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P22748

- CAH4_HUMAN

UniProt

P22748 - CAH4_HUMAN

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Protein

Carbonic anhydrase 4

Gene

CA4

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

Functioni

Reversible hydration of carbon dioxide. May stimulate the sodium/bicarbonate transporter activity of SLC4A4 that acts in pH homeostasis. It is essential for acid overload removal from the retina and retina epithelium, and acid release in the choriocapillaris in the choroid.1 Publication

Catalytic activityi

H2CO3 = CO2 + H2O.

Cofactori

Zinc.

Enzyme regulationi

Activated by histamine, L-adrenaline, D-phenylalanine, L- and D-histidine. Inhibited by coumarins, saccharin, sulfonamide derivatives such as acetazolamide and Foscarnet (phosphonoformate trisodium salt).8 Publications

Kineticsi

  1. KM=21.5 mM for CO21 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei88 – 881Proton acceptorBy similarity
Metal bindingi115 – 1151Zinc; catalytic
Metal bindingi117 – 1171Zinc; catalytic
Metal bindingi140 – 1401Zinc; catalytic

GO - Molecular functioni

  1. carbonate dehydratase activity Source: Reactome
  2. zinc ion binding Source: InterPro

GO - Biological processi

  1. bicarbonate transport Source: DFLAT
  2. one-carbon metabolic process Source: InterPro
  3. organ development Source: Ensembl
  4. response to drug Source: Ensembl
  5. response to steroid hormone Source: Ensembl
  6. small molecule metabolic process Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Lyase

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

BRENDAi4.2.1.1. 2681.
ReactomeiREACT_121123. Reversible hydration of carbon dioxide.
REACT_121329. Erythrocytes take up carbon dioxide and release oxygen.
REACT_121380. Erythrocytes take up oxygen and release carbon dioxide.
SABIO-RKP22748.

Names & Taxonomyi

Protein namesi
Recommended name:
Carbonic anhydrase 4 (EC:4.2.1.1)
Alternative name(s):
Carbonate dehydratase IV
Carbonic anhydrase IV
Short name:
CA-IV
Gene namesi
Name:CA4
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 17

Organism-specific databases

HGNCiHGNC:1375. CA4.

Subcellular locationi

GO - Cellular componenti

  1. anchored component of external side of plasma membrane Source: DFLAT
  2. apical plasma membrane Source: DFLAT
  3. brush border membrane Source: DFLAT
  4. cell surface Source: DFLAT
  5. endoplasmic reticulum-Golgi intermediate compartment Source: DFLAT
  6. extracellular vesicular exosome Source: UniProtKB
  7. Golgi apparatus Source: DFLAT
  8. membrane Source: ProtInc
  9. perinuclear region of cytoplasm Source: DFLAT
  10. plasma membrane Source: UniProtKB
  11. rough endoplasmic reticulum Source: DFLAT
  12. sarcolemma Source: Ensembl
  13. sarcoplasmic reticulum Source: Ensembl
  14. secretory granule membrane Source: DFLAT
  15. trans-Golgi network Source: DFLAT
  16. transport vesicle membrane Source: DFLAT
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

Pathology & Biotechi

Involvement in diseasei

Retinitis pigmentosa 17 (RP17) [MIM:600852]: A retinal dystrophy belonging to the group of pigmentary retinopathies. Retinitis pigmentosa is characterized by retinal pigment deposits visible on fundus examination and primary loss of rod photoreceptor cells followed by secondary loss of cone photoreceptors. Patients typically have night vision blindness and loss of midperipheral visual field. As their condition progresses, they lose their far peripheral visual field and eventually central vision as well.3 Publications
Note: The disease is caused by mutations affecting the gene represented in this entry. Defective acid overload removal from retina and retinal epithelium, due to mutant CA4, is responsible for photoreceptor degeneration, indicating that impaired pH homeostasis is the most likely cause underlying the RP17 phenotype.
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti12 – 121A → T in RP17. 1 Publication
VAR_071430
Natural varianti14 – 141R → W in RP17; abolishes interaction with SLC4A4; impaired SLC4A4 cotransporter activity stimulation. 1 Publication
VAR_024749
Natural varianti69 – 691R → H in RP17; has no effect on catalytic activity; loss of interaction with SLC4A4. 1 Publication
VAR_071431
Natural varianti219 – 2191R → S in RP17; no catalytic activity; impaired SLC4A4 cotransporter activity stimulation. 1 Publication
VAR_024750

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi284 – 2841S → F: Loss of C-terminal domain removal and inactivation. 1 Publication

Keywords - Diseasei

Disease mutation, Retinitis pigmentosa

Organism-specific databases

MIMi600852. phenotype.
Orphaneti791. Retinitis pigmentosa.
PharmGKBiPA25991.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 18181 PublicationAdd
BLAST
Chaini19 – 284266Carbonic anhydrase 4PRO_0000004226Add
BLAST
Propeptidei285 – 31228Removed in mature formPRO_0000004227Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi24 ↔ 361 Publication
Disulfide bondi46 ↔ 2291 Publication
Lipidationi284 – 2841GPI-anchor amidated serine1 Publication

Keywords - PTMi

Disulfide bond, Glycoprotein, GPI-anchor, Lipoprotein

Proteomic databases

PaxDbiP22748.
PRIDEiP22748.

PTM databases

PhosphoSiteiP22748.

Expressioni

Tissue specificityi

Expressed in the endothelium of the choriocapillaris in eyes (at protein level). Not expressed in the retinal epithelium at detectable levels.1 Publication

Gene expression databases

BgeeiP22748.
CleanExiHS_CA4.
ExpressionAtlasiP22748. baseline and differential.
GenevestigatoriP22748.

Organism-specific databases

HPAiHPA011089.
HPA017258.

Interactioni

Subunit structurei

Interacts with SLC4A4.4 Publications

Protein-protein interaction databases

BioGridi107217. 4 interactions.
IntActiP22748. 4 interactions.
STRINGi9606.ENSP00000300900.

Structurei

Secondary structure

1
312
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi26 – 294
Helixi39 – 413
Turni44 – 474
Beta strandi48 – 503
Helixi58 – 603
Beta strandi61 – 633
Beta strandi70 – 778
Beta strandi82 – 854
Beta strandi87 – 937
Beta strandi99 – 1024
Beta strandi109 – 11810
Beta strandi127 – 1304
Beta strandi136 – 14510
Beta strandi162 – 17514
Helixi178 – 1803
Helixi181 – 1866
Helixi187 – 1893
Beta strandi196 – 1983
Helixi205 – 2073
Helixi211 – 2144
Beta strandi217 – 2226
Beta strandi233 – 2408
Beta strandi242 – 2454
Helixi246 – 25510
Beta strandi257 – 2593
Beta strandi264 – 2663

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1ZNCX-ray2.80A/B19-284[»]
3F7BX-ray2.05A/B19-284[»]
3F7UX-ray2.00A/B/C/D19-284[»]
3FW3X-ray1.72A/B19-284[»]
ProteinModelPortaliP22748.
SMRiP22748. Positions 23-284.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP22748.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni225 – 2262Substrate bindingCurated

Sequence similaritiesi

Belongs to the alpha-carbonic anhydrase family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiCOG3338.
GeneTreeiENSGT00760000118915.
HOGENOMiHOG000112637.
HOVERGENiHBG002837.
InParanoidiP22748.
KOiK18246.
OMAiKGTSRNV.
OrthoDBiEOG7MD4QN.
PhylomeDBiP22748.
TreeFamiTF316425.

Family and domain databases

Gene3Di3.10.200.10. 1 hit.
InterProiIPR001148. Carbonic_anhydrase_a.
IPR023561. Carbonic_anhydrase_a-class.
IPR018338. Carbonic_anhydrase_a-class_CS.
IPR018343. Carbonic_anhydrase_CA4.
[Graphical view]
PANTHERiPTHR18952. PTHR18952. 1 hit.
PTHR18952:SF95. PTHR18952:SF95. 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]

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. Align

Isoform 1 (identifier: P22748) [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
MRMLLALLAL SAARPSASAE SHWCYEVQAE SSNYPCLVPV KWGGNCQKDR
60 70 80 90 100
QSPINIVTTK AKVDKKLGRF FFSGYDKKQT WTVQNNGHSV MMLLENKASI
110 120 130 140 150
SGGGLPAPYQ AKQLHLHWSD LPYKGSEHSL DGEHFAMEMH IVHEKEKGTS
160 170 180 190 200
RNVKEAQDPE DEIAVLAFLV EAGTQVNEGF QPLVEALSNI PKPEMSTTMA
210 220 230 240 250
ESSLLDLLPK EEKLRHYFRY LGSLTTPTCD EKVVWTVFRE PIQLHREQIL
260 270 280 290 300
AFSQKLYYDK EQTVSMKDNV RPLQQLGQRT VIKSGAPGRP LPWALPALLG
310
PMLACLLAGF LR
Length:312
Mass (Da):35,032
Last modified:August 1, 1992 - v2
Checksum:iEF5F182474ABE9B0
GO
Isoform 2 (identifier: P22748-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     90-106: VMMLLENKASISGGGLP → GWNPGERGLPATGGGTV
     107-312: Missing.

Note: No experimental confirmation available.

Show »
Length:106
Mass (Da):11,599
Checksum:i0149FBF9A98FFF2B
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti24 – 241C → E AA sequence (PubMed:2111324)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti12 – 121A → T in RP17. 1 Publication
VAR_071430
Natural varianti14 – 141R → W in RP17; abolishes interaction with SLC4A4; impaired SLC4A4 cotransporter activity stimulation. 1 Publication
VAR_024749
Natural varianti69 – 691R → H in RP17; has no effect on catalytic activity; loss of interaction with SLC4A4. 1 Publication
VAR_071431
Natural varianti177 – 1771N → K.1 Publication
VAR_071432
Natural varianti219 – 2191R → S in RP17; no catalytic activity; impaired SLC4A4 cotransporter activity stimulation. 1 Publication
VAR_024750
Natural varianti237 – 2371V → L.
Corresponds to variant rs2229178 [ dbSNP | Ensembl ].
VAR_048680

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei90 – 10617VMMLL…GGGLP → GWNPGERGLPATGGGTV in isoform 2. 1 PublicationVSP_055973Add
BLAST
Alternative sequencei107 – 312206Missing in isoform 2. 1 PublicationVSP_055974Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M83670 mRNA. Translation: AAA35630.1.
L10955
, L10951, L10953, L10954 Genomic DNA. Translation: AAA35625.1. Sequence problems.
L10955, L10954 Genomic DNA. Translation: AAA35626.1. Sequence problems.
AK289715 mRNA. Translation: BAF82404.1.
AK298710 mRNA. Translation: BAG60866.1.
CR541766 mRNA. Translation: CAG46565.1.
AC025048 Genomic DNA. No translation available.
CH471109 Genomic DNA. Translation: EAW94362.1.
BC057792 mRNA. Translation: AAH57792.1.
BC069649 mRNA. Translation: AAH69649.1.
BC074768 mRNA. Translation: AAH74768.1.
CCDSiCCDS11624.1. [P22748-1]
PIRiA45745. CRHU4.
RefSeqiNP_000708.1. NM_000717.3.
UniGeneiHs.89485.

Genome annotation databases

EnsembliENST00000300900; ENSP00000300900; ENSG00000167434. [P22748-1]
ENST00000586876; ENSP00000467465; ENSG00000167434. [P22748-2]
GeneIDi762.
KEGGihsa:762.
UCSCiuc002iym.4. human. [P22748-1]

Polymorphism databases

DMDMi115465.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M83670 mRNA. Translation: AAA35630.1 .
L10955
, L10951 , L10953 , L10954 Genomic DNA. Translation: AAA35625.1 . Sequence problems.
L10955 , L10954 Genomic DNA. Translation: AAA35626.1 . Sequence problems.
AK289715 mRNA. Translation: BAF82404.1 .
AK298710 mRNA. Translation: BAG60866.1 .
CR541766 mRNA. Translation: CAG46565.1 .
AC025048 Genomic DNA. No translation available.
CH471109 Genomic DNA. Translation: EAW94362.1 .
BC057792 mRNA. Translation: AAH57792.1 .
BC069649 mRNA. Translation: AAH69649.1 .
BC074768 mRNA. Translation: AAH74768.1 .
CCDSi CCDS11624.1. [P22748-1 ]
PIRi A45745. CRHU4.
RefSeqi NP_000708.1. NM_000717.3.
UniGenei Hs.89485.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1ZNC X-ray 2.80 A/B 19-284 [» ]
3F7B X-ray 2.05 A/B 19-284 [» ]
3F7U X-ray 2.00 A/B/C/D 19-284 [» ]
3FW3 X-ray 1.72 A/B 19-284 [» ]
ProteinModelPortali P22748.
SMRi P22748. Positions 23-284.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 107217. 4 interactions.
IntActi P22748. 4 interactions.
STRINGi 9606.ENSP00000300900.

Chemistry

BindingDBi P22748.
ChEMBLi CHEMBL3729.
DrugBanki DB00819. Acetazolamide.
DB00436. Bendroflumethiazide.
DB00562. Benzthiazide.
DB01194. Brinzolamide.
DB00880. Chlorothiazide.
DB00606. Cyclothiazide.
DB01144. Diclofenamide.
DB00869. Dorzolamide.
DB00999. Hydrochlorothiazide.
DB00774. Hydroflumethiazide.
DB00703. Methazolamide.
DB00232. Methyclothiazide.
DB00273. Topiramate.
DB01021. Trichlormethiazide.
DB00909. Zonisamide.
GuidetoPHARMACOLOGYi 2599.

PTM databases

PhosphoSitei P22748.

Polymorphism databases

DMDMi 115465.

Proteomic databases

PaxDbi P22748.
PRIDEi P22748.

Protocols and materials databases

DNASUi 762.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000300900 ; ENSP00000300900 ; ENSG00000167434 . [P22748-1 ]
ENST00000586876 ; ENSP00000467465 ; ENSG00000167434 . [P22748-2 ]
GeneIDi 762.
KEGGi hsa:762.
UCSCi uc002iym.4. human. [P22748-1 ]

Organism-specific databases

CTDi 762.
GeneCardsi GC17P058227.
GeneReviewsi CA4.
HGNCi HGNC:1375. CA4.
HPAi HPA011089.
HPA017258.
MIMi 114760. gene.
600852. phenotype.
neXtProti NX_P22748.
Orphaneti 791. Retinitis pigmentosa.
PharmGKBi PA25991.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG3338.
GeneTreei ENSGT00760000118915.
HOGENOMi HOG000112637.
HOVERGENi HBG002837.
InParanoidi P22748.
KOi K18246.
OMAi KGTSRNV.
OrthoDBi EOG7MD4QN.
PhylomeDBi P22748.
TreeFami TF316425.

Enzyme and pathway databases

BRENDAi 4.2.1.1. 2681.
Reactomei REACT_121123. Reversible hydration of carbon dioxide.
REACT_121329. Erythrocytes take up carbon dioxide and release oxygen.
REACT_121380. Erythrocytes take up oxygen and release carbon dioxide.
SABIO-RK P22748.

Miscellaneous databases

EvolutionaryTracei P22748.
GeneWikii Carbonic_anhydrase_4.
GenomeRNAii 762.
NextBioi 3082.
PROi P22748.
SOURCEi Search...

Gene expression databases

Bgeei P22748.
CleanExi HS_CA4.
ExpressionAtlasi P22748. baseline and differential.
Genevestigatori P22748.

Family and domain databases

Gene3Di 3.10.200.10. 1 hit.
InterProi IPR001148. Carbonic_anhydrase_a.
IPR023561. Carbonic_anhydrase_a-class.
IPR018338. Carbonic_anhydrase_a-class_CS.
IPR018343. Carbonic_anhydrase_CA4.
[Graphical view ]
PANTHERi PTHR18952. PTHR18952. 1 hit.
PTHR18952:SF95. PTHR18952:SF95. 1 hit.
Pfami PF00194. Carb_anhydrase. 1 hit.
[Graphical view ]
SMARTi SM01057. Carb_anhydrase. 1 hit.
[Graphical view ]
SUPFAMi SSF51069. SSF51069. 1 hit.
PROSITEi PS00162. ALPHA_CA_1. 1 hit.
PS51144. ALPHA_CA_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Human carbonic anhydrase IV: cDNA cloning, sequence comparison, and expression in COS cell membranes."
    Okuyama T., Sato S., Zhu X.L., Waheed A., Sly W.S.
    Proc. Natl. Acad. Sci. U.S.A. 89:1315-1319(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  2. "Genomic organization and localization of gene for human carbonic anhydrase IV to chromosome 17q."
    Okuyama T., Batanian J.R., Sly W.S.
    Genomics 16:678-684(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  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] (ISOFORMS 1 AND 2).
    Tissue: Brain.
  4. "Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
    Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.
    Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
  5. "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].
  6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  7. "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] (ISOFORM 1).
    Tissue: Brain and Placenta.
  8. "Carbonic anhydrase IV from human lung. Purification, characterization, and comparison with membrane carbonic anhydrase from human kidney."
    Zhu X.L., Sly W.S.
    J. Biol. Chem. 265:8795-8801(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 19-35; 113-123 AND 233-239.
    Tissue: Lung.
  9. "Carbonic anhydrase IV: purification of a secretory form of the recombinant human enzyme and identification of the positions and importance of its disulfide bonds."
    Waheed A., Okuyama T., Heyduk T., Sly W.S.
    Arch. Biochem. Biophys. 333:432-438(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: DISULFIDE BONDS.
  10. "Carbonic anhydrase IV: role of removal of C-terminal domain in glycosylphosphatidylinositol anchoring and realization of enzyme activity."
    Okuyama T., Waheed A., Kusumoto W., Zhu X.L., Sly W.S.
    Arch. Biochem. Biophys. 320:315-322(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: GPI-ANCHOR AT SER-284, MUTAGENESIS OF SER-284.
  11. "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.
  12. "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.
  13. "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.
  14. "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.
  15. "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.
  16. "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.
  17. "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.
  18. "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.
  19. "Crystal structure of the secretory form of membrane-associated human carbonic anhydrase IV at 2.8-A resolution."
    Stams T., Nair S.K., Okuyama T., Waheed A., Sly W.S., Christianson D.W.
    Proc. Natl. Acad. Sci. U.S.A. 93:13589-13594(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.80 ANGSTROMS) OF 19-284 IN COMPLEX WITH ZINC ION.
  20. "Thioether benzenesulfonamide inhibitors of carbonic anhydrases II and IV: structure-based drug design, synthesis, and biological evaluation."
    Vernier W.F., Chong W., Rewolinski D., Greasley S., Pauly T.A., Shaw M., Dinh D.M., Ferre R.A.A., Meador J.W. III, Nukui S., Ornelas M., Paz R.L., Reyner E.
    Bioorg. Med. Chem. 18:3307-3319(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 19-284 IN COMPLEX WITH INHIBITORS.
  21. Cited for: INVOLVEMENT IN RP17, VARIANTS RP17 TRP-14 AND SER-219, FUNCTION, TISSUE SPECIFICITY, INTERACTION WITH SLC4A4.
  22. "Identification and characterization of a novel mutation in the carbonic anhydrase IV gene that causes retinitis pigmentosa."
    Alvarez B.V., Vithana E.N., Yang Z., Koh A.H., Yeung K., Yong V., Shandro H.J., Chen Y., Kolatkar P., Palasingam P., Zhang K., Aung T., Casey J.R.
    Invest. Ophthalmol. Vis. Sci. 48:3459-3468(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH SLC4A4, VARIANT RP17 HIS-69, VARIANT LYS-177, CHARACTERIZATION OF VARIANT RP17 HIS-69.
  23. "Screening for the carbonic anhydrase IV gene mutations in Chinese retinitis pigmentosa patients."
    Tian Y., Tang L., Cui J., Zhu X.
    Curr. Eye Res. 35:440-444(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT RP17 THR-12.

Entry informationi

Entry nameiCAH4_HUMAN
AccessioniPrimary (citable) accession number: P22748
Secondary accession number(s): B4DQA4, Q6FHI7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1991
Last sequence update: August 1, 1992
Last modified: October 29, 2014
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 17
    Human chromosome 17: 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

External Data

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