CANT1_MOUSE
ID CANT1_MOUSE Reviewed; 403 AA.
AC Q8VCF1; B1AQJ8; Q8C3R8; Q8C4T6; Q9D3F2; Q9D9R1;
DT 10-MAY-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 142.
DE RecName: Full=Soluble calcium-activated nucleotidase 1;
DE Short=SCAN-1;
DE EC=3.6.1.6 {ECO:0000250|UniProtKB:Q8WVQ1};
DE AltName: Full=Apyrase homolog;
GN Name=Cant1;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 3).
RC STRAIN=C57BL/6J; TISSUE=Cerebellum, Hippocampus, Lung, Testis, and Thymus;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=FVB/N; TISSUE=Colon;
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. Involved in
CC proteoglycan synthesis. {ECO:0000250|UniProtKB:Q8WVQ1}.
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:0000250|UniProtKB:Q8WVQ1};
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000250|UniProtKB:Q8WVQ1};
CC -!- SUBUNIT: Monomer. Homodimer; dimerization is Ca(2+)-dependent.
CC {ECO:0000250|UniProtKB:Q8WVQ1}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:Q8K4Y7}; Single-pass type II membrane protein
CC {ECO:0000250|UniProtKB:Q8K4Y7}. Golgi apparatus, Golgi stack membrane
CC {ECO:0000250|UniProtKB:Q8K4Y7}; Single-pass type II membrane protein
CC {ECO:0000250|UniProtKB:Q8K4Y7}. Note=Processed form: Secreted.
CC {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q8VCF1-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8VCF1-2; Sequence=VSP_013763, VSP_013764;
CC Name=3;
CC IsoId=Q8VCF1-3; Sequence=VSP_013762;
CC -!- SIMILARITY: Belongs to the apyrase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB31014.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=BAC39351.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AK006565; BAB24655.1; -; mRNA.
DR EMBL; AK017942; BAB31014.1; ALT_FRAME; mRNA.
DR EMBL; AK049879; BAC33968.1; -; mRNA.
DR EMBL; AK081118; BAC38139.1; -; mRNA.
DR EMBL; AK085059; BAC39351.1; ALT_FRAME; mRNA.
DR EMBL; AL591404; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC020003; AAH20003.1; -; mRNA.
DR CCDS; CCDS25702.1; -. [Q8VCF1-1]
DR CCDS; CCDS59572.1; -. [Q8VCF1-3]
DR RefSeq; NP_001020788.1; NM_001025617.2. [Q8VCF1-1]
DR RefSeq; NP_001020789.1; NM_001025618.2. [Q8VCF1-1]
DR RefSeq; NP_001254520.1; NM_001267591.1. [Q8VCF1-1]
DR RefSeq; NP_001254521.1; NM_001267592.1. [Q8VCF1-3]
DR RefSeq; NP_083778.2; NM_029502.3. [Q8VCF1-1]
DR RefSeq; XP_006534467.1; XM_006534404.2. [Q8VCF1-3]
DR RefSeq; XP_006534468.1; XM_006534405.2. [Q8VCF1-3]
DR RefSeq; XP_006534469.1; XM_006534406.2. [Q8VCF1-3]
DR RefSeq; XP_006534470.1; XM_006534407.2. [Q8VCF1-3]
DR RefSeq; XP_006534471.1; XM_006534408.3. [Q8VCF1-3]
DR RefSeq; XP_006534472.1; XM_006534409.1. [Q8VCF1-3]
DR RefSeq; XP_006534473.1; XM_006534410.3. [Q8VCF1-3]
DR AlphaFoldDB; Q8VCF1; -.
DR SMR; Q8VCF1; -.
DR STRING; 10090.ENSMUSP00000090032; -.
DR GlyGen; Q8VCF1; 1 site.
DR iPTMnet; Q8VCF1; -.
DR PhosphoSitePlus; Q8VCF1; -.
DR EPD; Q8VCF1; -.
DR MaxQB; Q8VCF1; -.
DR PaxDb; Q8VCF1; -.
DR PeptideAtlas; Q8VCF1; -.
DR PRIDE; Q8VCF1; -.
DR ProteomicsDB; 265655; -. [Q8VCF1-1]
DR ProteomicsDB; 265656; -. [Q8VCF1-2]
DR ProteomicsDB; 265657; -. [Q8VCF1-3]
DR Antibodypedia; 19748; 334 antibodies from 31 providers.
DR DNASU; 76025; -.
DR Ensembl; ENSMUST00000017620; ENSMUSP00000017620; ENSMUSG00000025575. [Q8VCF1-1]
DR Ensembl; ENSMUST00000092378; ENSMUSP00000090032; ENSMUSG00000025575. [Q8VCF1-1]
DR Ensembl; ENSMUST00000106287; ENSMUSP00000101894; ENSMUSG00000025575. [Q8VCF1-1]
DR Ensembl; ENSMUST00000106288; ENSMUSP00000101895; ENSMUSG00000025575. [Q8VCF1-1]
DR Ensembl; ENSMUST00000106289; ENSMUSP00000101896; ENSMUSG00000025575. [Q8VCF1-3]
DR Ensembl; ENSMUST00000164927; ENSMUSP00000126919; ENSMUSG00000025575. [Q8VCF1-1]
DR GeneID; 76025; -.
DR KEGG; mmu:76025; -.
DR UCSC; uc007mpa.2; mouse. [Q8VCF1-1]
DR UCSC; uc007mpf.2; mouse. [Q8VCF1-2]
DR UCSC; uc011yin.2; mouse. [Q8VCF1-3]
DR CTD; 124583; -.
DR MGI; MGI:1923275; Cant1.
DR VEuPathDB; HostDB:ENSMUSG00000025575; -.
DR eggNOG; KOG4494; Eukaryota.
DR GeneTree; ENSGT00390000012872; -.
DR HOGENOM; CLU_047493_0_0_1; -.
DR InParanoid; Q8VCF1; -.
DR OMA; MGMISTT; -.
DR OrthoDB; 1126948at2759; -.
DR TreeFam; TF315248; -.
DR BRENDA; 3.1.3.5; 3474.
DR BRENDA; 3.6.1.6; 3474.
DR Reactome; R-MMU-6798695; Neutrophil degranulation.
DR BioGRID-ORCS; 76025; 3 hits in 74 CRISPR screens.
DR ChiTaRS; Cant1; mouse.
DR PRO; PR:Q8VCF1; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; Q8VCF1; protein.
DR Bgee; ENSMUSG00000025575; Expressed in pyloric antrum and 260 other tissues.
DR Genevisible; Q8VCF1; MM.
DR GO; GO:0005783; C:endoplasmic reticulum; ISO:MGI.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; ISO:MGI.
DR GO; GO:0005794; C:Golgi apparatus; ISO:MGI.
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:MGI.
DR GO; GO:0043262; F:adenosine-diphosphatase activity; ISO:MGI.
DR GO; GO:0005509; F:calcium ion binding; ISO:MGI.
DR GO; GO:0004382; F:guanosine-diphosphatase activity; ISO:MGI.
DR GO; GO:0042803; F:protein homodimerization activity; ISO:MGI.
DR GO; GO:0045134; F:uridine-diphosphatase activity; ISO:MGI.
DR GO; GO:0030166; P:proteoglycan biosynthetic process; ISS:UniProtKB.
DR GO; GO:0009191; P:ribonucleoside diphosphate catabolic process; IC:MGI.
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 2: Evidence at transcript level;
KW Alternative splicing; Calcium; Endoplasmic reticulum; Glycoprotein;
KW Golgi apparatus; Hydrolase; Membrane; Metal-binding; Reference proteome;
KW Signal-anchor; Transmembrane; Transmembrane helix.
FT CHAIN 1..403
FT /note="Soluble calcium-activated nucleotidase 1"
FT /id="PRO_0000209926"
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"
FT VAR_SEQ 213
FT /note="G -> GQLLLLSLALSPPSTRVCMLSSNDSWEQNLILASCVAG (in
FT isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_013762"
FT VAR_SEQ 214
FT /note="F -> K (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_013763"
FT VAR_SEQ 215..403
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_013764"
FT CONFLICT 8
FT /note="Q -> E (in Ref. 1; BAC38139)"
FT /evidence="ECO:0000305"
FT CONFLICT 113
FT /note="A -> G (in Ref. 1; BAC38139)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 403 AA; 45653 MW; 0CB2BC618CD4714E CRC64;
MPIQPFDQRE WNEPMHSLRI SVGGLPVLAS MTKATDPRFR PRWRVILTSF VGAALLWLLY
SHHQGPVPGR PPTHNAHNWR LSQQRISHYN DTYPLSPPQR TPGGIRYRIA VIADLDTGSR
AQEENTWFSY LKKGYLTLSD SGDRVSVEWD KDHGVLESHL AEKGRGMELS DLIVFNGKLY
SVDDRTGVIY QIEGTKAVPW VILSDGDGTV EKGFKAEWLA VKDEHLYVGG LGKEWTTTTG
EVMNENPEWV KVVGHRGSVD HENWVSSYNA LRAAAGIRPP GYLIHESACW SDTLQRWFFL
PRRASHERYS EKDDERKGSN LLLSAAQDFR DISVRQVGTL IPTHGFSSFK FIPNTDDQII
VALKSEEDNG RIATYVMAFT LDGRFLLPET KIGTVKYEGI EFI
