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SPARC-related modular calcium-binding protein 2 (Secreted modular calcium-binding protein 2) (SMOC-2) (Smooth muscle-associated protein 2) (SMAP-2)

 SMOC2_HUMAN             Reviewed;         446 AA.
Q9H3U7; B3KPS7; Q4G169; Q5TAT7; Q5TAT8; Q86VV9; Q96SF3; Q9H1L3;
Q9H1L4; Q9H3U0; Q9H4F7; Q9HCV2;
31-OCT-2003, integrated into UniProtKB/Swiss-Prot.
31-OCT-2003, sequence version 2.
05-DEC-2018, entry version 157.
RecName: Full=SPARC-related modular calcium-binding protein 2;
AltName: Full=Secreted modular calcium-binding protein 2;
Short=SMOC-2;
AltName: Full=Smooth muscle-associated protein 2;
Short=SMAP-2;
Flags: Precursor;
Name=SMOC2; Synonyms=SMAP2; ORFNames=MSTP117;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), AND TISSUE SPECIFICITY.
TISSUE=Heart;
PubMed=12031507; DOI=10.1016/S0167-4781(02)00345-7;
Nishimoto S., Hamajima Y., Toda Y., Toyoda H., Kitamura K.,
Komurasaki T.;
"Identification of a novel smooth muscle associated protein, smap2,
upregulated during neointima formation in a rat carotid endarterectomy
model.";
Biochim. Biophys. Acta 1576:225-230(2002).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Placenta;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
TISSUE=Lymph node;
PubMed=17974005; DOI=10.1186/1471-2164-8-399;
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H.,
Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
Ottenwaelder B., Poustka A., Wiemann S., Schupp I.;
"The full-ORF clone resource of the German cDNA consortium.";
BMC Genomics 8:399-399(2007).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=14574404; DOI=10.1038/nature02055;
Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E.,
Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R.,
Almeida J.P., Ambrose K.D., Andrews T.D., Ashwell R.I.S.,
Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J.,
Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P.,
Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y.,
Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E.,
Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A.,
Frankland J., French L., Garner P., Garnett J., Ghori M.J.,
Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M.,
Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S.,
Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R.,
Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E.,
Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A.,
Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C.,
Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M.,
Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K.,
McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T.,
Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R.,
Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W.,
Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M.,
Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L.,
Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J.,
Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B.,
Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L.,
Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W.,
Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A.,
Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.;
"The DNA sequence and analysis of human chromosome 6.";
Nature 425:805-811(2003).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Testis;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 43-446 (ISOFORM 1).
TISSUE=Aorta;
Liu Y.Q., Liu B., Wang X.Y., Sheng H., Qin B.M., Zhang Q., Zheng W.Y.,
Hui R.T.;
Submitted (AUG-1999) to the EMBL/GenBank/DDBJ databases.
[8]
NUCLEOTIDE SEQUENCE [MRNA] OF 168-446.
TISSUE=Fetal brain;
PubMed=12741954; DOI=10.1042/BJ20030532;
Vannahme C., Goesling S., Paulsson M., Maurer P., Hartmann U.;
"Characterization of SMOC-2, a modular extracellular calcium-binding
protein.";
Biochem. J. 373:805-814(2003).
[9]
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=16774925; DOI=10.1074/jbc.M513463200;
Rocnik E.F., Liu P., Sato K., Walsh K., Vaziri C.;
"The novel SPARC family member SMOC-2 potentiates angiogenic growth
factor activity.";
J. Biol. Chem. 281:22855-22864(2006).
[10]
INVOLVEMENT IN DTDP1.
PubMed=22152679; DOI=10.1016/j.ajhg.2011.11.002;
Bloch-Zupan A., Jamet X., Etard C., Laugel V., Muller J., Geoffroy V.,
Strauss J.P., Pelletier V., Marion V., Poch O., Strahle U.,
Stoetzel C., Dollfus H.;
"Homozygosity mapping and candidate prioritization identify mutations,
missed by whole-exome sequencing, in SMOC2, causing major dental
developmental defects.";
Am. J. Hum. Genet. 89:773-781(2011).
-!- FUNCTION: Promotes matrix assembly and cell adhesiveness (By
similarity). Can stimulate endothelial cell proliferation,
migration, as well as angiogenesis. {ECO:0000250,
ECO:0000269|PubMed:16774925}.
-!- SUBUNIT: Binds various proteins from the extracellular matrix.
{ECO:0000250}.
-!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
matrix, basement membrane {ECO:0000250}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1; Synonyms=Smap2;
IsoId=Q9H3U7-1; Sequence=Displayed;
Name=2; Synonyms=Smap2b;
IsoId=Q9H3U7-2; Sequence=VSP_008722;
-!- DISEASE: Dentin dysplasia 1 (DTDP1) [MIM:125400]: A dental defect
in which both primary and secondary dentitions are affected. The
clinical crowns of both permanent and deciduous teeth are of
normal shape, form and color in most cases, although they may be
slightly opalescent and blue or brown. Teeth may be very mobile
and exfoliate spontaneously because of inadequate root formation.
On radiographs, the roots are short and may be more pointed than
normal. Pulp chambers are usually absent except for a chevron-
shaped remnant in the crown. Root canals are usually absent.
{ECO:0000269|PubMed:22152679}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- SEQUENCE CAUTION:
Sequence=AAQ13639.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
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EMBL; AB014730; BAB20267.1; -; mRNA.
EMBL; AB014737; BAB20274.1; -; mRNA.
EMBL; AK056700; BAG51789.1; -; mRNA.
EMBL; AL832303; CAI46175.1; -; mRNA.
EMBL; AL109940; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AL136099; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AL138918; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AL442124; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471051; EAW47462.1; -; Genomic_DNA.
EMBL; BC028420; AAH28420.1; -; mRNA.
EMBL; BC047583; AAH47583.1; -; mRNA.
EMBL; AF173892; AAQ13639.1; ALT_INIT; mRNA.
EMBL; AJ249902; CAC10353.1; -; mRNA.
CCDS; CCDS5307.1; -. [Q9H3U7-2]
CCDS; CCDS55076.1; -. [Q9H3U7-1]
RefSeq; NP_001159884.1; NM_001166412.1. [Q9H3U7-1]
RefSeq; NP_071421.1; NM_022138.2. [Q9H3U7-2]
UniGene; Hs.487200; -.
ProteinModelPortal; Q9H3U7; -.
SMR; Q9H3U7; -.
BioGrid; 122056; 3.
IntAct; Q9H3U7; 1.
STRING; 9606.ENSP00000346537; -.
iPTMnet; Q9H3U7; -.
PhosphoSitePlus; Q9H3U7; -.
BioMuta; SMOC2; -.
DMDM; 38258648; -.
EPD; Q9H3U7; -.
MaxQB; Q9H3U7; -.
PaxDb; Q9H3U7; -.
PeptideAtlas; Q9H3U7; -.
PRIDE; Q9H3U7; -.
ProteomicsDB; 80763; -.
ProteomicsDB; 80764; -. [Q9H3U7-2]
Ensembl; ENST00000354536; ENSP00000346537; ENSG00000112562. [Q9H3U7-2]
Ensembl; ENST00000356284; ENSP00000348630; ENSG00000112562. [Q9H3U7-1]
GeneID; 64094; -.
KEGG; hsa:64094; -.
UCSC; uc003qwr.2; human. [Q9H3U7-1]
CTD; 64094; -.
DisGeNET; 64094; -.
EuPathDB; HostDB:ENSG00000112562.18; -.
GeneCards; SMOC2; -.
HGNC; HGNC:20323; SMOC2.
HPA; CAB033979; -.
MalaCards; SMOC2; -.
MIM; 125400; phenotype.
MIM; 607223; gene.
neXtProt; NX_Q9H3U7; -.
OpenTargets; ENSG00000112562; -.
Orphanet; 314721; Atypical dentin dysplasia due to SMOC2 deficiency.
PharmGKB; PA134934590; -.
eggNOG; KOG4578; Eukaryota.
eggNOG; ENOG410YP7C; LUCA.
GeneTree; ENSGT00390000018436; -.
HOVERGEN; HBG058558; -.
InParanoid; Q9H3U7; -.
OMA; PRCPGSI; -.
OrthoDB; EOG091G083O; -.
PhylomeDB; Q9H3U7; -.
TreeFam; TF320666; -.
ChiTaRS; SMOC2; human.
GeneWiki; SMOC2; -.
GenomeRNAi; 64094; -.
PRO; PR:Q9H3U7; -.
Proteomes; UP000005640; Chromosome 6.
Bgee; ENSG00000112562; Expressed in 186 organ(s), highest expression level in descending thoracic aorta.
CleanEx; HS_SMAP2; -.
ExpressionAtlas; Q9H3U7; baseline and differential.
Genevisible; Q9H3U7; HS.
GO; GO:0005604; C:basement membrane; IEA:UniProtKB-SubCell.
GO; GO:0071944; C:cell periphery; IDA:UniProtKB.
GO; GO:0005615; C:extracellular space; IDA:UniProtKB.
GO; GO:0005614; C:interstitial matrix; IEA:Ensembl.
GO; GO:0005509; F:calcium ion binding; ISA:UniProtKB.
GO; GO:0008201; F:heparin binding; IEA:Ensembl.
GO; GO:0030198; P:extracellular matrix organization; IEA:Ensembl.
GO; GO:0045766; P:positive regulation of angiogenesis; IDA:UniProtKB.
GO; GO:0010811; P:positive regulation of cell-substrate adhesion; IEA:Ensembl.
GO; GO:2000573; P:positive regulation of DNA biosynthetic process; IDA:UniProtKB.
GO; GO:2001028; P:positive regulation of endothelial cell chemotaxis; IGI:UniProtKB.
GO; GO:0010595; P:positive regulation of endothelial cell migration; IDA:UniProtKB.
GO; GO:0045743; P:positive regulation of fibroblast growth factor receptor signaling pathway; IDA:UniProtKB.
GO; GO:0045931; P:positive regulation of mitotic cell cycle; IDA:UniProtKB.
GO; GO:1900748; P:positive regulation of vascular endothelial growth factor signaling pathway; IDA:UniProtKB.
GO; GO:0035470; P:positive regulation of vascular wound healing; IDA:UniProtKB.
CDD; cd16241; EFh_SPARC_SMOC2; 1.
CDD; cd00191; TY; 2.
Gene3D; 4.10.800.10; -; 2.
InterPro; IPR011992; EF-hand-dom_pair.
InterPro; IPR018247; EF_Hand_1_Ca_BS.
InterPro; IPR002048; EF_hand_dom.
InterPro; IPR002350; Kazal_dom.
InterPro; IPR036058; Kazal_dom_sf.
InterPro; IPR037640; SMOC2_EC.
InterPro; IPR019577; SPARC/Testican_Ca-bd-dom.
InterPro; IPR000716; Thyroglobulin_1.
InterPro; IPR036857; Thyroglobulin_1_sf.
Pfam; PF07648; Kazal_2; 1.
Pfam; PF10591; SPARC_Ca_bdg; 1.
Pfam; PF00086; Thyroglobulin_1; 2.
SMART; SM00280; KAZAL; 1.
SMART; SM00211; TY; 2.
SUPFAM; SSF100895; SSF100895; 1.
SUPFAM; SSF47473; SSF47473; 1.
SUPFAM; SSF57610; SSF57610; 2.
PROSITE; PS00018; EF_HAND_1; 2.
PROSITE; PS50222; EF_HAND_2; 2.
PROSITE; PS51465; KAZAL_2; 1.
PROSITE; PS00484; THYROGLOBULIN_1_1; 2.
PROSITE; PS51162; THYROGLOBULIN_1_2; 2.
2: Evidence at transcript level;
Alternative splicing; Basement membrane; Calcium; Complete proteome;
Disulfide bond; Extracellular matrix; Glycoprotein; Metal-binding;
Reference proteome; Repeat; Secreted; Signal.
SIGNAL 1 21 {ECO:0000255}.
CHAIN 22 446 SPARC-related modular calcium-binding
protein 2.
/FTId=PRO_0000020318.
DOMAIN 34 86 Kazal-like. {ECO:0000255|PROSITE-
ProRule:PRU00798}.
DOMAIN 87 153 Thyroglobulin type-1 1.
{ECO:0000255|PROSITE-ProRule:PRU00500}.
DOMAIN 213 281 Thyroglobulin type-1 2.
{ECO:0000255|PROSITE-ProRule:PRU00500}.
DOMAIN 347 382 EF-hand 1. {ECO:0000255|PROSITE-
ProRule:PRU00448}.
DOMAIN 384 419 EF-hand 2. {ECO:0000255|PROSITE-
ProRule:PRU00448}.
CA_BIND 360 371 1. {ECO:0000255|PROSITE-
ProRule:PRU00448}.
CA_BIND 397 408 2. {ECO:0000255|PROSITE-
ProRule:PRU00448}.
CARBOHYD 206 206 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 362 362 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 40 71 {ECO:0000255|PROSITE-ProRule:PRU00798}.
DISULFID 44 64 {ECO:0000255|PROSITE-ProRule:PRU00798}.
DISULFID 53 84 {ECO:0000255|PROSITE-ProRule:PRU00798}.
DISULFID 90 113 {ECO:0000250}.
DISULFID 124 131 {ECO:0000250}.
DISULFID 133 153 {ECO:0000250}.
DISULFID 216 240 {ECO:0000250}.
DISULFID 251 258 {ECO:0000250}.
DISULFID 260 281 {ECO:0000250}.
VAR_SEQ 170 170 T -> TVSLQIFSVLNS (in isoform 2).
{ECO:0000303|PubMed:12031507,
ECO:0000303|PubMed:17974005}.
/FTId=VSP_008722.
CONFLICT 169 170 KT -> TR (in Ref. 8; CAC10353).
{ECO:0000305}.
CONFLICT 212 212 S -> P (in Ref. 1; BAB20267).
{ECO:0000305}.
CONFLICT 434 434 A -> V (in Ref. 6; AAH47583).
{ECO:0000305}.
CONFLICT 439 439 N -> Y (in Ref. 8; CAC10353).
{ECO:0000305}.
SEQUENCE 446 AA; 49674 MW; CF0D92A71C9E1006 CRC64;
MLLPQLCWLP LLAGLLPPVP AQKFSALTFL RVDQDKDKDC SLDCAGSPQK PLCASDGRTF
LSRCEFQRAK CKDPQLEIAY RGNCKDVSRC VAERKYTQEQ ARKEFQQVFI PECNDDGTYS
QVQCHSYTGY CWCVTPNGRP ISGTAVAHKT PRCPGSVNEK LPQREGTGKT DDAAAPALET
QPQGDEEDIA SRYPTLWTEQ VKSRQNKTNK NSVSSCDQEH QSALEEAKQP KNDNVVIPEC
AHGGLYKPVQ CHPSTGYCWC VLVDTGRPIP GTSTRYEQPK CDNTARAHPA KARDLYKGRQ
LQGCPGAKKH EFLTSVLDAL STDMVHAASD PSSSSGRLSE PDPSHTLEER VVHWYFKLLD
KNSSGDIGKK EIKPFKRFLR KKSKPKKCVK KFVEYCDVNN DKSISVQELM GCLGVAKEDG
KADTKKRHTP RGHAESTSNR QPRKQG


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