Q9ULX7 (CAH14_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Carbonic anhydrase 14
EC=4.2.1.1

Alternative name(s):
Carbonate dehydratase XIV
Carbonic anhydrase XIV
Short name=CA-XIV

Gene names

Name:	CA14
ORF Names:	UNQ690/PRO1335

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	337 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Reversible hydration of carbon dioxide.
Catalytic activity	H2CO3 = CO2 + H2O.
Cofactor	Zinc By similarity.
Enzyme regulation	Activated by histamine, L-adrenaline, L- and D-histidine, and L- and D-phenylalanine. Inhibited by coumarins, saccharin, sulfonamide derivatives such as acetazolamide (AZA) and Foscarnet (phosphonoformate trisodium salt). Ref.7 Ref.8 Ref.9 Ref.10 Ref.11 Ref.12 Ref.13 Ref.14
Subcellular location	Membrane; Single-pass type I membrane protein Potential.
Tissue specificity	High expression in all parts of the central nervous system and lower expression in adult liver, heart, small intestine, colon, kidney, urinary bladder and skeletal muscle.
Sequence similarities	Belongs to the alpha-carbonic anhydrase family.
Biophysicochemical properties	Kinetic parameters: KM=7.9 mM for CO2 Ref.14

Ontologies

Keywords
Cellular component	Membrane
Domain	Signal Transmembrane Transmembrane helix
Ligand	Metal-binding Zinc
Molecular function	Lyase
PTM	Disulfide bond Glycoprotein Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	bicarbonate transport Traceable author statement. Source: Reactome small molecule metabolic process Traceable author statement. Source: Reactome
Cellular_component	integral to membrane Traceable author statement Ref.1. Source: ProtInc plasma membrane Traceable author statement. Source: Reactome
Molecular_function	carbonate dehydratase activity Traceable author statement Ref.1. Source: ProtInc metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 15	15	Potential
	Chain	16 – 337	322	Carbonic anhydrase 14		PRO_0000004251
Regions
	Topological domain	16 – 290	275	Extracellular Potential
	Transmembrane	291 – 311	21	Helical; Potential
	Topological domain	312 – 337	26	Cytoplasmic Potential
	Region	217 – 218	2	Substrate binding By similarity
Sites
	Active site	84	1	Proton acceptor By similarity
	Active site	144	1	By similarity
	Metal binding	109	1	Zinc; catalytic By similarity
	Metal binding	111	1	Zinc; catalytic By similarity
	Metal binding	135	1	Zinc; catalytic By similarity
Amino acid modifications
	Modified residue	325	1	Phosphoserine Ref.15
	Glycosylation	213	1	N-linked (GlcNAc...) Potential
	Disulfide bond	40 ↔ 221		By similarity
Experimental info
	Sequence conflict	229	1	V → A in BAC11191. Ref.3

Sequences

	Sequence		Length	Mass (Da)
	Q9ULX7 [UniParc]. Last modified May 1, 2000. Version 1. Checksum: 6E101C44EA70A700	FASTA	337	37,668
	10 20 30 40 50 60 MLFSALLLEV IWILAADGGQ HWTYEGPHGQ DHWPASYPEC GNNAQSPIDI QTDSVTFDPD 70 80 90 100 110 120 LPALQPHGYD QPGTEPLDLH NNGHTVQLSL PSTLYLGGLP RKYVAAQLHL HWGQKGSPGG 130 140 150 160 170 180 SEHQINSEAT FAELHIVHYD SDSYDSLSEA AERPQGLAVL GILIEVGETK NIAYEHILSH 190 200 210 220 230 240 LHEVRHKDQK TSVPPFNLRE LLPKQLGQYF RYNGSLTTPP CYQSVLWTVF YRRSQISMEQ 250 260 270 280 290 300 LEKLQGTLFS TEEEPSKLLV QNYRALQPLN QRMVFASFIQ AGSSYTTGEM LSLGVGILVG 310 320 330 CLCLLLAVYF IARKIRKKRL ENRKSVVFTS AQATTEA

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Human carbonic anhydrase XIV (CA14): cDNA cloning, mRNA expression, and mapping to chromosome 1." Fujikawa-Adachi K., Nishimori I., Taguchi T., Onishi S. Genomics 61:74-81(1999) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	"The secreted protein discovery initiative (SPDI), a large-scale effort to identify novel human secreted and transmembrane proteins: a bioinformatics assessment." Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J., Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P., Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E. , Heldens S., Huang A., Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J., Lewis L., Liao D., Mark M.R., Robbie E., Sanchez C., Schoenfeld J., Seshagiri S., Simmons L., Singh J., Smith V., Stinson J., Vagts A., Vandlen R.L., Watanabe C., Wieand D., Woods K., Xie M.-H., Yansura D.G., Yi S., Yu G., Yuan J., Zhang M., Zhang Z., Goddard A.D., Wood W.I., Godowski P.J., Gray A.M. Genome Res. 13:2265-2270(2003) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[3]	"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].
[4]	"Cloning of human full-length CDSs in BD Creator(TM) system donor vector." Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A. Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[5]	"The DNA sequence and biological annotation of human chromosome 1." Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K. , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R. Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]	"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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Brain, Lung and Testis.
[7]	"Carbonic anhydrase activators. Activation of isozymes I, II, IV, VA, VII, and XIV with l- and d-histidine and crystallographic analysis of their adducts with isoform II: engineering proton-transfer processes within the active site of an enzyme." Temperini C., Scozzafava A., Vullo D., Supuran C.T. Chemistry 12:7057-7066(2006) [PubMed] [Europe PMC] [Abstract] Cited for: ENZYME REGULATION.
[8]	"Carbonic anhydrase activators. Activation of isoforms I, II, IV, VA, VII, and XIV with L- and D-phenylalanine and crystallographic analysis of their adducts with isozyme II: stereospecific recognition within the active site of an enzyme and its consequences for the drug design." Temperini C., Scozzafava A., Vullo D., Supuran C.T. J. Med. Chem. 49:3019-3027(2006) [PubMed] [Europe PMC] [Abstract] Cited for: ENZYME REGULATION.
[9]	"Saccharin inhibits carbonic anhydrases: possible explanation for its unpleasant metallic aftertaste." Koehler K., Hillebrecht A., Schulze Wischeler J., Innocenti A., Heine A., Supuran C.T., Klebe G. Angew. Chem. Int. Ed. Engl. 46:7697-7699(2007) [PubMed] [Europe PMC] [Abstract] Cited for: ENZYME REGULATION.
[10]	"Carbonic anhydrase activators: L-Adrenaline plugs the active site entrance of isozyme II, activating better isoforms I, IV, VA, VII, and XIV." Temperini C., Innocenti A., Scozzafava A., Mastrolorenzo A., Supuran C.T. Bioorg. Med. Chem. Lett. 17:628-635(2007) [PubMed] [Europe PMC] [Abstract] Cited for: ENZYME REGULATION.
[11]	"Phosph(on)ate as a zinc-binding group in metalloenzyme inhibitors: X-ray crystal structure of the antiviral drug foscarnet complexed to human carbonic anhydrase I." Temperini C., Innocenti A., Guerri A., Scozzafava A., Rusconi S., Supuran C.T. Bioorg. Med. Chem. Lett. 17:2210-2215(2007) [PubMed] [Europe PMC] [Abstract] Cited for: ENZYME REGULATION.
[12]	"A thiabendazole sulfonamide shows potent inhibitory activity against mammalian and nematode alpha-carbonic anhydrases." Crocetti L., Maresca A., Temperini C., Hall R.A., Scozzafava A., Muehlschlegel F.A., Supuran C.T. Bioorg. Med. Chem. Lett. 19:1371-1375(2009) [PubMed] [Europe PMC] [Abstract] Cited for: ENZYME REGULATION.
[13]	"Non-zinc mediated inhibition of carbonic anhydrases: coumarins are a new class of suicide inhibitors." Maresca A., Temperini C., Vu H., Pham N.B., Poulsen S.-A., Scozzafava A., Quinn R.J., Supuran C.T. J. Am. Chem. Soc. 131:3057-3062(2009) [PubMed] [Europe PMC] [Abstract] Cited for: ENZYME REGULATION.
[14]	"Crystal structure of human carbonic anhydrase XIII and its complex with the inhibitor acetazolamide." Di Fiore A., Monti S.M., Hilvo M., Parkkila S., Romano V., Scaloni A., Pedone C., Scozzafava A., Supuran C.T., De Simone G. Proteins 74:164-175(2009) [PubMed] [Europe PMC] [Abstract] Cited for: BIOPHYSICOCHEMICAL PROPERTIES, ENZYME REGULATION.
[15]	"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation." Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B. Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-325, MASS SPECTROMETRY.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AB025904 mRNA. Translation: BAA85002.1. AY358689 mRNA. Translation: AAQ89052.1. AK074765 mRNA. Translation: BAC11191.1. BT020054 mRNA. Translation: AAV38857.1. AL138795 Genomic DNA. Translation: CAI22810.1. BC034412 mRNA. Translation: AAH34412.1.
IPI	IPI00008504.
RefSeq	NP_036245.1. NM_012113.1.
UniGene	Hs.528988.
3D structure databases
ProteinModelPortal	Q9ULX7.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q9ULX7. 1 interaction.
STRING	9606.ENSP00000358107.
PTM databases
PhosphoSite	Q9ULX7.
Polymorphism databases
DMDM	8928036.
Proteomic databases
PaxDb	Q9ULX7.
PRIDE	Q9ULX7.
Protocols and materials databases
DNASU	23632.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000369111; ENSP00000358107; ENSG00000118298. ENST00000582010; ENSP00000462389; ENSG00000264654.
GeneID	23632.
KEGG	hsa:23632.
UCSC	uc001etx.3. human.
Organism-specific databases
CTD	23632.
GeneCards	GC01P150230.
HGNC	HGNC:1372. CA14.
HPA	HPA008482.
MIM	604832. gene.
neXtProt	NX_Q9ULX7.
PharmGKB	PA25988.
GenAtlas	Search...
Phylogenomic databases
eggNOG	COG3338.
HOGENOM	HOG000112637.
HOVERGEN	HBG002837.
InParanoid	Q9ULX7.
KO	K01672.
OMA	GPHGQDH.
OrthoDB	EOG45MN5P.
PhylomeDB	Q9ULX7.
Enzyme and pathway databases
BRENDA	4.2.1.1. 2681.
Reactome	REACT_111217. Metabolism.
SABIO-RK	Q9ULX7.
Gene expression databases
ArrayExpress	Q9ULX7.
Bgee	Q9ULX7.
CleanEx	HS_CA14.
Genevestigator	Q9ULX7.
GermOnline	ENSG00000118298. Homo sapiens.
Family and domain databases
Gene3D	3.10.200.10. 1 hit.
InterPro	IPR001148. Carbonic_anhydrase_a. IPR023561. Carbonic_anhydrase_a-class. IPR018431. Carbonic_anhydrase_CA14. [Graphical view]
PANTHER	PTHR18952. PTHR18952. 1 hit. PTHR18952:SF20. PTHR18952:SF20. 1 hit.
Pfam	PF00194. Carb_anhydrase. 1 hit. [Graphical view]
SMART	SM01057. Carb_anhydrase. 1 hit. [Graphical view]
SUPFAM	SSF51069. Euk_COanhd. 1 hit.
PROSITE	PS00162. ALPHA_CA_1. False negative. PS51144. ALPHA_CA_2. 1 hit. [Graphical view]
ProtoNet	Search...
Other
BindingDB	Q9ULX7.
ChEMBL	CHEMBL3510.
ChiTaRS	CA14. human.
GenomeRNAi	23632.
NextBio	46407.
SOURCE	Search...

Entry information

Entry name

CAH14_HUMAN

Accession

Primary (citable) accession number: Q9ULX7
Secondary accession number(s): Q5TB24, Q8NCF4

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 1, 2000
Last sequence update:	May 1, 2000
Last modified:	May 1, 2013
This is version 119 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

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