ID   CAH11_HUMAN             Reviewed;         328 AA.
AC   O75493; O60596; Q6FHI1; Q9UEC4;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2000, sequence version 2.
DT   24-JAN-2024, entry version 179.
DE   RecName: Full=Carbonic anhydrase-related protein 11;
DE   AltName: Full=CA-RP XI;
DE            Short=CA-XI;
DE            Short=CARP XI;
DE   AltName: Full=Carbonic anhydrase-related protein 2;
DE            Short=CA-RP II;
DE            Short=CARP-2;
DE   Flags: Precursor;
GN   Name=CA11; Synonyms=CARP2; ORFNames=UNQ211/PRO237;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=9878543; DOI=10.1006/bbrc.1998.9449;
RA   Bellingham J., Gregory-Evans K., Gregory-Evans C.Y.;
RT   "Sequence and tissue expression of a novel human carbonic anhydrase-related
RT   protein, CARP-2, mapping to chromosome 19q13.3.";
RL   Biochem. Biophys. Res. Commun. 253:364-367(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Pancreas;
RX   PubMed=10350627; DOI=10.1016/s0167-4838(99)00067-9;
RA   Fujikawa-Adachi K., Nishimori I., Taguchi T., Yuri K., Onishi S.;
RT   "cDNA sequence, mRNA expression, and chromosomal localization of human
RT   carbonic anhydrase-related protein, CA-RP XI.";
RL   Biochim. Biophys. Acta 1431:518-524(1999).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX   PubMed=12975309; DOI=10.1101/gr.1293003;
RA   Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J.,
RA   Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P.,
RA   Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E., Heldens S., Huang A.,
RA   Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J., Lewis L., Liao D.,
RA   Mark M.R., Robbie E., Sanchez C., Schoenfeld J., Seshagiri S., Simmons L.,
RA   Singh J., Smith V., Stinson J., Vagts A., Vandlen R.L., Watanabe C.,
RA   Wieand D., Woods K., Xie M.-H., Yansura D.G., Yi S., Yu G., Yuan J.,
RA   Zhang M., Zhang Z., Goddard A.D., Wood W.I., Godowski P.J., Gray A.M.;
RT   "The secreted protein discovery initiative (SPDI), a large-scale effort to
RT   identify novel human secreted and transmembrane proteins: a bioinformatics
RT   assessment.";
RL   Genome Res. 13:2265-2270(2003).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA   Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA   Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA   Phelan M., Farmer A.;
RT   "Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
RL   Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA   Halleck A., Ebert L., Mkoundinya M., Schick M., Eisenstein S., Neubert P.,
RA   Kstrang K., Schatten R., Shen B., Henze S., Mar W., Korn B., Zuo D., Hu Y.,
RA   LaBaer J.;
RT   "Cloning of human full open reading frames in Gateway(TM) system entry
RT   vector (pDONR201).";
RL   Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Uterus;
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   [7]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 48-314.
RC   TISSUE=Brain;
RX   PubMed=9878252; DOI=10.1006/geno.1998.5585;
RA   Lovejoy D.A., Hewett-Emmett D., Porter C.A., Cepoi D., Sheffield A.,
RA   Vale W.W., Tashian R.E.;
RT   "Evolutionarily conserved, 'acatalytic' carbonic anhydrase-related protein
RT   XI contains a sequence motif present in the neuropeptide sauvagine: the
RT   human CA-RP XI gene (CA11) is embedded between the secretor gene cluster
RT   and the DBP gene at 19q13.3.";
RL   Genomics 54:484-493(1998).
RN   [8]
RP   GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-118.
RC   TISSUE=Plasma;
RX   PubMed=16335952; DOI=10.1021/pr0502065;
RA   Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E., Moore R.J.,
RA   Smith R.D.;
RT   "Human plasma N-glycoproteome analysis by immunoaffinity subtraction,
RT   hydrazide chemistry, and mass spectrometry.";
RL   J. Proteome Res. 4:2070-2080(2005).
CC   -!- FUNCTION: Does not have a catalytic activity.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
CC   -!- TISSUE SPECIFICITY: Expressed abundantly in the brain with moderate
CC       expression also present in spinal cord and thyroid.
CC   -!- SIMILARITY: Belongs to the alpha-carbonic anhydrase family.
CC       {ECO:0000305}.
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DR   EMBL; AF067662; AAC99689.1; -; mRNA.
DR   EMBL; AB018195; BAA36840.1; -; mRNA.
DR   EMBL; AY358967; AAQ89326.1; -; mRNA.
DR   EMBL; CR541772; CAG46571.1; -; mRNA.
DR   EMBL; BT007265; AAP35929.1; -; mRNA.
DR   EMBL; BC002662; AAH02662.1; -; mRNA.
DR   EMBL; AF050106; AAD08802.1; -; mRNA.
DR   CCDS; CCDS12729.1; -.
DR   PIR; JE0375; JE0375.
DR   RefSeq; NP_001208.2; NM_001217.4.
DR   AlphaFoldDB; O75493; -.
DR   SMR; O75493; -.
DR   BioGRID; 107224; 13.
DR   IntAct; O75493; 5.
DR   STRING; 9606.ENSP00000084798; -.
DR   BindingDB; O75493; -.
DR   ChEMBL; CHEMBL2420; -.
DR   DrugBank; DB00909; Zonisamide.
DR   GlyCosmos; O75493; 3 sites, No reported glycans.
DR   GlyGen; O75493; 3 sites.
DR   iPTMnet; O75493; -.
DR   PhosphoSitePlus; O75493; -.
DR   BioMuta; CA11; -.
DR   MassIVE; O75493; -.
DR   PaxDb; 9606-ENSP00000084798; -.
DR   PeptideAtlas; O75493; -.
DR   ProteomicsDB; 50047; -.
DR   Antibodypedia; 31755; 128 antibodies from 24 providers.
DR   DNASU; 770; -.
DR   Ensembl; ENST00000084798.9; ENSP00000084798.3; ENSG00000063180.9.
DR   GeneID; 770; -.
DR   KEGG; hsa:770; -.
DR   MANE-Select; ENST00000084798.9; ENSP00000084798.3; NM_001217.5; NP_001208.2.
DR   UCSC; uc002pjz.2; human.
DR   AGR; HGNC:1370; -.
DR   CTD; 770; -.
DR   DisGeNET; 770; -.
DR   GeneCards; CA11; -.
DR   HGNC; HGNC:1370; CA11.
DR   HPA; ENSG00000063180; Tissue enriched (brain).
DR   MIM; 604644; gene.
DR   neXtProt; NX_O75493; -.
DR   OpenTargets; ENSG00000063180; -.
DR   PharmGKB; PA25986; -.
DR   VEuPathDB; HostDB:ENSG00000063180; -.
DR   eggNOG; KOG0382; Eukaryota.
DR   GeneTree; ENSGT00940000162098; -.
DR   HOGENOM; CLU_039326_7_0_1; -.
DR   InParanoid; O75493; -.
DR   OMA; HKNQNAC; -.
DR   OrthoDB; 49814at2759; -.
DR   PhylomeDB; O75493; -.
DR   TreeFam; TF352926; -.
DR   PathwayCommons; O75493; -.
DR   SignaLink; O75493; -.
DR   BioGRID-ORCS; 770; 27 hits in 1161 CRISPR screens.
DR   ChiTaRS; CA11; human.
DR   GeneWiki; CA11; -.
DR   GenomeRNAi; 770; -.
DR   Pharos; O75493; Tchem.
DR   PRO; PR:O75493; -.
DR   Proteomes; UP000005640; Chromosome 19.
DR   RNAct; O75493; Protein.
DR   Bgee; ENSG00000063180; Expressed in right hemisphere of cerebellum and 176 other cell types or tissues.
DR   ExpressionAtlas; O75493; baseline and differential.
DR   GO; GO:0016323; C:basolateral plasma membrane; IBA:GO_Central.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
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   CDD; cd03121; alpha_CARP_X_XI_like; 1.
DR   Gene3D; 3.10.200.10; Alpha carbonic anhydrase; 1.
DR   InterPro; IPR041878; Alpha_CARP_X/XI.
DR   InterPro; IPR001148; CA_dom.
DR   InterPro; IPR036398; CA_dom_sf.
DR   InterPro; IPR023561; Carbonic_anhydrase_a-class.
DR   PANTHER; PTHR18952; CARBONIC ANHYDRASE; 1.
DR   PANTHER; PTHR18952:SF93; CARBONIC ANHYDRASE-RELATED PROTEIN 11; 1.
DR   Pfam; PF00194; Carb_anhydrase; 1.
DR   SMART; SM01057; Carb_anhydrase; 1.
DR   SUPFAM; SSF51069; Carbonic anhydrase; 1.
DR   PROSITE; PS51144; ALPHA_CA_2; 1.
DR   Genevisible; O75493; HS.
PE   1: Evidence at protein level;
KW   Glycoprotein; Reference proteome; Secreted; Signal.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000255"
FT   CHAIN           24..328
FT                   /note="Carbonic anhydrase-related protein 11"
FT                   /id="PRO_0000004245"
FT   DOMAIN          33..303
FT                   /note="Alpha-carbonic anhydrase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01134"
FT   REGION          299..328
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        118
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000269|PubMed:16335952"
FT   CARBOHYD        170
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        260
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CONFLICT        23..24
FT                   /note="AH -> GN (in Ref. 2; BAA36840)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        75
FT                   /note="L -> V (in Ref. 1; AAC99689)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        280
FT                   /note="I -> M (in Ref. 7; AAD08802)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   328 AA;  36238 MW;  A4FC408718B2E857 CRC64;
     MGAAARLSAP RALVLWAALG AAAHIGPAPD PEDWWSYKDN LQGNFVPGPP FWGLVNAAWS
     LCAVGKRQSP VDVELKRVLY DPFLPPLRLS TGGEKLRGTL YNTGRHVSFL PAPRPVVNVS
     GGPLLYSHRL SELRLLFGAR DGAGSEHQIN HQGFSAEVQL IHFNQELYGN FSAASRGPNG
     LAILSLFVNV ASTSNPFLSR LLNRDTITRI SYKNDAYFLQ DLSLELLFPE SFGFITYQGS
     LSTPPCSETV TWILIDRALN ITSLQMHSLR LLSQNPPSQI FQSLSGNSRP LQPLAHRALR
     GNRDPRHPER RCRGPNYRLH VDGVPHGR
//