CAH11_HUMAN
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 03-AUG-2022, entry version 171.
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}.
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; 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; 11.
DR IntAct; O75493; 4.
DR STRING; 9606.ENSP00000084798; -.
DR BindingDB; O75493; -.
DR ChEMBL; CHEMBL2420; -.
DR DrugBank; DB00909; Zonisamide.
DR GlyGen; O75493; 3 sites.
DR iPTMnet; O75493; -.
DR PhosphoSitePlus; O75493; -.
DR BioMuta; CA11; -.
DR MassIVE; O75493; -.
DR PaxDb; O75493; -.
DR PeptideAtlas; O75493; -.
DR PRIDE; O75493; -.
DR ProteomicsDB; 50047; -.
DR Antibodypedia; 31755; 116 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 CTD; 770; -.
DR DisGeNET; 770; -.
DR GeneCards; CA11; -.
DR HGNC; HGNC:1370; CA11.
DR HPA; ENSG00000063180; Group enriched (brain, choroid plexus).
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; FPMEIQL; -.
DR OrthoDB; 1377476at2759; -.
DR PhylomeDB; O75493; -.
DR TreeFam; TF352926; -.
DR PathwayCommons; O75493; -.
DR SignaLink; O75493; -.
DR BioGRID-ORCS; 770; 24 hits in 1081 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 174 other tissues.
DR ExpressionAtlas; O75493; baseline and differential.
DR Genevisible; O75493; HS.
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; -; 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; PTHR18952; 1.
DR Pfam; PF00194; Carb_anhydrase; 1.
DR SMART; SM01057; Carb_anhydrase; 1.
DR SUPFAM; SSF51069; SSF51069; 1.
DR PROSITE; PS51144; ALPHA_CA_2; 1.
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