SMOC1_MOUSE
ID SMOC1_MOUSE Reviewed; 463 AA.
AC Q8BLY1; Q9WVN9;
DT 31-OCT-2003, integrated into UniProtKB/Swiss-Prot.
DT 31-OCT-2003, sequence version 2.
DT 03-AUG-2022, entry version 148.
DE RecName: Full=SPARC-related modular calcium-binding protein 1;
DE AltName: Full=SPARC-related gene protein;
DE AltName: Full=Secreted modular calcium-binding protein 1;
DE Short=SMOC-1;
DE Flags: Precursor;
GN Name=Smoc1; Synonyms=Srg;
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 2).
RC STRAIN=129/Sv;
RA Poleev A., Plachov D.;
RT "A Sparc-related gene (SRG).";
RL Submitted (JUN-1998) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Aorta, and Vein;
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 2).
RC TISSUE=Mammary tumor;
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, DEVELOPMENTAL STAGE, AND DISRUPTION PHENOTYPE.
RX PubMed=21194678; DOI=10.1016/j.ajhg.2010.11.012;
RA Okada I., Hamanoue H., Terada K., Tohma T., Megarbane A., Chouery E.,
RA Abou-Ghoch J., Jalkh N., Cogulu O., Ozkinay F., Horie K., Takeda J.,
RA Furuichi T., Ikegawa S., Nishiyama K., Miyatake S., Nishimura A.,
RA Mizuguchi T., Niikawa N., Hirahara F., Kaname T., Yoshiura K.,
RA Tsurusaki Y., Doi H., Miyake N., Furukawa T., Matsumoto N., Saitsu H.;
RT "SMOC1 is essential for ocular and limb development in humans and mice.";
RL Am. J. Hum. Genet. 88:30-41(2011).
RN [5]
RP FUNCTION, AND DEVELOPMENTAL STAGE.
RX PubMed=21750680; DOI=10.1371/journal.pgen.1002114;
RA Rainger J., van Beusekom E., Ramsay J.K., McKie L., Al-Gazali L.,
RA Pallotta R., Saponari A., Branney P., Fisher M., Morrison H., Bicknell L.,
RA Gautier P., Perry P., Sokhi K., Sexton D., Bardakjian T.M., Schneider A.S.,
RA Elcioglu N., Ozkinay F., Koenig R., Megarbane A., Semerci C.N., Khan A.,
RA Zafar S., Hennekam R., Sousa S.B., Ramos L., Garavelli L., Furga A.S.,
RA Wischmeijer A., Jackson I.J., Gillessen-Kaesbach G., Brunner H.G.,
RA Wieczorek D., van Bokhoven H., Fitzpatrick D.R.;
RT "Loss of the BMP antagonist, SMOC-1, causes Ophthalmo-acromelic
RT (Waardenburg Anophthalmia) syndrome in humans and mice.";
RL PLoS Genet. 7:E1002114-E1002114(2011).
CC -!- FUNCTION: Probable regulator of osteoblast differentiation. Plays
CC essential roles in both eye and limb development.
CC {ECO:0000269|PubMed:21194678, ECO:0000269|PubMed:21750680}.
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC matrix, basement membrane {ECO:0000250}. Note=In or around the basement
CC membrane. {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8BLY1-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8BLY1-2; Sequence=VSP_008721;
CC -!- TISSUE SPECIFICITY: Widely expressed in many tissues with a strongest
CC signal in ovary.
CC -!- DEVELOPMENTAL STAGE: Found in the forebrain, midbrain, hindbrain,
CC pharyngeal arch, somites, and forelimb buds at day 9.5 dpc. At day 10.5
CC dpc, strongly expressed in dorsal neural tube, developing pharyngeal
CC arches and frontonasal region with low expression in the ectoderm
CC overlying the developing optic vesicle, expression can be observed in
CC the optic stalk. At 11.5 dpc it is localized to the closure site of the
CC optic cup. In developing limbs between days 10.5 dpc and 11.5 dpc, it
CC is found in both dorsal and ventral regions, but expression is
CC predominant dorsal in hindlimb bud and not detected in the most
CC anterior, posterior, and distal parts of limb buds. Expression
CC coinciding with chondrogenic condensation can be observed at 12.5 dpc.
CC Expression is restricted to future synovial joint regions at day 13.5
CC dpc. {ECO:0000269|PubMed:21194678, ECO:0000269|PubMed:21750680}.
CC -!- PTM: Glycosylated. {ECO:0000250}.
CC -!- DISRUPTION PHENOTYPE: Null mice present with a phenotype resembling
CC human microphthalmia with limb anomalies. The phenotype includes
CC aplasia or hypoplasia of optic nerves, hypoplastic fibula and bowed
CC tibia, and syndactyly in limbs. A thinned and irregular ganglion cell
CC layer and atrophy of the anteroventral part of the retina is observed.
CC {ECO:0000269|PubMed:21194678}.
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DR EMBL; AF070470; AAD41590.1; -; mRNA.
DR EMBL; AK040931; BAC30750.1; -; mRNA.
DR EMBL; BC031804; AAH31804.1; -; mRNA.
DR CCDS; CCDS26017.1; -. [Q8BLY1-2]
DR CCDS; CCDS49102.1; -. [Q8BLY1-1]
DR RefSeq; NP_001139689.1; NM_001146217.1.
DR RefSeq; NP_071711.2; NM_022316.2.
DR AlphaFoldDB; Q8BLY1; -.
DR STRING; 10090.ENSMUSP00000105976; -.
DR GlyGen; Q8BLY1; 2 sites.
DR iPTMnet; Q8BLY1; -.
DR PhosphoSitePlus; Q8BLY1; -.
DR MaxQB; Q8BLY1; -.
DR PaxDb; Q8BLY1; -.
DR PRIDE; Q8BLY1; -.
DR ProteomicsDB; 261443; -. [Q8BLY1-1]
DR ProteomicsDB; 261444; -. [Q8BLY1-2]
DR DNASU; 64075; -.
DR GeneID; 64075; -.
DR KEGG; mmu:64075; -.
DR UCSC; uc007obu.2; mouse. [Q8BLY1-1]
DR CTD; 64093; -.
DR MGI; MGI:1929878; Smoc1.
DR eggNOG; KOG4578; Eukaryota.
DR InParanoid; Q8BLY1; -.
DR OrthoDB; 1057719at2759; -.
DR PhylomeDB; Q8BLY1; -.
DR TreeFam; TF320666; -.
DR BioGRID-ORCS; 64075; 1 hit in 57 CRISPR screens.
DR ChiTaRS; Smoc1; mouse.
DR PRO; PR:Q8BLY1; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; Q8BLY1; protein.
DR GO; GO:0005604; C:basement membrane; IDA:MGI.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0050840; F:extracellular matrix binding; IDA:MGI.
DR GO; GO:0008201; F:heparin binding; IBA:GO_Central.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR GO; GO:0030198; P:extracellular matrix organization; IDA:MGI.
DR GO; GO:0001654; P:eye development; IMP:UniProtKB.
DR GO; GO:0060173; P:limb development; IMP:UniProtKB.
DR GO; GO:0010811; P:positive regulation of cell-substrate adhesion; IDA:MGI.
DR GO; GO:0045667; P:regulation of osteoblast differentiation; ISO:MGI.
DR CDD; cd16240; EFh_SPARC_SMOC1; 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; IPR002350; Kazal_dom.
DR InterPro; IPR036058; Kazal_dom_sf.
DR InterPro; IPR037639; SMOC1_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; SSF100895; SSF100895; 1.
DR SUPFAM; SSF47473; SSF47473; 1.
DR SUPFAM; SSF57610; SSF57610; 2.
DR PROSITE; PS00018; EF_HAND_1; 2.
DR PROSITE; PS51465; KAZAL_2; 1.
DR PROSITE; PS00484; THYROGLOBULIN_1_1; 2.
DR PROSITE; PS51162; THYROGLOBULIN_1_2; 2.
PE 2: Evidence at transcript level;
KW Alternative splicing; Basement membrane; Calcium; Developmental protein;
KW Differentiation; Disulfide bond; Extracellular matrix; Glycoprotein;
KW Metal-binding; Reference proteome; Repeat; Secreted; Signal.
FT SIGNAL 1..25
FT /evidence="ECO:0000255"
FT CHAIN 26..463
FT /note="SPARC-related modular calcium-binding protein 1"
FT /id="PRO_0000020317"
FT DOMAIN 36..88
FT /note="Kazal-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT DOMAIN 91..157
FT /note="Thyroglobulin type-1 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00500"
FT DOMAIN 234..302
FT /note="Thyroglobulin type-1 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00500"
FT DOMAIN 369..404
FT /note="EF-hand 1"
FT DOMAIN 406..441
FT /note="EF-hand 2"
FT BINDING 382
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10142"
FT BINDING 384
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10142"
FT BINDING 386
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10142"
FT BINDING 388
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10142"
FT BINDING 393
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10142"
FT BINDING 419
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10142"
FT BINDING 421
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10142"
FT BINDING 423
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10142"
FT BINDING 430
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10142"
FT CARBOHYD 224
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 384
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 42..73
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT DISULFID 46..66
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT DISULFID 55..86
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT DISULFID 94..117
FT /evidence="ECO:0000250"
FT DISULFID 128..135
FT /evidence="ECO:0000250"
FT DISULFID 137..157
FT /evidence="ECO:0000250"
FT DISULFID 237..261
FT /evidence="ECO:0000250"
FT DISULFID 272..279
FT /evidence="ECO:0000250"
FT DISULFID 281..302
FT /evidence="ECO:0000250"
FT VAR_SEQ 175..185
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334, ECO:0000303|Ref.1"
FT /id="VSP_008721"
FT CONFLICT 311
FT /note="V -> I (in Ref. 2; BAC30750)"
FT /evidence="ECO:0000305"
SQ 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
