SPRL1_MOUSE
ID SPRL1_MOUSE Reviewed; 650 AA.
AC P70663; E9QPH2; P97810; Q99L82;
DT 19-SEP-2002, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 3.
DT 03-AUG-2022, entry version 171.
DE RecName: Full=SPARC-like protein 1;
DE AltName: Full=Extracellular matrix protein 2;
DE AltName: Full=Matrix glycoprotein Sc1;
DE Flags: Precursor;
GN Name=Sparcl1; Synonyms=Ecm2, Sc1;
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 [GENOMIC DNA / MRNA].
RC STRAIN=129/SvJ;
RX PubMed=8938431; DOI=10.1101/gr.6.11.1077;
RA McKinnon P.J., Kapsetaki M., Margolskee R.F.;
RT "The exon structure of the mouse Sc1 gene is very similar to the mouse
RT Sparc gene.";
RL Genome Res. 6:1077-1083(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Brain;
RX PubMed=9199668; DOI=10.1177/002215549704500607;
RA Soderling J.A., Reed M.J., Corsa A., Sage E.H.;
RT "Cloning and expression of murine SC1, a gene product homologous to
RT SPARC.";
RL J. Histochem. Cytochem. 45:823-835(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-353 AND SER-406, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, and Lung;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC matrix.
CC -!- TISSUE SPECIFICITY: Highest expression in brain. Moderate levels in
CC heart, adrenal gland, epididymis and lung. Low levels in kidney, eye,
CC liver, spleen, submandibular gland and testis.
CC -!- SIMILARITY: Belongs to the SPARC family. {ECO:0000305}.
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DR EMBL; U66166; AAB06444.1; -; Genomic_DNA.
DR EMBL; U66158; AAB06444.1; JOINED; Genomic_DNA.
DR EMBL; U66159; AAB06444.1; JOINED; Genomic_DNA.
DR EMBL; U66160; AAB06444.1; JOINED; Genomic_DNA.
DR EMBL; U66161; AAB06444.1; JOINED; Genomic_DNA.
DR EMBL; U66162; AAB06444.1; JOINED; Genomic_DNA.
DR EMBL; U66163; AAB06444.1; JOINED; Genomic_DNA.
DR EMBL; U66164; AAB06444.1; JOINED; Genomic_DNA.
DR EMBL; U66165; AAB06444.1; JOINED; Genomic_DNA.
DR EMBL; U77330; AAC53172.1; -; mRNA.
DR EMBL; U64827; AAB08451.1; -; mRNA.
DR EMBL; AL714024; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC003759; AAH03759.1; -; mRNA.
DR CCDS; CCDS19483.1; -.
DR RefSeq; NP_034227.3; NM_010097.4.
DR RefSeq; XP_006534831.1; XM_006534768.1.
DR RefSeq; XP_017176145.1; XM_017320656.1.
DR AlphaFoldDB; P70663; -.
DR SMR; P70663; -.
DR BioGRID; 199367; 1.
DR IntAct; P70663; 4.
DR MINT; P70663; -.
DR STRING; 10090.ENSMUSP00000031249; -.
DR GlyConnect; 2737; 9 N-Linked glycans (2 sites).
DR GlyGen; P70663; 3 sites, 9 N-linked glycans (2 sites).
DR iPTMnet; P70663; -.
DR PhosphoSitePlus; P70663; -.
DR CPTAC; non-CPTAC-3616; -.
DR MaxQB; P70663; -.
DR PaxDb; P70663; -.
DR PeptideAtlas; P70663; -.
DR PRIDE; P70663; -.
DR ProteomicsDB; 263328; -.
DR Antibodypedia; 25430; 283 antibodies from 32 providers.
DR DNASU; 13602; -.
DR Ensembl; ENSMUST00000031249; ENSMUSP00000031249; ENSMUSG00000029309.
DR GeneID; 13602; -.
DR KEGG; mmu:13602; -.
DR UCSC; uc008ykb.2; mouse.
DR CTD; 8404; -.
DR MGI; MGI:108110; Sparcl1.
DR VEuPathDB; HostDB:ENSMUSG00000029309; -.
DR eggNOG; KOG4004; Eukaryota.
DR GeneTree; ENSGT00510000046787; -.
DR HOGENOM; CLU_026297_0_1_1; -.
DR InParanoid; P70663; -.
DR OMA; CKRGHVC; -.
DR OrthoDB; 1528521at2759; -.
DR PhylomeDB; P70663; -.
DR TreeFam; TF319356; -.
DR Reactome; R-MMU-381426; Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs).
DR Reactome; R-MMU-8957275; Post-translational protein phosphorylation.
DR BioGRID-ORCS; 13602; 5 hits in 71 CRISPR screens.
DR ChiTaRS; Sparcl1; mouse.
DR PRO; PR:P70663; -.
DR Proteomes; UP000000589; Chromosome 5.
DR RNAct; P70663; protein.
DR Bgee; ENSMUSG00000029309; Expressed in cerebellar nuclear complex and 246 other tissues.
DR ExpressionAtlas; P70663; baseline and differential.
DR Genevisible; P70663; MM.
DR GO; GO:0098965; C:extracellular matrix of synaptic cleft; ISO:MGI.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0098978; C:glutamatergic synapse; IDA:SynGO.
DR GO; GO:0045202; C:synapse; ISO:MGI.
DR GO; GO:0005509; F:calcium ion binding; IBA:GO_Central.
DR GO; GO:0005518; F:collagen binding; IBA:GO_Central.
DR GO; GO:0050840; F:extracellular matrix binding; IBA:GO_Central.
DR GO; GO:0048856; P:anatomical structure development; IBA:GO_Central.
DR GO; GO:0050807; P:regulation of synapse organization; ISO:MGI.
DR GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR GO; GO:0099560; P:synaptic membrane adhesion; IDA:SynGO.
DR InterPro; IPR011992; EF-hand-dom_pair.
DR InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR InterPro; IPR002048; EF_hand_dom.
DR InterPro; IPR003645; Fol_N.
DR InterPro; IPR015369; Follistatin/Osteonectin_EGF.
DR InterPro; IPR002350; Kazal_dom.
DR InterPro; IPR036058; Kazal_dom_sf.
DR InterPro; IPR001999; Osteonectin_CS.
DR InterPro; IPR016359; SPARC-like_p1.
DR InterPro; IPR019577; SPARC/Testican_Ca-bd-dom.
DR Pfam; PF09289; FOLN; 1.
DR Pfam; PF00050; Kazal_1; 1.
DR Pfam; PF10591; SPARC_Ca_bdg; 1.
DR PIRSF; PIRSF002574; SPARC-like_p1; 1.
DR SMART; SM00274; FOLN; 1.
DR SMART; SM00280; KAZAL; 1.
DR SUPFAM; SSF100895; SSF100895; 1.
DR SUPFAM; SSF47473; SSF47473; 1.
DR PROSITE; PS00018; EF_HAND_1; 1.
DR PROSITE; PS50222; EF_HAND_2; 1.
DR PROSITE; PS51465; KAZAL_2; 1.
DR PROSITE; PS00612; OSTEONECTIN_1; 1.
DR PROSITE; PS00613; OSTEONECTIN_2; 1.
PE 1: Evidence at protein level;
KW Calcium; Disulfide bond; Extracellular matrix; Glycoprotein; Metal-binding;
KW Phosphoprotein; Reference proteome; Secreted; Signal.
FT SIGNAL 1..16
FT /evidence="ECO:0000255"
FT CHAIN 17..650
FT /note="SPARC-like protein 1"
FT /id="PRO_0000020313"
FT DOMAIN 418..440
FT /note="Follistatin-like"
FT DOMAIN 436..497
FT /note="Kazal-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT DOMAIN 608..643
FT /note="EF-hand"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT REGION 51..352
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 375..415
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 54..90
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 108..173
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 186..214
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 215..244
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 245..270
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 272..296
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 379..394
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 395..415
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 621
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 623
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 625
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 627
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 632
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT MOD_RES 70
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P24054"
FT MOD_RES 78
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P24054"
FT MOD_RES 86
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P24054"
FT MOD_RES 155
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P24054"
FT MOD_RES 163
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P24054"
FT MOD_RES 272
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P24054"
FT MOD_RES 353
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 406
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT CARBOHYD 148
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 168
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 462
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 419..430
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT DISULFID 424..440
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT DISULFID 442..476
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT DISULFID 448..469
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT DISULFID 458..495
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT DISULFID 501..612
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT DISULFID 620..636
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT CONFLICT 25
FT /note="S -> F (in Ref. 2; AAC53172)"
FT /evidence="ECO:0000305"
FT CONFLICT 59
FT /note="S -> N (in Ref. 1; AAB06444/AAB08451, 2; AAC53172
FT and 4; AAH03759)"
FT /evidence="ECO:0000305"
FT CONFLICT 199
FT /note="D -> E (in Ref. 1; AAB06444/AAB08451)"
FT /evidence="ECO:0000305"
FT CONFLICT 281
FT /note="A -> S (in Ref. 1; AAB06444/AAB08451)"
FT /evidence="ECO:0000305"
FT CONFLICT 385
FT /note="R -> Q (in Ref. 1; AAB06444/AAB08451)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 650 AA; 72287 MW; 8E2CA0145DE3E66E CRC64;
MKAVLLLLCA LGTAVAIPTS TRFLSDHSNP TTATLVTPED ATVPIAGVEA TADIENHPSD
KAEKPSALNS EEETHEQSTE QDKTYSFEVD LKDEEDGDGD LSVDPTEGTL TLDLQEGTSE
PQQKSLPENG DFPATVSTSY VDPNQRANIT KGKESQEQPV SDSHQQPNES SKQTQDLKAE
ESQTQDPDIP NEEEEEEEDE EEEEEEEPED IGAPSDNQEE GKEPLEEQPT SKWEGNREQS
DDTLEESSQP TQISKTEKHQ SEQGNQGQES DSEAEGEDKA AGSKEHIPHT EQQDQEGKAG
LEAIGNQKDT DEKAVSTEPT DAAVVPRSHG GAGDNGGGDD SKHGAGDDYF IPSQEFLEAE
RMHSLSYYLK YGGGEETTTG ESENRREAAD NQEAKKAESS PNAEPSDEGN SREHSAGSCT
NFQCKRGHIC KTDPQGKPHC VCQDPETCPP AKILDQACGT DNQTYASSCH LFATKCRLEG
TKKGHQLQLD YFGACKSIPA CTDFEVAQFP LRMRDWLKNI LMQLYEPNPK HGGYLNEKQR
SKVKKIYLDE KRLLAGDHPI ELLLRDFKKN YHMYVYPVHW QFNELDQHPA DRILTHSELA
PLRASLVPME HCITRFFEEC DPNKDKHITL KEWGHCFGIK EEDIDENLLF
