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SPARC-related modular calcium-binding protein 1 (Secreted modular calcium-binding protein 1) (SMOC-1)

 SMOC1_HUMAN             Reviewed;         434 AA.
Q9H4F8; A8K1S3; B2R7P5; Q96F78;
31-OCT-2003, integrated into UniProtKB/Swiss-Prot.
01-MAR-2001, sequence version 1.
12-SEP-2018, entry version 158.
RecName: Full=SPARC-related modular calcium-binding protein 1;
AltName: Full=Secreted modular calcium-binding protein 1;
Short=SMOC-1;
Flags: Precursor;
Name=SMOC1;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY,
SUBCELLULAR LOCATION, AND GLYCOSYLATION.
TISSUE=Fetal brain;
PubMed=12130637; DOI=10.1074/jbc.M203830200;
Vannahme C., Smyth N., Miosge N., Goesling S., Frie C., Paulsson M.,
Maurer P., Hartmann U.;
"Characterization of SMOC-1, a novel modular calcium-binding protein
in basement membranes.";
J. Biol. Chem. 277:37977-37986(2002).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
TISSUE=Caudate nucleus;
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 GENOMIC DNA].
PubMed=12508121; DOI=10.1038/nature01348;
Heilig R., Eckenberg R., Petit J.-L., Fonknechten N., Da Silva C.,
Cattolico L., Levy M., Barbe V., De Berardinis V., Ureta-Vidal A.,
Pelletier E., Vico V., Anthouard V., Rowen L., Madan A., Qin S.,
Sun H., Du H., Pepin K., Artiguenave F., Robert C., Cruaud C.,
Bruels T., Jaillon O., Friedlander L., Samson G., Brottier P.,
Cure S., Segurens B., Aniere F., Samain S., Crespeau H., Abbasi N.,
Aiach N., Boscus D., Dickhoff R., Dors M., Dubois I., Friedman C.,
Gouyvenoux M., James R., Madan A., Mairey-Estrada B., Mangenot S.,
Martins N., Menard M., Oztas S., Ratcliffe A., Shaffer T., Trask B.,
Vacherie B., Bellemere C., Belser C., Besnard-Gonnet M.,
Bartol-Mavel D., Boutard M., Briez-Silla S., Combette S.,
Dufosse-Laurent V., Ferron C., Lechaplais C., Louesse C., Muselet D.,
Magdelenat G., Pateau E., Petit E., Sirvain-Trukniewicz P., Trybou A.,
Vega-Czarny N., Bataille E., Bluet E., Bordelais I., Dubois M.,
Dumont C., Guerin T., Haffray S., Hammadi R., Muanga J., Pellouin V.,
Robert D., Wunderle E., Gauguet G., Roy A., Sainte-Marthe L.,
Verdier J., Verdier-Discala C., Hillier L.W., Fulton L., McPherson J.,
Matsuda F., Wilson R., Scarpelli C., Gyapay G., Wincker P., Saurin W.,
Quetier F., Waterston R., Hood L., Weissenbach J.;
"The DNA sequence and analysis of human chromosome 14.";
Nature 421:601-607(2003).
[4]
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 (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
TISSUE=Brain, and Lung;
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).
[6]
FUNCTION AS REGULATOR OF OSTEOBLAST DIFFERENTIATION, SUBCELLULAR
LOCATION, AND IDENTIFICATION BY MASS SPECTROMETRY.
PubMed=20359165; DOI=10.1021/pr901110q;
Choi Y.A., Lim J., Kim K.M., Acharya B., Cho J.Y., Bae Y.C.,
Shin H.I., Kim S.Y., Park E.K.;
"Secretome analysis of human BMSCs and identification of SMOC1 as an
important ECM protein in osteoblast differentiation.";
J. Proteome Res. 9:2946-2956(2010).
[7]
FUNCTION, AND INVOLVEMENT IN OAS.
PubMed=21194678; DOI=10.1016/j.ajhg.2010.11.012;
Okada I., Hamanoue H., Terada K., Tohma T., Megarbane A., Chouery E.,
Abou-Ghoch J., Jalkh N., Cogulu O., Ozkinay F., Horie K., Takeda J.,
Furuichi T., Ikegawa S., Nishiyama K., Miyatake S., Nishimura A.,
Mizuguchi T., Niikawa N., Hirahara F., Kaname T., Yoshiura K.,
Tsurusaki Y., Doi H., Miyake N., Furukawa T., Matsumoto N., Saitsu H.;
"SMOC1 is essential for ocular and limb development in humans and
mice.";
Am. J. Hum. Genet. 88:30-41(2011).
[8]
FUNCTION, AND INVOLVEMENT IN OAS.
PubMed=21194680; DOI=10.1016/j.ajhg.2010.12.002;
Abouzeid H., Boisset G., Favez T., Youssef M., Marzouk I.,
Shakankiry N., Bayoumi N., Descombes P., Agosti C., Munier F.L.,
Schorderet D.F.;
"Mutations in the SPARC-related modular calcium-binding protein 1
gene, SMOC1, cause waardenburg anophthalmia syndrome.";
Am. J. Hum. Genet. 88:92-98(2011).
[9]
VARIANTS OAS CYS-278 AND ASN-283.
PubMed=21750680; DOI=10.1371/journal.pgen.1002114;
Rainger J., van Beusekom E., Ramsay J.K., McKie L., Al-Gazali L.,
Pallotta R., Saponari A., Branney P., Fisher M., Morrison H.,
Bicknell L., Gautier P., Perry P., Sokhi K., Sexton D.,
Bardakjian T.M., Schneider A.S., Elcioglu N., Ozkinay F., Koenig R.,
Megarbane A., Semerci C.N., Khan A., Zafar S., Hennekam R.,
Sousa S.B., Ramos L., Garavelli L., Furga A.S., Wischmeijer A.,
Jackson I.J., Gillessen-Kaesbach G., Brunner H.G., Wieczorek D.,
van Bokhoven H., Fitzpatrick D.R.;
"Loss of the BMP antagonist, SMOC-1, causes Ophthalmo-acromelic
(Waardenburg Anophthalmia) syndrome in humans and mice.";
PLoS Genet. 7:E1002114-E1002114(2011).
[10]
VARIANT OAS HIS-286.
PubMed=23646827; DOI=10.1111/cge.12184;
Aldahmesh M.A., Khan A.O., Hijazi H., Alkuraya F.S.;
"Mutations in ALDH1A3 cause Microphthalmia.";
Clin. Genet. 84:128-131(2013).
-!- FUNCTION: Plays essential roles in both eye and limb development.
Probable regulator of osteoblast differentiation.
{ECO:0000269|PubMed:20359165, ECO:0000269|PubMed:21194678,
ECO:0000269|PubMed:21194680}.
-!- INTERACTION:
P09022:Hoxa1 (xeno); NbExp=2; IntAct=EBI-2801103, EBI-3957603;
P60410:KRTAP10-8; NbExp=3; IntAct=EBI-2801103, EBI-10171774;
Q7Z3S9:NOTCH2NL; NbExp=3; IntAct=EBI-2801103, EBI-945833;
P15884:TCF4; NbExp=3; IntAct=EBI-2801103, EBI-533224;
-!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
matrix, basement membrane {ECO:0000269|PubMed:12130637,
ECO:0000269|PubMed:20359165}. Note=In or around the basement
membrane.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q9H4F8-1; Sequence=Displayed;
Name=2;
IsoId=Q9H4F8-2; Sequence=VSP_008720;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Widely expressed in many tissues with a
strongest signal in ovary. No expression in spleen.
{ECO:0000269|PubMed:12130637}.
-!- PTM: Glycosylated. {ECO:0000269|PubMed:12130637}.
-!- DISEASE: Ophthalmoacromelic syndrome (OAS) [MIM:206920]: A rare
disorder presenting with ocular anomalies, ranging from mild
microphthalmia to true anophthalmia, and limb anomalies. Limb
malformations include fused 4th and 5th metacarpals and short 5th
finger in hands, and oligodactyly in foot (four toes). Most
patients have bilateral anophthalmia/ microphthalmia, but
unilateral abnormality is also noted. Other malformations are
rare, but venous or vertebral anomaly was recognized each in
single cases. {ECO:0000269|PubMed:21194678,
ECO:0000269|PubMed:21194680, ECO:0000269|PubMed:21750680,
ECO:0000269|PubMed:23646827}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
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EMBL; AJ249900; CAC10352.1; -; mRNA.
EMBL; AK289988; BAF82677.1; -; mRNA.
EMBL; AK313063; BAG35892.1; -; mRNA.
EMBL; AL135747; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AL157789; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471061; EAW81013.1; -; Genomic_DNA.
EMBL; CH471061; EAW81014.1; -; Genomic_DNA.
EMBL; BC008608; AAH08608.1; -; mRNA.
EMBL; BC011548; AAH11548.1; -; mRNA.
CCDS; CCDS32110.1; -. [Q9H4F8-2]
CCDS; CCDS9798.1; -. [Q9H4F8-1]
RefSeq; NP_001030024.1; NM_001034852.2. [Q9H4F8-2]
RefSeq; NP_071420.1; NM_022137.5. [Q9H4F8-1]
UniGene; Hs.497349; -.
ProteinModelPortal; Q9H4F8; -.
SMR; Q9H4F8; -.
BioGrid; 122055; 30.
IntAct; Q9H4F8; 9.
STRING; 9606.ENSP00000355110; -.
iPTMnet; Q9H4F8; -.
PhosphoSitePlus; Q9H4F8; -.
BioMuta; SMOC1; -.
DMDM; 38258649; -.
EPD; Q9H4F8; -.
MaxQB; Q9H4F8; -.
PaxDb; Q9H4F8; -.
PeptideAtlas; Q9H4F8; -.
PRIDE; Q9H4F8; -.
ProteomicsDB; 80829; -.
ProteomicsDB; 80830; -. [Q9H4F8-2]
DNASU; 64093; -.
Ensembl; ENST00000361956; ENSP00000355110; ENSG00000198732. [Q9H4F8-2]
Ensembl; ENST00000381280; ENSP00000370680; ENSG00000198732. [Q9H4F8-1]
GeneID; 64093; -.
KEGG; hsa:64093; -.
UCSC; uc001xls.3; human. [Q9H4F8-1]
CTD; 64093; -.
DisGeNET; 64093; -.
EuPathDB; HostDB:ENSG00000198732.10; -.
GeneCards; SMOC1; -.
HGNC; HGNC:20318; SMOC1.
HPA; CAB034427; -.
HPA; HPA004153; -.
MalaCards; SMOC1; -.
MIM; 206920; phenotype.
MIM; 608488; gene.
neXtProt; NX_Q9H4F8; -.
OpenTargets; ENSG00000198732; -.
Orphanet; 1106; Microphthalmia with limb anomalies.
PharmGKB; PA134942329; -.
eggNOG; KOG4578; Eukaryota.
eggNOG; ENOG410YP7C; LUCA.
GeneTree; ENSGT00390000018436; -.
HOGENOM; HOG000234328; -.
HOVERGEN; HBG058558; -.
InParanoid; Q9H4F8; -.
OMA; RGHRTTG; -.
OrthoDB; EOG091G083O; -.
PhylomeDB; Q9H4F8; -.
TreeFam; TF320666; -.
ChiTaRS; SMOC1; human.
GenomeRNAi; 64093; -.
PRO; PR:Q9H4F8; -.
Proteomes; UP000005640; Chromosome 14.
Bgee; ENSG00000198732; Expressed in 164 organ(s), highest expression level in tendon of biceps brachii.
CleanEx; HS_SMOC1; -.
ExpressionAtlas; Q9H4F8; baseline and differential.
Genevisible; Q9H4F8; HS.
GO; GO:0005604; C:basement membrane; IEA:UniProtKB-SubCell.
GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
GO; GO:0050840; F:extracellular matrix binding; IEA:InterPro.
GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
GO; GO:0001654; P:eye development; IMP:UniProtKB.
GO; GO:0060173; P:limb development; IMP:UniProtKB.
GO; GO:0045667; P:regulation of osteoblast differentiation; IMP:UniProtKB.
CDD; cd16240; EFh_SPARC_SMOC1; 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; IPR002350; Kazal_dom.
InterPro; IPR036058; Kazal_dom_sf.
InterPro; IPR037639; SMOC1_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; PS51465; KAZAL_2; 1.
PROSITE; PS00484; THYROGLOBULIN_1_1; 2.
PROSITE; PS51162; THYROGLOBULIN_1_2; 2.
1: Evidence at protein level;
Alternative splicing; Basement membrane; Calcium; Complete proteome;
Developmental protein; Differentiation; Disease mutation;
Disulfide bond; Extracellular matrix; Glycoprotein; Metal-binding;
Microphthalmia; Polymorphism; Reference proteome; Repeat; Secreted;
Signal.
SIGNAL 1 26 {ECO:0000255}.
CHAIN 27 434 SPARC-related modular calcium-binding
protein 1.
/FTId=PRO_0000020316.
DOMAIN 37 89 Kazal-like. {ECO:0000255|PROSITE-
ProRule:PRU00798}.
DOMAIN 92 158 Thyroglobulin type-1 1.
{ECO:0000255|PROSITE-ProRule:PRU00500}.
DOMAIN 224 292 Thyroglobulin type-1 2.
{ECO:0000255|PROSITE-ProRule:PRU00500}.
DOMAIN 359 394 EF-hand 1.
DOMAIN 396 431 EF-hand 2.
CA_BIND 372 383 1. {ECO:0000255}.
CA_BIND 409 420 2. {ECO:0000255}.
CARBOHYD 214 214 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 374 374 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 43 74 {ECO:0000255|PROSITE-ProRule:PRU00798}.
DISULFID 47 67 {ECO:0000255|PROSITE-ProRule:PRU00798}.
DISULFID 56 87 {ECO:0000255|PROSITE-ProRule:PRU00798}.
DISULFID 95 118 {ECO:0000250}.
DISULFID 129 136 {ECO:0000250}.
DISULFID 138 158 {ECO:0000250}.
DISULFID 227 251 {ECO:0000250}.
DISULFID 262 269 {ECO:0000250}.
DISULFID 271 292 {ECO:0000250}.
VAR_SEQ 430 430 E -> EV (in isoform 2).
{ECO:0000303|PubMed:14702039,
ECO:0000303|PubMed:15489334}.
/FTId=VSP_008720.
VARIANT 82 82 V -> M (in dbSNP:rs10150925).
/FTId=VAR_034498.
VARIANT 278 278 R -> C (in OAS; dbSNP:rs776638586).
{ECO:0000269|PubMed:21750680}.
/FTId=VAR_069326.
VARIANT 283 283 T -> N (in OAS).
{ECO:0000269|PubMed:21750680}.
/FTId=VAR_069327.
VARIANT 286 286 R -> H (in OAS).
{ECO:0000269|PubMed:23646827}.
/FTId=VAR_069328.
SEQUENCE 434 AA; 48163 MW; 2CB639212BA42478 CRC64;
MLPARCARLL TPHLLLVLVQ LSPARGHRTT GPRFLISDRD PQCNLHCSRT QPKPICASDG
RSYESMCEYQ RAKCRDPTLG VVHRGRCKDA GQSKCRLERA QALEQAKKPQ EAVFVPECGE
DGSFTQVQCH TYTGYCWCVT PDGKPISGSS VQNKTPVCSG SVTDKPLSQG NSGRKDDGSK
PTPTMETQPV FDGDEITAPT LWIKHLVIKD SKLNNTNIRN SEKVYSCDQE RQSALEEAQQ
NPREGIVIPE CAPGGLYKPV QCHQSTGYCW CVLVDTGRPL PGTSTRYVMP SCESDARAKT
TEADDPFKDR ELPGCPEGKK MEFITSLLDA LTTDMVQAIN SAAPTGGGRF SEPDPSHTLE
ERVVHWYFSQ LDSNSSNDIN KREMKPFKRY VKKKAKPKKC ARRFTDYCDL NKDKVISLPE
LKGCLGVSKE GRLV


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