P35219 (CAH8_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Carbonic anhydrase-related protein
Short name=CARP

Alternative name(s):
Carbonic anhydrase VIII
Short name=CA-VIII

Gene names

Name:	CA8
Synonyms:	CALS

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	290 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	Does not have a carbonic anhydrase catalytic activity.
Involvement in disease	Defects in CA8 are the cause of cerebellar ataxia mental retardation and dysequilibrium syndrome type 3 (CMARQ3) [MIM:613227]. CMARQ3 is a congenital cerebellar ataxia associated with dysarthia, quadrupedal gait and mild mental retardation. Ref.8
Sequence similarities	Belongs to the alpha-carbonic anhydrase family.
Caution	Lacks the conserved His in position 116 that is important for binding the catalytic zinc ion in catalytically active family members.

Ontologies

Keywords
Disease	Disease mutation Mental retardation
Ligand	Metal-binding Zinc
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	one-carbon metabolic process Inferred from electronic annotation. Source: InterPro
Molecular function	carbonate dehydratase activity Traceable author statement. Source: ProtInc zinc ion binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

1

1

Removed By similarity

Chain

2 – 290

289

Carbonic anhydrase-related protein

PRO_0000077433

Regions

Compositional bias

15 – 36

22

Glu-rich (acidic)

Sites

Metal binding

118

1

Zinc Potential

Metal binding

141

1

Zinc Potential

Site

116

1

Ancestral zinc ligand

Natural variations

Natural variant

100

1

S → P in CMARQ3; affects protein stability owing to accelerated proteasomal degradation. Ref.8

VAR_063634

Experimental info

Sequence conflict

106

1

Q → R in BAG52209. Ref.3

Secondary structure

1

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290

Helix Strand Turn

Details...

Helix

42 – 44

3

Helix

56 – 58

3

Helix

63 – 66

4

Beta strand

71 – 73

3

Beta strand

77 – 84

8

Beta strand

89 – 92

4

Beta strand

97 – 100

4

Beta strand

110 – 118

9

Beta strand

129 – 131

3

Beta strand

137 – 146

10

Turn

147 – 149

3

Helix

153 – 156

4

Beta strand

164 – 171

8

Helix

180 – 183

4

Helix

184 – 189

6

Beta strand

195 – 199

5

Helix

203 – 206

4

Beta strand

215 – 218

4

Beta strand

232 – 238

7

Helix

244 – 250

7

Beta strand

286 – 288

3

Sequences

	Sequence		Length	Mass (Da)
	P35219 [UniParc]. Last modified January 23, 2007. Version 3. Checksum: C142711660A972DB	FASTA	290	32,973
	10 20 30 40 50 60 MADLSFIEDT VAFPEKEEDE EEEEEGVEWG YEEGVEWGLV FPDANGEYQS PINLNSREAR 70 80 90 100 110 120 YDPSLLDVRL SPNYVVCRDC EVTNDGHTIQ VILKSKSVLS GGPLPQGHEF ELYEVRFHWG 130 140 150 160 170 180 RENQRGSEHT VNFKAFPMEL HLIHWNSTLF GSIDEAVGKP HGIAIIALFV QIGKEHVGLK 190 200 210 220 230 240 AVTEILQDIQ YKGKSKTIPC FNPNTLLPDP LLRDYWVYEG SLTIPPCSEG VTWILFRYPL 250 260 270 280 290 TISQLQIEEF RRLRTHVKGA ELVEGCDGIL GDNFRPTQPL SDRVIRAAFQ

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The deduced amino acid sequence of human carbonic anhydrase-related protein (CARP) is 98% identical to the mouse homologue." Skaggs L.A., Bergenhem N.C.H., Venta P.J., Tashian R.E. Gene 126:291-292(1993) [PubMed: 8482548] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	"Molecular identification of carbonic anhydrases (CA) and CA-related (CAR) genes." Chen Y., Huang C.-H. Submitted (JAN-2002) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [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: 14702039] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Cerebellum.
[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. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (JUL-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].
[6]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed: 21269460] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[7]	"Crystal structure of human carbonic anhydrase-related protein VIII reveals the basis for catalytic silencing." Picaud S.S., Muniz J.R.C., Kramm A., Pilka E.S., Kochan G., Oppermann U., Yue W.W. Proteins 76:507-511(2009) [PubMed: 19360879] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS).
[8]	"CA8 mutations cause a novel syndrome characterized by ataxia and mild mental retardation with predisposition to quadrupedal gait." Turkmen S., Guo G., Garshasbi M., Hoffmann K., Alshalah A.J., Mischung C., Kuss A., Humphrey N., Mundlos S., Robinson P.N. PLoS Genet. 5:E1000487-E1000487(2009) [PubMed: 19461874] [Abstract] Cited for: VARIANT CMARQ3 PRO-100, CHARACTERIZATION OF VARIANT CMARQ3 PRO-100.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

L04656 mRNA. Translation: AAA35653.2.
AY075022 mRNA. Translation: AAL78170.1.
AK289470 mRNA. Translation: BAF82159.1.
AK314538 mRNA. Translation: BAG37128.1.
AK090655 mRNA. Translation: BAG52209.1.
CH471068 Genomic DNA. Translation: EAW86826.1.
BC069744 mRNA. Translation: AAH69744.1.
BC069794 mRNA. Translation: AAH69794.1.
BC108929 mRNA. Translation: AAI08930.1.

IPI

IPI00219669.

PIR

JN0576.

RefSeq

NP_004047.3. NM_004056.4.

UniGene

Hs.654388.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2W2J	X-ray	1.60	A	1-290	[»]

ProteinModelPortal

P35219.

SMR

P35219. Positions 23-290.

ModBase

Search...

Protein-protein interaction databases

IntAct

P35219. 1 interaction.

MINT

MINT-1406878.

STRING

P35219.

Polymorphism databases

DMDM

461681.

Proteomic databases

PeptideAtlas

P35219.

PRIDE

P35219.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000317995; ENSP00000314407; ENSG00000178538.

GeneID

767.

KEGG

hsa:767.

UCSC

uc003xtz.1. human.

Organism-specific databases

CTD

767.

GeneCards

GC08M061151.

H-InvDB

HIX0019739.

HGNC

HGNC:1382. CA8.

HPA

CAB025545.
CAB047309.
HPA024748.

MIM

114815. gene.
613227. phenotype.

neXtProt

NX_P35219.

PharmGKB

PA25997.

GenAtlas

Search...

Phylogenomic databases

eggNOG

prNOG08308.

GeneTree

ENSGT00560000076828.

HOGENOM

HBG717384.

HOVERGEN

HBG002837.

InParanoid

P35219.

OMA

GHEFELH.

OrthoDB

EOG4W6NWN.

PhylomeDB

P35219.

Gene expression databases

ArrayExpress

P35219.

Bgee

P35219.

CleanEx

HS_CA8.

Genevestigator

P35219.

GermOnline

ENSG00000178538. Homo sapiens.

Family and domain databases

InterPro

IPR001148. a_carbonic_anhydrase.
IPR023561. Carbonic_anhydrase_a-class.
IPR018338. Carbonic_anhydrase_a-class_CS.
IPR018434. Carbonic_anhydrase_RP_CA8.
[Graphical view]

Gene3D

G3DSA:3.10.200.10. Euk_COanhd. 1 hit.

KO

K01672.

PANTHER

PTHR18952:SF23. Carbonic_anhydrase_RP_CA8. 1 hit.
PTHR18952. Euk_COanhd. 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. 1 hit.
PS51144. ALPHA_CA_2. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

NextBio

3102.

SOURCE

Search...

Entry information

Entry name

CAH8_HUMAN

Accession

Primary (citable) accession number: P35219
Secondary accession number(s): A8K0A5, B3KQZ7, Q32MY2

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1994
Last sequence update:	January 23, 2007
Last modified:	January 25, 2012
This is version 102 of the entry and version 3 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.