Carbonic anhydrase 9 precursor - Homo sapiens (Human)

Names and origin

Protein names

Recommended name:
    Carbonic anhydrase 9
    EC=4.2.1.1
Alternative name(s):
    Carbonic anhydrase IX
      Short name=CA-IX
      Short name=CAIX
    Carbonate dehydratase IX
    Membrane antigen MN
    P54/58N
    Renal cell carcinoma-associated antigen G250
      Short name=RCC-associated antigen G250
    pMW1

Gene names

Name:	CA9
Synonyms:	G250, MN

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Hide | Top

Protein attributes

Sequence length	459 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

Hide | Top

General annotation (Comments)

Function	Reversible hydration of carbon dioxide. May be involved in the control of cell proliferation and transformation. Appears to be a novel specific biomarker for a cervical neoplasia.
Catalytic activity	H(2)CO(3) = CO(2) + H(2)O.
Cofactor	Zinc By similarity.
Subunit structure	Forms oligomers linked by disulfide bonds.
Subcellular location	Nucleus. Nucleus › nucleolus. Cell membrane; Single-pass type I membrane protein. Cell projection › microvillus membrane; Single-pass type I membrane protein. Note= Found on the surface microvilli and in the nucleus, particularly in nucleolus.
Tissue specificity	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.
Post-translational modification	N-glycosylated.
Sequence similarities	Belongs to the alpha-carbonic anhydrase family.

Hide | Top

Ontologies

Keywords
Cellular component	Cell membrane Cell projection Membrane Nucleus
Coding sequence diversity	Polymorphism
Domain	Signal Transmembrane
Ligand	Metal-binding Zinc
Molecular function	Lyase
PTM	Glycoprotein
Technical term	3D-structure Direct protein sequencing
Gene Ontology (GO)
Biological process	one-carbon compound metabolic process Inferred from electronic annotation. Source: InterPro
Cellular component	cell projection Inferred from electronic annotation. Source: UniProtKB-KW integral to membrane Traceable author statement. Source: ProtInc nucleus Inferred from electronic annotation. Source: UniProtKB-KW plasma membrane Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	carbonate dehydratase activity Traceable author statement. Source: ProtInc zinc ion binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Hide | Top

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 37

37

Chain

38 – 459

422

Carbonic anhydrase 9

PRO_0000004243

Regions

Topological domain

38 – 414

377

Extracellular

Transmembrane

415 – 435

21

Potential

Topological domain

436 – 459

24

Cytoplasmic

Sites

Metal binding

226

1

Zinc; catalytic By similarity

Metal binding

228

1

Zinc; catalytic By similarity

Metal binding

251

1

Zinc; catalytic By similarity

Amino acid modifications

Glycosylation

346

1

N-linked (GlcNAc...)

Natural variations

Natural variant

33

1

V → M: dbSNP rs2071676.

VAR_010787

Natural variant

326

1

Q → R: dbSNP rs3829078.

VAR_020049

Hide | Top

Sequences

Sequence

Length

Mass (Da)

Tools

Q16790-1 [UniParc].

Last modified December 6, 2005. Version 2.
Checksum: BA67195483F0F5CE
Show »

FASTA

459

49,698

        10         20         30         40         50         60 
MAPLCPSPWL PLLIPAPAPG LTVQLLLSLL LLVPVHPQRL PRMQEDSPLG GGSSGEDDPL 

        70         80         90        100        110        120 
GEEDLPSEED SPREEDPPGE EDLPGEEDLP GEEDLPEVKP KSEEEGSLKL EDLPTVEAPG 

       130        140        150        160        170        180 
DPQEPQNNAH RDKEGDDQSH WRYGGDPPWP RVSPACAGRF QSPVDIRPQL AAFCPALRPL 

       190        200        210        220        230        240 
ELLGFQLPPL PELRLRNNGH SVQLTLPPGL EMALGPGREY RALQLHLHWG AAGRPGSEHT 

       250        260        270        280        290        300 
VEGHRFPAEI HVVHLSTAFA RVDEALGRPG GLAVLAAFLE EGPEENSAYE QLLSRLEEIA 

       310        320        330        340        350        360 
EEGSETQVPG LDISALLPSD FSRYFQYEGS LTTPPCAQGV IWTVFNQTVM LSAKQLHTLS 

       370        380        390        400        410        420 
DTLWGPGDSR LQLNFRATQP LNGRVIEASF PAGVDSSPRA AEPVQLNSCL AAGDILALVF 

       430        440        450 
GLLFAVTSVA FLVQMRRQHR RGTKGGVSYR PAEVAETGA

« Hide

Hide | Top

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Cloning and characterization of MN, a human tumor-associated protein with a domain homologous to carbonic anhydrase and a putative helix-loop-helix DNA binding segment." Pastorek J., Pastorekova S., Callebaut I., Mornon J.-P., Zelnik V., Opavsky R., Zat'Ovicova M., Liao S., Portetelle D., Stanbridge E.J., Zavada J., Burny A., Kettmann R. Oncogene 9:2877-2888(1994) [PubMed: 8084592] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], CHARACTERIZATION, VARIANT MET-33. Tissue: Carcinoma.
[2]	"Molecular cloning and immunogenicity of renal cell carcinoma-associated antigen G250." Grabmaier K., Vissers J.L.M., De Weijert M.C.A., Oosterwijk-Wakka J.C., Van Bokhoven A., Brakenhoff R.H., Noessner E., Mulders P.A., Merkx G., Figdor C.G., Adema G.J., Oosterwijk E. Int. J. Cancer 85:865-870(2000) [PubMed: 10709109] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Renal cell carcinoma.
[3]	"DNA sequence and analysis of human chromosome 9." Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S., Bagguley C.L. Dunham I. Nature 429:369-374(2004) [PubMed: 15164053] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]	Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. Venter J.C. Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT MET-33. Tissue: Colon.
[6]	"Signal peptide prediction based on analysis of experimentally verified cleavage sites." Zhang Z., Henzel W.J. Protein Sci. 13:2819-2824(2004) [PubMed: 15340161] [Abstract] Cited for: PROTEIN SEQUENCE OF 38-52.
[7]	"A novel quasi-viral agent, MaTu, is a two-component system." Pastorekova S., Zavadova Z., Kostal M., Babusikova O., Zavada J. Virology 187:620-626(1992) [PubMed: 1312272] [Abstract] Cited for: CHARACTERIZATION.
[8]	"Expression of MaTu-MN protein in human tumor cultures and in clinical specimens." Zavada J., Zavadova Z., Pastorekova S., Ciampor F., Pastorek J., Zelnik V. Int. J. Cancer 54:268-274(1993) [PubMed: 8486430] [Abstract] Cited for: SUBCELLULAR LOCATION.
+	Additional computationally mapped references.

Hide | Top

Cross-references

Sequence databases

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.

PIR

I38013.

RefSeq

NP_001207.2.

UniGene

Hs.63287

3D structure databases

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2HKF	X-ray	2.01	P	83-91	[»]

ModBase

Search...

PTM databases

PhosphoSite

Q16790.

Genome annotation databases

Ensembl

ENSG00000107159. Homo sapiens. [Contig view]

GeneID

768.

KEGG

hsa:768.

Organism-specific databases

HGNC

HGNC:1383. CA9.

HPA

CAB005100.
CAB017107.

MIM

603179. gene.

PharmGKB

PA24384.

GenAtlas

Search...

GeneCards

Search...

Phylogenomic databases

HOGENOM

Q16790.

HOVERGEN

Q16790.

Gene expression databases

ArrayExpress

Q16790.

CleanEx

HS_CA9.

GermOnline

ENSG00000107159. Homo sapiens.

Family and domain databases

InterPro

IPR001148. Euk_COanhd.
[Graphical view]

Gene3D

G3DSA:3.10.200.10. Euk_COanhd. 1 hit.

PANTHER

PTHR18952. Euk_COanhd. 1 hit.

Pfam

PF00194. Carb_anhydrase. 1 hit.
[Graphical view]

ProDom

PD000865. Euk_COanhd. 1 hit.
[Graphical view] [Entries sharing at least one domain]

PROSITE

PS00162. ALPHA_CA_1. 1 hit.
PS51144. ALPHA_CA_2. 1 hit.
[Graphical view]

ProtoNet

Search...

Other Resources

NextBio

3106.

SOURCE

Search...

Hide | Top

Entry information

Entry name

CAH9_HUMAN

Accession

Primary (citable) accession number: Q16790
Secondary accession number(s): Q5T4R1

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 15, 1999
Last sequence update:	December 6, 2005
Last modified:	November 25, 2008
This is version 85 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

Hide | Top

Relevant documents

Human chromosome 9

Human chromosome 9: entries, gene names and cross-references to MIM

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Keywords

Gene Ontology (GO)

Sequence annotation (Features)

Molecule processing

Regions

Sites

Amino acid modifications

Natural variations

Sequences

References

Cross-references

Sequence databases

3D structure databases

PTM databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Gene expression databases

Family and domain databases

Other Resources

Entry information

Relevant documents