CAH8_MOUSE
ID CAH8_MOUSE Reviewed; 291 AA.
AC P28651; Q8CF58; Q91XF6;
DT 01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 5.
DT 03-AUG-2022, entry version 160.
DE RecName: Full=Carbonic anhydrase-related protein;
DE Short=CARP;
DE AltName: Full=Carbonic anhydrase VIII;
DE Short=CA-VIII;
GN Name=Ca8; Synonyms=Cals, Cals1, Car8, Carp;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=BALB/cJ; TISSUE=Brain;
RX PubMed=2121526; DOI=10.1016/0014-5793(90)80390-5;
RA Kato K.;
RT "Sequence of a novel carbonic anhydrase-related polypeptide and its
RT exclusive presence in Purkinje cells.";
RL FEBS Lett. 271:137-140(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF N-TERMINUS, AND
RP MUTAGENESIS.
RX PubMed=8977131; DOI=10.1016/s0014-5793(96)01263-x;
RA Sjoeblom B., Elleby B., Wallgren K., Jonsson B.-H., Lindskog S.;
RT "Two point mutations convert a catalytically inactive carbonic anhydrase-
RT related protein (CARP) to an active enzyme.";
RL FEBS Lett. 398:322-325(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Liver;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Colon;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Liver, and Lung;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Does not have a carbonic anhydrase catalytic activity.
CC -!- TISSUE SPECIFICITY: Expressed only in Purkinje cells.
CC -!- SIMILARITY: Belongs to the alpha-carbonic anhydrase family.
CC {ECO:0000305}.
CC -!- CAUTION: Although it belongs to the alpha-carbonic anhydrase family,
CC Arg-117 is present instead of the conserved His which is a zinc-binding
CC residue. It is therefore expected that this protein lacks carbonic
CC anhydrase activity. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; X61397; CAA43668.1; -; mRNA.
DR EMBL; AK004896; BAC25100.1; -; mRNA.
DR EMBL; BC010773; AAH10773.1; -; mRNA.
DR CCDS; CCDS17954.1; -.
DR PIR; S12867; S12867.
DR RefSeq; NP_031618.2; NM_007592.3.
DR AlphaFoldDB; P28651; -.
DR SMR; P28651; -.
DR BioGRID; 198459; 4.
DR STRING; 10090.ENSMUSP00000063511; -.
DR iPTMnet; P28651; -.
DR PhosphoSitePlus; P28651; -.
DR SwissPalm; P28651; -.
DR jPOST; P28651; -.
DR MaxQB; P28651; -.
DR PaxDb; P28651; -.
DR PeptideAtlas; P28651; -.
DR PRIDE; P28651; -.
DR ProteomicsDB; 265423; -.
DR Antibodypedia; 11840; 292 antibodies from 35 providers.
DR DNASU; 12319; -.
DR Ensembl; ENSMUST00000066674; ENSMUSP00000063511; ENSMUSG00000041261.
DR GeneID; 12319; -.
DR KEGG; mmu:12319; -.
DR UCSC; uc008rxv.1; mouse.
DR CTD; 12319; -.
DR MGI; MGI:88253; Car8.
DR VEuPathDB; HostDB:ENSMUSG00000041261; -.
DR eggNOG; KOG0382; Eukaryota.
DR GeneTree; ENSGT00940000158863; -.
DR HOGENOM; CLU_039326_2_1_1; -.
DR InParanoid; P28651; -.
DR OMA; THNEREM; -.
DR OrthoDB; 1377476at2759; -.
DR PhylomeDB; P28651; -.
DR TreeFam; TF316425; -.
DR BioGRID-ORCS; 12319; 1 hit in 73 CRISPR screens.
DR ChiTaRS; Car8; mouse.
DR PRO; PR:P28651; -.
DR Proteomes; UP000000589; Chromosome 4.
DR RNAct; P28651; protein.
DR Bgee; ENSMUSG00000041261; Expressed in cerebellum lobe and 231 other tissues.
DR Genevisible; P28651; MM.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0004089; F:carbonate dehydratase activity; IEA:InterPro.
DR GO; GO:0016836; F:hydro-lyase activity; IBA:GO_Central.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006730; P:one-carbon metabolic process; IBA:GO_Central.
DR GO; GO:0048015; P:phosphatidylinositol-mediated signaling; IDA:MGI.
DR CDD; cd03120; alpha_CARP_VIII; 1.
DR Gene3D; 3.10.200.10; -; 1.
DR InterPro; IPR001148; CA_dom.
DR InterPro; IPR036398; CA_dom_sf.
DR InterPro; IPR023561; Carbonic_anhydrase_a-class.
DR InterPro; IPR018338; Carbonic_anhydrase_a-class_CS.
DR InterPro; IPR041877; CARP_VIII.
DR PANTHER; PTHR18952; PTHR18952; 1.
DR Pfam; PF00194; Carb_anhydrase; 1.
DR SMART; SM01057; Carb_anhydrase; 1.
DR SUPFAM; SSF51069; SSF51069; 1.
DR PROSITE; PS00162; ALPHA_CA_1; 1.
DR PROSITE; PS51144; ALPHA_CA_2; 1.
PE 1: Evidence at protein level;
KW Direct protein sequencing; Metal-binding; Phosphoprotein;
KW Reference proteome; Zinc.
FT CHAIN 1..291
FT /note="Carbonic anhydrase-related protein"
FT /id="PRO_0000077434"
FT DOMAIN 28..290
FT /note="Alpha-carbonic anhydrase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01134"
FT REGION 1..28
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 13..28
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 88
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000250|UniProtKB:P00918"
FT BINDING 119
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255"
FT BINDING 142
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255"
FT SITE 117
FT /note="Ancestral zinc ligand"
FT MOD_RES 5
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5PPN4"
FT MUTAGEN 115..117
FT /note="EVR->QVH: Restores zinc-binding and activity."
FT /evidence="ECO:0000269|PubMed:8977131"
FT CONFLICT 261
FT /note="A -> V (in Ref. 1; CAA43668)"
FT /evidence="ECO:0000305"
FT CONFLICT 285
FT /note="V -> I (in Ref. 3; BAC25100)"
FT /evidence="ECO:0000305"
FT CONFLICT 291
FT /note="Q -> SSQRDREQTHLHQ (in Ref. 1; CAA43668)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 291 AA; 33081 MW; FAA2B1678A9AEF54 CRC64;
MADLSFIEDA VAFPEKEEDE EEEEEEGVEW GYEEGVEWGL VFPDANGEYQ SPINLNSREA
RYDPSLLDVR LSPNYVVCRD CEVTNDGHTI QVILKSKSVL SGGPLPQGQE FELYEVRFHW
GRENQRGSEH TVNFKAFPME LHLIHWNSTL FGSIDEAVGK PHGIAIIALF VQIGKEHVGL
KAVTEILQDI QYKGKSKTIP CFNPNTLLPD PLLRDYWVYE GSLTIPPCSE GVTWILFRYP
LTISQMQIEE FRRLRTHVKG AELVEGCDGI LGDNFRPTQP LSDRVIRAAF Q
