
HVVHLSTAFA RVDEALGRPG GLAVLAAFLE EGPEENSAYE QLLSRLEEIA
310 320 330 340 350
EEGSETQVPG LDISALLPSD FSRYFQYEGS LTTPPCAQGV IWTVFNQTVM
360 370 380 390 400
LSAKQLHTLS DTLWGPGDSR LQLNFRATQP LNGRVIEASF PAGVDSSPRA
410 420 430 440 450
AEPVQLNSCL AAGDILALVF GLLFAVTSVA FLVQMRRQHR RGTKGGVSYR

PAEVAETGA
Length:459
Mass (Da):49,698
Last modified:December 6, 2005 - v2
Checksum:iBA67195483F0F5CE
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti33 – 331V → M.2 Publications
Corresponds to variant rs2071676 [ dbSNP | Ensembl ].
VAR_010787
Natural varianti326 – 3261Q → R.
Corresponds to variant rs3829078 [ dbSNP | Ensembl ].
VAR_020049

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X66839 mRNA. Translation: CAA47315.1.
AJ010588 mRNA. Translation: CAB82444.1.
AL133410, AL357874 Genomic DNA. Translation: CAI10985.1.
AL357874, AL133410 Genomic DNA. Translation: CAI13455.1.
CH471071 Genomic DNA. Translation: EAW58359.1.
BC014950 mRNA. Translation: AAH14950.1.
CCDSiCCDS6585.1.
PIRiI38013.
RefSeqiNP_001207.2. NM_001216.2.
UniGeneiHs.63287.

Genome annotation databases

EnsembliENST00000378357; ENSP00000367608; ENSG00000107159.
GeneIDi768.
KEGGihsa:768.
UCSCiuc003zxo.5. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X66839 mRNA. Translation: CAA47315.1.
AJ010588 mRNA. Translation: CAB82444.1.
AL133410, AL357874 Genomic DNA. Translation: CAI10985.1.
AL357874, AL133410 Genomic DNA. Translation: CAI13455.1.
CH471071 Genomic DNA. Translation: EAW58359.1.
BC014950 mRNA. Translation: AAH14950.1.
CCDSiCCDS6585.1.
PIRiI38013.
RefSeqiNP_001207.2. NM_001216.2.
UniGeneiHs.63287.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2HKFX-ray2.01P83-91[»]
3IAIX-ray2.20A/B/C/D137-391[»]
5FL4X-ray1.82A/B/C/D137-391[»]
5FL5X-ray2.05A/B/C/D137-391[»]
5FL6X-ray1.95A/B/C/D137-391[»]
ProteinModelPortaliQ16790.
SMRiQ16790. Positions 139-391.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi107223. 30 interactions.
DIPiDIP-48973N.
STRINGi9606.ENSP00000367608.

Chemistry

BindingDBiQ16790.
ChEMBLiCHEMBL2095180.
DrugBankiDB00562. Benzthiazide.
DB00999. Hydrochlorothiazide.
DB00774. Hydroflumethiazide.
DB00909. Zonisamide.

PTM databases

iPTMnetiQ16790.
PhosphoSiteiQ16790.

Polymorphism and mutation databases

BioMutaiCA9.
DMDMi83300925.

Proteomic databases

MaxQBiQ16790.
PaxDbiQ16790.
PeptideAtlasiQ16790.
PRIDEiQ16790.

Protocols and materials databases

DNASUi768.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000378357; ENSP00000367608; ENSG00000107159.
GeneIDi768.
KEGGihsa:768.
UCSCiuc003zxo.5. human.

Organism-specific databases

CTDi768.
GeneCardsiCA9.
H-InvDBHIX0008019.
HGNCiHGNC:1383. CA9.
HPAiCAB005100.
CAB017107.
HPA055207.
MIMi603179. gene.
neXtProtiNX_Q16790.
PharmGKBiPA25998.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG0382. Eukaryota.
COG3338. LUCA.
GeneTreeiENSGT00760000118915.
HOGENOMiHOG000112637.
HOVERGENiHBG002837.
InParanoidiQ16790.
KOiK01672.
OMAiSRYFRYE.
OrthoDBiEOG091G0XFM.
PhylomeDBiQ16790.
TreeFamiTF316425.

Enzyme and pathway databases

BRENDAi4.2.1.1. 2681.
ReactomeiR-HSA-1234158. Regulation of gene expression by Hypoxia-inducible Factor.
R-HSA-1475029. Reversible hydration of carbon dioxide.
SIGNORiQ16790.

Miscellaneous databases

EvolutionaryTraceiQ16790.
GeneWikiiCarbonic_anhydrase_9.
GenomeRNAii768.
PROiQ16790.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000107159.
CleanExiHS_CA9.
ExpressionAtlasiQ16790. baseline and differential.
GenevisibleiQ16790. HS.

Family and domain databases

Gene3Di3.10.200.10. 1 hit.
InterProiIPR018429. CA9.
IPR001148. Carbonic_anhydrase_a.
IPR023561. Carbonic_anhydrase_a-class.
IPR018338. Carbonic_anhydrase_a-class_CS.
[Graphical view]
PANTHERiPTHR18952. PTHR18952. 1 hit.
PTHR18952:SF18. PTHR18952:SF18. 1 hit.
PfamiPF00194. Carb_anhydrase. 1 hit.
[Graphical view]
SMARTiSM01057. Carb_anhydrase. 1 hit.
[Graphical view]
SUPFAMiSSF51069. SSF51069. 1 hit.
PROSITEiPS00162. ALPHA_CA_1. 1 hit.
PS51144. ALPHA_CA_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiCAH9_HUMAN
AccessioniPrimary (citable) accession number: Q16790
Secondary accession number(s): Q5T4R1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 15, 1999
Last sequence update: December 6, 2005
Last modified: September 7, 2016
This is version 159 of the entry and version 2 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

Keywords - Technical termi

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

Documents

  1. Human chromosome 9
    Human chromosome 9: 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.