ID CAH8_RAT Reviewed; 290 AA.
AC Q5PPN4;
DT 13-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 27-MAR-2024, entry version 116.
DE RecName: Full=Carbonic anhydrase-related protein;
DE Short=CARP;
DE AltName: Full=Carbonic anhydrase VIII;
DE Short=CA-VIII;
GN Name=Ca8; Synonyms=Car8;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
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 [2]
RP IDENTIFICATION BY MASS SPECTROMETRY.
RA Maurya D.K., Bhargava P.;
RL Submitted (DEC-2008) to UniProtKB.
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-5, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
CC -!- FUNCTION: Does not have a carbonic anhydrase catalytic activity.
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-116 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}.
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DR EMBL; BC087586; AAH87586.1; -; mRNA.
DR RefSeq; NP_001009662.1; NM_001009662.1.
DR AlphaFoldDB; Q5PPN4; -.
DR SMR; Q5PPN4; -.
DR STRING; 10116.ENSRNOP00000007802; -.
DR iPTMnet; Q5PPN4; -.
DR PhosphoSitePlus; Q5PPN4; -.
DR jPOST; Q5PPN4; -.
DR PaxDb; 10116-ENSRNOP00000007802; -.
DR Ensembl; ENSRNOT00000007802.8; ENSRNOP00000007802.5; ENSRNOG00000005669.8.
DR Ensembl; ENSRNOT00055034772; ENSRNOP00055028191; ENSRNOG00055020347.
DR Ensembl; ENSRNOT00060028830; ENSRNOP00060023201; ENSRNOG00060016809.
DR Ensembl; ENSRNOT00065026252; ENSRNOP00065020628; ENSRNOG00065015781.
DR GeneID; 297814; -.
DR KEGG; rno:297814; -.
DR UCSC; RGD:1304709; rat.
DR AGR; RGD:1304709; -.
DR CTD; 12319; -.
DR RGD; 1304709; Ca8.
DR eggNOG; KOG0382; Eukaryota.
DR GeneTree; ENSGT00940000158863; -.
DR InParanoid; Q5PPN4; -.
DR OMA; SANGEYQ; -.
DR OrthoDB; 49814at2759; -.
DR PhylomeDB; Q5PPN4; -.
DR TreeFam; TF316425; -.
DR PRO; PR:Q5PPN4; -.
DR Proteomes; UP000002494; Chromosome 5.
DR Bgee; ENSRNOG00000005669; Expressed in cerebellum and 19 other cell types or tissues.
DR ExpressionAtlas; Q5PPN4; baseline and differential.
DR Genevisible; Q5PPN4; RN.
DR GO; GO:0005737; C:cytoplasm; ISO:RGD.
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:0050850; P:positive regulation of calcium-mediated signaling; ISO:RGD.
DR CDD; cd03120; alpha_CARP_VIII; 1.
DR Gene3D; 3.10.200.10; Alpha carbonic anhydrase; 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; CARBONIC ANHYDRASE; 1.
DR PANTHER; PTHR18952:SF104; CARBONIC ANHYDRASE-RELATED PROTEIN; 1.
DR Pfam; PF00194; Carb_anhydrase; 1.
DR SMART; SM01057; Carb_anhydrase; 1.
DR SUPFAM; SSF51069; Carbonic anhydrase; 1.
DR PROSITE; PS00162; ALPHA_CA_1; 1.
DR PROSITE; PS51144; ALPHA_CA_2; 1.
PE 1: Evidence at protein level;
KW Metal-binding; Phosphoprotein; Reference proteome; Zinc.
FT CHAIN 1..290
FT /note="Carbonic anhydrase-related protein"
FT /id="PRO_0000077435"
FT DOMAIN 27..289
FT /note="Alpha-carbonic anhydrase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01134"
FT ACT_SITE 87
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000250|UniProtKB:P00918"
FT BINDING 118
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255"
FT BINDING 141
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255"
FT SITE 116
FT /note="Ancestral zinc ligand"
FT MOD_RES 5
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
SQ SEQUENCE 290 AA; 32962 MW; 25240A2E7647EE26 CRC64;
MADLSFIEDA VAFPEKEEDE EEEEEGVEWG YEEGVEWGLV FPDANGEYQS PINLNSREAR
YDPSLLDVRL SPNYVVCRDC EVTNDGHTIQ VILKSKSVLS GGPLPQGQEF ELYEVRFHWG
RENQRGSEHT VNFKAFPMEL HLIHWNSTLF GSIDEAVGKP HGIVIIALFV QIGKEHVGLK
AVTEILQDIQ YKGKSKTIPC FNPNTLLPDP LLRDYWVYEG SLTIPPCSEG VTWILFRYPL
TISQLQIEEF RRLRTHVKGA ELVEGCDGIL GDNFRPTQPL SDRVIRAAFQ
//
