SMOC2_MOUSE
ID SMOC2_MOUSE Reviewed; 447 AA.
AC Q8CD91; Q8VCM1; Q9D9K2; Q9ER95;
DT 31-OCT-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 159.
DE RecName: Full=SPARC-related modular calcium-binding protein 2;
DE AltName: Full=Secreted modular calcium-binding protein 2;
DE Short=SMOC-2;
DE Flags: Precursor;
GN Name=Smoc2;
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 [MRNA] (ISOFORM 1), GLYCOSYLATION, AND TISSUE
RP SPECIFICITY.
RC TISSUE=Brain;
RX PubMed=12741954; DOI=10.1042/bj20030532;
RA Vannahme C., Goesling S., Paulsson M., Maurer P., Hartmann U.;
RT "Characterization of SMOC-2, a modular extracellular calcium-binding
RT protein.";
RL Biochem. J. 373:805-814(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=C57BL/6J; TISSUE=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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Salivary gland;
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 [4]
RP FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, AND DEVELOPMENTAL STAGE.
RX PubMed=18757743; DOI=10.1073/pnas.0803640105;
RA Manabe R., Tsutsui K., Yamada T., Kimura M., Nakano I., Shimono C.,
RA Sanzen N., Furutani Y., Fukuda T., Oguri Y., Shimamoto K., Kiyozumi D.,
RA Sato Y., Sado Y., Senoo H., Yamashina S., Fukuda S., Kawai J., Sugiura N.,
RA Kimata K., Hayashizaki Y., Sekiguchi K.;
RT "Transcriptome-based systematic identification of extracellular matrix
RT proteins.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:12849-12854(2008).
CC -!- FUNCTION: Can stimulate endothelial cell proliferation, migration, as
CC well as angiogenesis (By similarity). Promotes matrix assembly and cell
CC adhesiveness. {ECO:0000250, ECO:0000269|PubMed:18757743}.
CC -!- SUBUNIT: Binds various proteins from the extracellular matrix.
CC {ECO:0000269|PubMed:18757743}.
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC matrix, basement membrane {ECO:0000269|PubMed:18757743}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8CD91-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8CD91-2; Sequence=VSP_008723;
CC -!- TISSUE SPECIFICITY: Strongly expressed in ovary, followed by heart,
CC muscle, spleen, brain, thymus, lung, liver, kidney, spleen, testis,
CC ovary and skeletal muscle. {ECO:0000269|PubMed:12741954}.
CC -!- DEVELOPMENTAL STAGE: At 16.5 dpc, present in rib cartilage, choroid
CC plexus epithelium and associated blood vessels, and developing oral and
CC tooth germ epithelia (at protein level). {ECO:0000269|PubMed:18757743}.
CC -!- PTM: N-glycosylated. {ECO:0000269|PubMed:12741954}.
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DR EMBL; AK030958; BAC27193.1; -; mRNA.
DR EMBL; AK006809; BAB24753.1; -; mRNA.
DR EMBL; AJ249901; CAC10355.1; -; mRNA.
DR EMBL; BC019527; AAH19527.1; -; mRNA.
DR CCDS; CCDS37442.1; -. [Q8CD91-1]
DR RefSeq; NP_071710.2; NM_022315.2. [Q8CD91-1]
DR AlphaFoldDB; Q8CD91; -.
DR BioGRID; 211022; 1.
DR STRING; 10090.ENSMUSP00000024660; -.
DR GlyGen; Q8CD91; 2 sites.
DR PhosphoSitePlus; Q8CD91; -.
DR MaxQB; Q8CD91; -.
DR PaxDb; Q8CD91; -.
DR PRIDE; Q8CD91; -.
DR ProteomicsDB; 261275; -. [Q8CD91-1]
DR ProteomicsDB; 261276; -. [Q8CD91-2]
DR Antibodypedia; 33562; 138 antibodies from 24 providers.
DR DNASU; 64074; -.
DR Ensembl; ENSMUST00000024660; ENSMUSP00000024660; ENSMUSG00000023886. [Q8CD91-1]
DR GeneID; 64074; -.
DR KEGG; mmu:64074; -.
DR UCSC; uc008amy.2; mouse. [Q8CD91-1]
DR UCSC; uc008ana.2; mouse. [Q8CD91-2]
DR CTD; 64094; -.
DR MGI; MGI:1929881; Smoc2.
DR VEuPathDB; HostDB:ENSMUSG00000023886; -.
DR eggNOG; KOG4578; Eukaryota.
DR GeneTree; ENSGT00390000018436; -.
DR HOGENOM; CLU_023483_0_0_1; -.
DR InParanoid; Q8CD91; -.
DR OrthoDB; 1057719at2759; -.
DR PhylomeDB; Q8CD91; -.
DR TreeFam; TF320666; -.
DR BioGRID-ORCS; 64074; 4 hits in 71 CRISPR screens.
DR ChiTaRS; Smoc2; mouse.
DR PRO; PR:Q8CD91; -.
DR Proteomes; UP000000589; Chromosome 17.
DR RNAct; Q8CD91; protein.
DR Bgee; ENSMUSG00000023886; Expressed in gastrula and 239 other tissues.
DR ExpressionAtlas; Q8CD91; baseline and differential.
DR Genevisible; Q8CD91; MM.
DR GO; GO:0005604; C:basement membrane; IDA:MGI.
DR GO; GO:0071944; C:cell periphery; ISO:MGI.
DR GO; GO:0031012; C:extracellular matrix; IDA:MGI.
DR GO; GO:0005615; C:extracellular space; ISO:MGI.
DR GO; GO:0005614; C:interstitial matrix; IDA:MGI.
DR GO; GO:0005509; F:calcium ion binding; IDA:UniProtKB.
DR GO; GO:0050840; F:extracellular matrix binding; IBA:GO_Central.
DR GO; GO:0005539; F:glycosaminoglycan binding; IDA:MGI.
DR GO; GO:0008201; F:heparin binding; IDA:MGI.
DR GO; GO:0030198; P:extracellular matrix organization; IDA:MGI.
DR GO; GO:0045766; P:positive regulation of angiogenesis; ISO:MGI.
DR GO; GO:0010811; P:positive regulation of cell-substrate adhesion; IDA:MGI.
DR GO; GO:2000573; P:positive regulation of DNA biosynthetic process; ISO:MGI.
DR GO; GO:2001028; P:positive regulation of endothelial cell chemotaxis; ISO:MGI.
DR GO; GO:0010595; P:positive regulation of endothelial cell migration; ISO:MGI.
DR GO; GO:0045743; P:positive regulation of fibroblast growth factor receptor signaling pathway; ISO:MGI.
DR GO; GO:0045931; P:positive regulation of mitotic cell cycle; ISO:MGI.
DR GO; GO:1900748; P:positive regulation of vascular endothelial growth factor signaling pathway; ISO:MGI.
DR GO; GO:0035470; P:positive regulation of vascular wound healing; ISO:MGI.
DR CDD; cd16241; EFh_SPARC_SMOC2; 1.
DR CDD; cd00191; TY; 2.
DR Gene3D; 4.10.800.10; -; 2.
DR InterPro; IPR011992; EF-hand-dom_pair.
DR InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR InterPro; IPR002048; EF_hand_dom.
DR InterPro; IPR002350; Kazal_dom.
DR InterPro; IPR037640; SMOC2_EC.
DR InterPro; IPR019577; SPARC/Testican_Ca-bd-dom.
DR InterPro; IPR000716; Thyroglobulin_1.
DR InterPro; IPR036857; Thyroglobulin_1_sf.
DR Pfam; PF07648; Kazal_2; 1.
DR Pfam; PF10591; SPARC_Ca_bdg; 1.
DR Pfam; PF00086; Thyroglobulin_1; 2.
DR SMART; SM00280; KAZAL; 1.
DR SMART; SM00211; TY; 2.
DR SUPFAM; SSF47473; SSF47473; 1.
DR SUPFAM; SSF57610; SSF57610; 2.
DR PROSITE; PS00018; EF_HAND_1; 2.
DR PROSITE; PS50222; EF_HAND_2; 2.
DR PROSITE; PS51465; KAZAL_2; 1.
DR PROSITE; PS00484; THYROGLOBULIN_1_1; 2.
DR PROSITE; PS51162; THYROGLOBULIN_1_2; 2.
PE 1: Evidence at protein level;
KW Alternative splicing; Basement membrane; Calcium; Disulfide bond;
KW Extracellular matrix; Glycoprotein; Metal-binding; Reference proteome;
KW Repeat; Secreted; Signal.
FT SIGNAL 1..21
FT /evidence="ECO:0000255"
FT CHAIN 22..447
FT /note="SPARC-related modular calcium-binding protein 2"
FT /id="PRO_0000020319"
FT DOMAIN 34..86
FT /note="Kazal-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT DOMAIN 87..153
FT /note="Thyroglobulin type-1 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00500"
FT DOMAIN 213..281
FT /note="Thyroglobulin type-1 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00500"
FT DOMAIN 347..382
FT /note="EF-hand 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 384..419
FT /note="EF-hand 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT REGION 147..230
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 416..447
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 196..220
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 433..447
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 360
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 362
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 364
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 366
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 371
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 397
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 399
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 401
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 403
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 408
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT CARBOHYD 206
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 362
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 40..71
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT DISULFID 44..64
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT DISULFID 53..84
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT DISULFID 90..113
FT /evidence="ECO:0000250"
FT DISULFID 124..131
FT /evidence="ECO:0000250"
FT DISULFID 133..153
FT /evidence="ECO:0000250"
FT DISULFID 216..240
FT /evidence="ECO:0000250"
FT DISULFID 251..258
FT /evidence="ECO:0000250"
FT DISULFID 260..281
FT /evidence="ECO:0000250"
FT VAR_SEQ 1..336
FT /note="MLPPQLCWLPLLAALLPPVPAQKFSALTFLRVDQDKDRDCSLDCPSSPQKPL
FT CASDGRTFLSRCEFQRAKCKDPQLEIAHRGNCKDVSRCVAERKYTQEQARKEFQQVFIP
FT ECNDDGTYSQVQCHSYTGYCWCVTPNGRPISGTAVAHKTPRCPGSINEKVPQREGAGKA
FT DDAAAPALETQPQGDEEDIASRYPTLWTEQVKSRQNKTNKNSASSCDQEHQSALEEAKQ
FT PKNDNVVIPECAHGGLYKPVQCHPSTGYCWCVLVDTGRPIPGTSTRYEQPKCDNTARAH
FT PAKARDLYKNRPLQGCPGAKKHEFLTSVLDALSTDMVHAVSDPSSSSG -> MLLFLDL
FT SPGL (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_008723"
FT CONFLICT 351
FT /note="V -> D (in Ref. 2; BAB24753)"
FT /evidence="ECO:0000305"
FT CONFLICT 437..438
FT /note="SS -> T (in Ref. 1)"
FT /evidence="ECO:0000305"
FT CONFLICT 439
FT /note="S -> F (in Ref. 2; BAB24753)"
FT /evidence="ECO:0000305"
FT CONFLICT 440
FT /note="N -> Y (in Ref. 3; AAH19527)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 447 AA; 49891 MW; 26AB802F9D13A00C CRC64;
MLPPQLCWLP LLAALLPPVP AQKFSALTFL RVDQDKDRDC SLDCPSSPQK PLCASDGRTF
LSRCEFQRAK CKDPQLEIAH RGNCKDVSRC VAERKYTQEQ ARKEFQQVFI PECNDDGTYS
QVQCHSYTGY CWCVTPNGRP ISGTAVAHKT PRCPGSINEK VPQREGAGKA DDAAAPALET
QPQGDEEDIA SRYPTLWTEQ VKSRQNKTNK NSASSCDQEH QSALEEAKQP KNDNVVIPEC
AHGGLYKPVQ CHPSTGYCWC VLVDTGRPIP GTSTRYEQPK CDNTARAHPA KARDLYKNRP
LQGCPGAKKH EFLTSVLDAL STDMVHAVSD PSSSSGRLSE PDPSHTLEER VVHWYFKLLD
KNSSGDIGKK EIKPFKRFLR KKSKPKKCVK KFVEYCDMNN DKSITVQELM GCLGVTREEG
KANTRKRHTP RGNAESSSSN RQPRKQG
