CD38_RABIT
ID CD38_RABIT Reviewed; 298 AA.
AC Q9MZ03;
DT 27-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 25-MAY-2022, entry version 109.
DE RecName: Full=ADP-ribosyl cyclase/cyclic ADP-ribose hydrolase 1;
DE EC=3.2.2.6 {ECO:0000305|PubMed:10477767, ECO:0000305|PubMed:10891341};
DE AltName: Full=2'-phospho-ADP-ribosyl cyclase;
DE AltName: Full=2'-phospho-ADP-ribosyl cyclase/2'-phospho-cyclic-ADP-ribose transferase;
DE EC=2.4.99.20;
DE AltName: Full=2'-phospho-cyclic-ADP-ribose transferase;
DE AltName: Full=ADP-ribosyl cyclase 1;
DE Short=ADPRC 1;
DE AltName: Full=Cyclic ADP-ribose hydrolase 1;
DE Short=cADPr hydrolase 1;
DE AltName: CD_antigen=CD38;
GN Name=CD38;
OS Oryctolagus cuniculus (Rabbit).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX NCBI_TaxID=9986;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, TISSUE SPECIFICITY,
RP FUNCTION, AND CATALYTIC ACTIVITY.
RC TISSUE=Osteoclast;
RX PubMed=10477767; DOI=10.1083/jcb.146.5.1161;
RA Sun L., Adebanjo O.A., Moonga B.S., Corisdeo S., Anandatheerthavarada H.K.,
RA Biswas G., Arakawa T., Hakeda Y., Koval A., Sodam B., Bevis P.J.R.,
RA Moser A.J., Lai F.A., Epstein S., Troen B.R., Kumegawa M., Zaidi M.;
RT "CD38/ADP-ribosyl cyclase: a new role in the regulation of osteoclastic
RT bone resorption.";
RL J. Cell Biol. 146:1161-1172(1999).
RN [2]
RP ERRATUM OF PUBMED:10477767.
RA Sun L., Adebanjo O.A., Moonga B.S., Corisdeo S., Anandatheerthavarada H.K.,
RA Biswas G., Arakawa T., Hakeda Y., Koval A., Sodam B., Bevis P.J.R.,
RA Moser A.J., Lai F.A., Epstein S., Troen B.R., Kumegawa M., Zaidi M.;
RL J. Cell Biol. 146:1391-1392(1999).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, AND CATALYTIC
RP ACTIVITY.
RC TISSUE=Osteoclast;
RX PubMed=10891341; DOI=10.1006/bbrc.2000.3041;
RA Adebanjo O.A., Koval A., Moonga B.S., Wu X.B., Yao S., Bevis P.J.R.,
RA Kumegawa M., Zaidi M., Sun L.;
RT "Molecular cloning, expression, and functional characterization of a novel
RT member of the CD38 family of ADP-ribosyl cyclases.";
RL Biochem. Biophys. Res. Commun. 273:884-889(2000).
CC -!- FUNCTION: Synthesizes the second messengers cyclic ADP-ribose and
CC nicotinate-adenine dinucleotide phosphate, the former a second
CC messenger for glucose-induced insulin secretion. Also has cADPr
CC hydrolase activity. {ECO:0000269|PubMed:10477767,
CC ECO:0000269|PubMed:10891341}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + NAD(+) = ADP-D-ribose + H(+) + nicotinamide;
CC Xref=Rhea:RHEA:16301, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:17154, ChEBI:CHEBI:57540, ChEBI:CHEBI:57967; EC=3.2.2.6;
CC Evidence={ECO:0000305|PubMed:10477767, ECO:0000305|PubMed:10891341};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=NADP(+) + nicotinate = nicotinamide + nicotinate-adenine
CC dinucleotide phosphate; Xref=Rhea:RHEA:38599, ChEBI:CHEBI:17154,
CC ChEBI:CHEBI:32544, ChEBI:CHEBI:58349, ChEBI:CHEBI:75967;
CC EC=2.4.99.20;
CC -!- SUBCELLULAR LOCATION: Cell membrane; Single-pass type II membrane
CC protein. Microsome membrane; Single-pass type II membrane protein.
CC Endoplasmic reticulum membrane; Single-pass type II membrane protein.
CC -!- TISSUE SPECIFICITY: Osteoclasts. {ECO:0000269|PubMed:10477767}.
CC -!- SIMILARITY: Belongs to the ADP-ribosyl cyclase family. {ECO:0000305}.
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DR EMBL; AF272974; AAF87715.1; -; mRNA.
DR PIR; JC7323; JC7323.
DR RefSeq; NP_001076152.1; NM_001082683.1.
DR AlphaFoldDB; Q9MZ03; -.
DR SMR; Q9MZ03; -.
DR STRING; 9986.ENSOCUP00000015283; -.
DR GeneID; 100009409; -.
DR KEGG; ocu:100009409; -.
DR CTD; 952; -.
DR eggNOG; ENOG502S1HV; Eukaryota.
DR InParanoid; Q9MZ03; -.
DR Proteomes; UP000001811; Unplaced.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0050135; F:NAD(P)+ nucleosidase activity; IEA:UniProtKB-EC.
DR GO; GO:0003953; F:NAD+ nucleosidase activity; IDA:UniProtKB.
DR GO; GO:0061809; F:NAD+ nucleotidase, cyclic ADP-ribose generating; IEA:UniProtKB-EC.
DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR GO; GO:0035556; P:intracellular signal transduction; IDA:UniProtKB.
DR CDD; cd04759; Rib_hydrolase; 1.
DR InterPro; IPR003193; ADP-ribosyl_cyclase.
DR InterPro; IPR033567; CD38.
DR PANTHER; PTHR10912; PTHR10912; 1.
DR PANTHER; PTHR10912:SF5; PTHR10912:SF5; 1.
DR Pfam; PF02267; Rib_hydrolayse; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Disulfide bond; Endoplasmic reticulum; Glycoprotein;
KW Hydrolase; Membrane; Microsome; NAD; NADP; Reference proteome;
KW Signal-anchor; Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..298
FT /note="ADP-ribosyl cyclase/cyclic ADP-ribose hydrolase 1"
FT /id="PRO_0000144069"
FT TOPO_DOM 1..21
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 22..42
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 43..298
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT ACT_SITE 117
FT /evidence="ECO:0000250"
FT ACT_SITE 199
FT /evidence="ECO:0000250"
FT CARBOHYD 98
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 118
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 177
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 207
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 268
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 64..80
FT /evidence="ECO:0000250"
FT DISULFID 97..178
FT /evidence="ECO:0000250"
FT DISULFID 158..171
FT /evidence="ECO:0000250"
FT DISULFID 252..273
FT /evidence="ECO:0000250"
FT DISULFID 285..294
FT /evidence="ECO:0000250"
SQ SEQUENCE 298 AA; 33637 MW; 7A4942F5A4625B60 CRC64;
MPDYEFSPAS GDRPRSWISK QVLIVLGVCL PVILALAIWV GVLTWRQSSM GATDHVSAIV
LGRCLTYTRN MHPELRNQDC KKILNTFTSA FVSKDPCNIT KEDYQPLIDL VTQTVPCNKT
LFWSRSKELA HQYSGIQKEM FTLEDTLLGY IADNLVWCGD PRTSEVKEEF CPYRNENCSS
TATSVFWTVV SQKFAESACG TVYVMLNGSR TTAFSKASTF GSVEVFNLHP DRVHTLHAWV
MHDIGGVERD SCLGSSIKEL KSIVNQRNIS FFCQDDYRPA RFVQCVRHPE HPSCSVLM
