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   03-AUG-2022, entry version 107.
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}.
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; 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; Q5PPN4; -.
DR   PRIDE; Q5PPN4; -.
DR   Ensembl; ENSRNOT00000007802; ENSRNOP00000007802; ENSRNOG00000005669.
DR   GeneID; 297814; -.
DR   KEGG; rno:297814; -.
DR   UCSC; RGD:1304709; rat.
DR   CTD; 767; -.
DR   RGD; 1304709; Ca8.
DR   eggNOG; KOG0382; Eukaryota.
DR   GeneTree; ENSGT00940000158863; -.
DR   InParanoid; Q5PPN4; -.
DR   OMA; THNEREM; -.
DR   OrthoDB; 1377476at2759; -.
DR   PhylomeDB; Q5PPN4; -.
DR   TreeFam; TF316425; -.
DR   PRO; PR:Q5PPN4; -.
DR   Proteomes; UP000002494; Chromosome 5.
DR   Bgee; ENSRNOG00000005669; Expressed in cerebellum and 19 other 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:0048015; P:phosphatidylinositol-mediated signaling; ISO:RGD.
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   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