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

 SMOC1_MOUSE             Reviewed;         463 AA.
Q8BLY1; Q9WVN9;
31-OCT-2003, integrated into UniProtKB/Swiss-Prot.
31-OCT-2003, sequence version 2.
18-JUL-2018, entry version 134.
RecName: Full=SPARC-related modular calcium-binding protein 1;
AltName: Full=SPARC-related gene protein;
AltName: Full=Secreted modular calcium-binding protein 1;
Short=SMOC-1;
Flags: Precursor;
Name=Smoc1; Synonyms=Srg;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
STRAIN=129/Sv;
Poleev A., Plachov D.;
"A Sparc-related gene (SRG).";
Submitted (JUN-1998) to the EMBL/GenBank/DDBJ databases.
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
STRAIN=C57BL/6J; TISSUE=Aorta, and Vein;
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
TISSUE=Mammary tumor;
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).
[4]
FUNCTION, DEVELOPMENTAL STAGE, AND DISRUPTION PHENOTYPE.
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).
[5]
FUNCTION, AND DEVELOPMENTAL STAGE.
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).
-!- FUNCTION: Probable regulator of osteoblast differentiation. Plays
essential roles in both eye and limb development.
{ECO:0000269|PubMed:21194678, ECO:0000269|PubMed:21750680}.
-!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
matrix, basement membrane {ECO:0000250}. Note=In or around the
basement membrane. {ECO:0000250}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q8BLY1-1; Sequence=Displayed;
Note=No experimental confirmation available.;
Name=2;
IsoId=Q8BLY1-2; Sequence=VSP_008721;
-!- TISSUE SPECIFICITY: Widely expressed in many tissues with a
strongest signal in ovary.
-!- DEVELOPMENTAL STAGE: Found in the forebrain, midbrain, hindbrain,
pharyngeal arch, somites, and forelimb buds at day E9.5. At day
E10.5, strongly expressed in dorsal neural tube, developing
pharyngeal arches and frontonasal region with low expression in
the ectoderm overlying the developing optic vesicle, expression
can be observed in the optic stalk. At E11.5 it is localized to
the closure site of the optic cup. In developing limbs between
days E10.5 and E11.5, it is found in both dorsal and ventral
regions, but expression is predominant dorsal in hindlimb bud and
not detected in the most anterior, posterior, and distal parts of
limb buds. Expression coinciding with chondrogenic condensation
can be observed at E12.5. Expression is restricted to future
synovial joint regions at day E13.5. {ECO:0000269|PubMed:21194678,
ECO:0000269|PubMed:21750680}.
-!- PTM: Glycosylated. {ECO:0000250}.
-!- DISRUPTION PHENOTYPE: Null mice present with a phenotype
resembling human microphthalmia with limb anomalies. The phenotype
includes aplasia or hypoplasia of optic nerves, hypoplastic fibula
and bowed tibia, and syndactyly in limbs. A thinned and irregular
ganglion cell layer and atrophy of the anteroventral part of the
retina is observed. {ECO:0000269|PubMed:21194678}.
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EMBL; AF070470; AAD41590.1; -; mRNA.
EMBL; AK040931; BAC30750.1; -; mRNA.
EMBL; BC031804; AAH31804.1; -; mRNA.
CCDS; CCDS26017.1; -. [Q8BLY1-2]
CCDS; CCDS49102.1; -. [Q8BLY1-1]
RefSeq; NP_001139689.1; NM_001146217.1.
RefSeq; NP_071711.2; NM_022316.2.
UniGene; Mm.273295; -.
ProteinModelPortal; Q8BLY1; -.
SMR; Q8BLY1; -.
STRING; 10090.ENSMUSP00000105976; -.
iPTMnet; Q8BLY1; -.
PhosphoSitePlus; Q8BLY1; -.
PaxDb; Q8BLY1; -.
PRIDE; Q8BLY1; -.
GeneID; 64075; -.
KEGG; mmu:64075; -.
UCSC; uc007obu.2; mouse. [Q8BLY1-1]
CTD; 64093; -.
MGI; MGI:1929878; Smoc1.
eggNOG; KOG4578; Eukaryota.
eggNOG; ENOG410YP7C; LUCA.
HOGENOM; HOG000234328; -.
HOVERGEN; HBG058558; -.
InParanoid; Q8BLY1; -.
PhylomeDB; Q8BLY1; -.
TreeFam; TF320666; -.
ChiTaRS; Smoc1; mouse.
PRO; PR:Q8BLY1; -.
Proteomes; UP000000589; Unplaced.
GO; GO:0005604; C:basement membrane; IDA:MGI.
GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
GO; GO:0050840; F:extracellular matrix binding; IDA:MGI.
GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
GO; GO:0030198; P:extracellular matrix organization; IDA:MGI.
GO; GO:0001654; P:eye development; IMP:UniProtKB.
GO; GO:0060173; P:limb development; IMP:UniProtKB.
GO; GO:0010811; P:positive regulation of cell-substrate adhesion; IDA:MGI.
GO; GO:0045667; P:regulation of osteoblast differentiation; ISO:MGI.
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.
2: Evidence at transcript level;
Alternative splicing; Basement membrane; Calcium; Complete proteome;
Developmental protein; Differentiation; Disulfide bond;
Extracellular matrix; Glycoprotein; Metal-binding; Reference proteome;
Repeat; Secreted; Signal.
SIGNAL 1 25 {ECO:0000255}.
CHAIN 26 463 SPARC-related modular calcium-binding
protein 1.
/FTId=PRO_0000020317.
DOMAIN 36 88 Kazal-like. {ECO:0000255|PROSITE-
ProRule:PRU00798}.
DOMAIN 91 157 Thyroglobulin type-1 1.
{ECO:0000255|PROSITE-ProRule:PRU00500}.
DOMAIN 234 302 Thyroglobulin type-1 2.
{ECO:0000255|PROSITE-ProRule:PRU00500}.
DOMAIN 369 404 EF-hand 1.
DOMAIN 406 441 EF-hand 2.
CA_BIND 382 393 1. {ECO:0000255}.
CA_BIND 419 430 2. {ECO:0000255}.
CARBOHYD 224 224 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 384 384 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 42 73 {ECO:0000255|PROSITE-ProRule:PRU00798}.
DISULFID 46 66 {ECO:0000255|PROSITE-ProRule:PRU00798}.
DISULFID 55 86 {ECO:0000255|PROSITE-ProRule:PRU00798}.
DISULFID 94 117 {ECO:0000250}.
DISULFID 128 135 {ECO:0000250}.
DISULFID 137 157 {ECO:0000250}.
DISULFID 237 261 {ECO:0000250}.
DISULFID 272 279 {ECO:0000250}.
DISULFID 281 302 {ECO:0000250}.
VAR_SEQ 175 185 Missing (in isoform 2).
{ECO:0000303|PubMed:15489334,
ECO:0000303|Ref.1}.
/FTId=VSP_008721.
CONFLICT 311 311 V -> I (in Ref. 2; BAC30750).
{ECO:0000305}.
SEQUENCE 463 AA; 51076 MW; C4EE880F34259698 CRC64;
MLPARVRLLT PHLLLVLVQL SPAGGHRTTG PRFLISDRDP PCNPHCPRTQ PKPICASDGR
SYESMCEYQR AKCRDPALAV VHRGRCKDAG QSKCRLERAQ ALEQAKKPQE AVFVPECGED
GSFTQVQCHT YTGYCWCVTP DGKPISGSSV QNKTPVCSGP VTDKPLSQGN SGRKVSFRFF
LTLNSDDGSK PTPTMETQPV FDGDEITAPT LWIKHLVIKD SKLNNTNVRN SEKVHSCDQE
RQSALEEARQ NPREGIVIPE CAPGGLYKPV QCHQSTGYCW CVLVDTGRPL PGTSTRYVMP
SCESDARAKS VEADDPFKDR ELPGCPEGKK MEFITSLLDA LTTDMVQAIN SAAPTGGGRF
SEPDPSHTLE ERVAHWYFSQ LDSNSSDDIN KREMKPFKRY VKKKAKPKKC ARRFTDYCDL
NKDKVISLPE LKGCLGVSKE GGSLGSFPQG KRAGTNPFIG RLV


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