CANT1_RAT
ID CANT1_RAT Reviewed; 403 AA.
AC Q8K4Y7; Q4V8N9;
DT 10-MAY-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 122.
DE RecName: Full=Soluble calcium-activated nucleotidase 1;
DE Short=SCAN-1;
DE EC=3.6.1.6 {ECO:0000269|PubMed:12167635};
DE AltName: Full=Apyrase homolog;
GN Name=Cant1; Synonyms=Srapy;
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 [MRNA], FUNCTION, CATALYTIC ACTIVITY, COFACTOR,
RP BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RC STRAIN=Sprague-Dawley; TISSUE=Brain;
RX PubMed=12167635; DOI=10.1074/jbc.m201656200;
RA Failer B.U., Braun N., Zimmermann H.;
RT "Cloning, expression, and functional characterization of a Ca2+-dependent
RT endoplasmic reticulum nucleoside diphosphatase.";
RL J. Biol. Chem. 277:36978-36986(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Placenta;
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).
CC -!- FUNCTION: Calcium-dependent nucleotidase with a preference for UDP. The
CC order of activity with different substrates is UDP > GDP > IDP >> UTP >
CC CDP = GTP = ITP. Has very low activity towards ADP and even lower
CC activity towards ATP. Does not hydrolyze AMP and GMP (PubMed:12167635).
CC Involved in proteoglycan synthesis (By similarity).
CC {ECO:0000250|UniProtKB:Q8WVQ1, ECO:0000269|PubMed:12167635}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a ribonucleoside 5'-diphosphate + H2O = a ribonucleoside 5'-
CC phosphate + H(+) + phosphate; Xref=Rhea:RHEA:36799,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:57930, ChEBI:CHEBI:58043; EC=3.6.1.6;
CC Evidence={ECO:0000269|PubMed:12167635};
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000269|PubMed:12167635};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=216 uM for UDP {ECO:0000269|PubMed:12167635};
CC -!- SUBUNIT: Monomer. Homodimer; dimerization is Ca(2+)-dependent.
CC {ECO:0000250|UniProtKB:Q8WVQ1}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:12167635}; Single-pass type II membrane protein
CC {ECO:0000269|PubMed:12167635}. Golgi apparatus, Golgi stack membrane
CC {ECO:0000269|PubMed:12167635}; Single-pass type II membrane protein
CC {ECO:0000269|PubMed:12167635}. Note=Processed form: Secreted.
CC -!- TISSUE SPECIFICITY: Detected in intestine, thymus, heart, lung, spleen,
CC kidney, liver, testis, skeletal muscle and brain.
CC {ECO:0000269|PubMed:12167635}.
CC -!- SIMILARITY: Belongs to the apyrase family. {ECO:0000305}.
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DR EMBL; AJ312207; CAC85467.1; -; mRNA.
DR EMBL; BC097279; AAH97279.1; -; mRNA.
DR RefSeq; NP_653355.1; NM_144754.2.
DR RefSeq; XP_006247851.1; XM_006247789.3.
DR RefSeq; XP_006247852.1; XM_006247790.1.
DR AlphaFoldDB; Q8K4Y7; -.
DR SMR; Q8K4Y7; -.
DR STRING; 10116.ENSRNOP00000059931; -.
DR GlyGen; Q8K4Y7; 1 site.
DR PhosphoSitePlus; Q8K4Y7; -.
DR PaxDb; Q8K4Y7; -.
DR Ensembl; ENSRNOT00000066303; ENSRNOP00000059931; ENSRNOG00000003239.
DR GeneID; 246272; -.
DR KEGG; rno:246272; -.
DR UCSC; RGD:628743; rat.
DR CTD; 124583; -.
DR RGD; 628743; Cant1.
DR eggNOG; KOG4494; Eukaryota.
DR GeneTree; ENSGT00390000012872; -.
DR HOGENOM; CLU_047493_0_0_1; -.
DR InParanoid; Q8K4Y7; -.
DR OMA; DEHMGCN; -.
DR OrthoDB; 1126948at2759; -.
DR BRENDA; 3.6.1.6; 5301.
DR Reactome; R-RNO-6798695; Neutrophil degranulation.
DR SABIO-RK; Q8K4Y7; -.
DR PRO; PR:Q8K4Y7; -.
DR Proteomes; UP000002494; Chromosome 10.
DR Bgee; ENSRNOG00000003239; Expressed in colon and 19 other tissues.
DR Genevisible; Q8K4Y7; RN.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IDA:RGD.
DR GO; GO:0032580; C:Golgi cisterna membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; ISO:RGD.
DR GO; GO:0043262; F:adenosine-diphosphatase activity; ISO:RGD.
DR GO; GO:0005509; F:calcium ion binding; ISO:RGD.
DR GO; GO:0004382; F:guanosine-diphosphatase activity; ISO:RGD.
DR GO; GO:0042803; F:protein homodimerization activity; ISO:RGD.
DR GO; GO:0045134; F:uridine-diphosphatase activity; IBA:GO_Central.
DR GO; GO:0030166; P:proteoglycan biosynthetic process; ISS:UniProtKB.
DR Gene3D; 2.120.10.100; -; 1.
DR InterPro; IPR009283; Apyrase.
DR InterPro; IPR036258; Apyrase_sf.
DR PANTHER; PTHR13023; PTHR13023; 1.
DR SUPFAM; SSF101887; SSF101887; 1.
PE 1: Evidence at protein level;
KW Calcium; Endoplasmic reticulum; Glycoprotein; Golgi apparatus; Hydrolase;
KW Membrane; Metal-binding; Reference proteome; Signal-anchor; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..403
FT /note="Soluble calcium-activated nucleotidase 1"
FT /id="PRO_0000209927"
FT TOPO_DOM 1..44
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 45..61
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 62..403
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT BINDING 170
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:Q8WVQ1"
FT BINDING 171
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:Q8WVQ1"
FT BINDING 217
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:Q8WVQ1"
FT BINDING 286
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:Q8WVQ1"
FT BINDING 347
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:Q8WVQ1"
FT BINDING 398
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:Q8WVQ1"
FT SITE 162
FT /note="Important for dimer formation"
FT /evidence="ECO:0000250|UniProtKB:Q8WVQ1"
FT SITE 202
FT /note="Important for dimer formation"
FT /evidence="ECO:0000250|UniProtKB:Q8WVQ1"
FT SITE 204
FT /note="Important for dimer formation"
FT /evidence="ECO:0000250|UniProtKB:Q8WVQ1"
FT SITE 258
FT /note="Important for dimer formation"
FT /evidence="ECO:0000250|UniProtKB:Q8WVQ1"
FT CARBOHYD 90
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 403 AA; 45659 MW; 34340AF7917334F1 CRC64;
MPIQPFDQRE WNEPMHSLRI SVGGLPVLAS MTKATDPRFR PRWRVILTSF VGAALLWLLY
SHHQTPVSGR PPIHNAHNWR LRQERISQYN DTYPLSPPQR TPGGIRYRIA VIADLDTGSK
AQEENTWFSY LKKGYLTLSD SGDRVSVEWD KDRGVLESHL AEKGRGMELS DLIVFNGKLY
SVDDRTGVIY QIEGTKAVPW VILSDGDGAV EKGFKAEWLA VKDEHLYVGG LGKEWTTTTG
EVVNENPEWV KVVGHRGSVE HENWVSSYNA LRAAAGIQPP GYLIHESACW SDTLQRWFFL
PRRASHERYS EREDERKGSN LLLSAAQDFR DISVRQVGAL VPTHGFSSFK FIPNTDDQII
VALKSEEDNG RIATYVMAFT LDGRFLLPET KIGSVKYEGI EFI
