SPRL1_RAT
ID SPRL1_RAT Reviewed; 634 AA.
AC P24054;
DT 01-MAR-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-1992, sequence version 1.
DT 03-AUG-2022, entry version 140.
DE RecName: Full=SPARC-like protein 1;
DE AltName: Full=Matrix glycoprotein Sc1;
DE Flags: Precursor;
GN Name=Sparcl1; Synonyms=Sc1;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Brain;
RX PubMed=1690015; DOI=10.1016/0896-6273(90)90452-l;
RA Johnston I.G., Paladino T., Gurd J.W., Brown I.R.;
RT "Molecular cloning of SC1: a putative brain extracellular matrix
RT glycoprotein showing partial similarity to osteonectin/BM40/SPARC.";
RL Neuron 4:165-176(1990).
RN [2]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-68; SER-76; SER-84; SER-151;
RP SER-159; SER-259; SER-333; SER-340 AND SER-370, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC matrix.
CC -!- TISSUE SPECIFICITY: Expressed in many types of neurons in the brain.
CC -!- DEVELOPMENTAL STAGE: Expressed throughout postnatal development of the
CC brain and present at high levels in the adult.
CC -!- SIMILARITY: Belongs to the SPARC family. {ECO:0000305}.
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DR EMBL; U27562; AAA68708.1; -; mRNA.
DR PIR; I58173; GERTX1.
DR RefSeq; NP_037078.1; NM_012946.1.
DR AlphaFoldDB; P24054; -.
DR SMR; P24054; -.
DR STRING; 10116.ENSRNOP00000020357; -.
DR GlyGen; P24054; 3 sites.
DR iPTMnet; P24054; -.
DR PhosphoSitePlus; P24054; -.
DR PaxDb; P24054; -.
DR PRIDE; P24054; -.
DR GeneID; 25434; -.
DR KEGG; rno:25434; -.
DR CTD; 8404; -.
DR RGD; 2531; Sparcl1.
DR eggNOG; KOG4004; Eukaryota.
DR InParanoid; P24054; -.
DR OrthoDB; 1528521at2759; -.
DR PhylomeDB; P24054; -.
DR Reactome; R-RNO-381426; Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs).
DR Reactome; R-RNO-8957275; Post-translational protein phosphorylation.
DR PRO; PR:P24054; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0098965; C:extracellular matrix of synaptic cleft; IDA:SynGO.
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; IDA:RGD.
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; IDA:SynGO.
DR GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR GO; GO:0099560; P:synaptic membrane adhesion; ISO:RGD.
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..634
FT /note="SPARC-like protein 1"
FT /id="PRO_0000020314"
FT DOMAIN 402..424
FT /note="Follistatin-like"
FT DOMAIN 420..481
FT /note="Kazal-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT DOMAIN 592..627
FT /note="EF-hand"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT REGION 50..335
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 360..398
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 51..88
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 107..121
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 132..169
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 170..187
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 188..202
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 203..217
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 220..258
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 259..279
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 289..305
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 360..376
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 377..398
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 605
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 607
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 609
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 611
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 616
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT MOD_RES 68
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 76
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 84
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 151
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 159
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 259
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 333
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 340
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 370
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 390
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P70663"
FT CARBOHYD 144
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 368
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 446
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 403..414
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT DISULFID 408..424
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT DISULFID 426..460
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT DISULFID 432..453
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT DISULFID 442..479
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT DISULFID 485..596
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT DISULFID 604..620
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
SQ SEQUENCE 634 AA; 70634 MW; 0EE63805AA91957D CRC64;
MKAVLLLLYA LGIAAAVPTT FLSDHSNPTS ATLPTLEDAT VPTVPAEAAA DIEKHPNHKA
EKPSALNSEE EAHEQSTEQD KTYSFEVDLK DEEDGDGDLS VDPTERTLDL QEGTSEPQQK
RLPENADFPA TVSTPFVDSD QPANITKGEE SQEQPVSDSH QQQDESGKQT QDSMTEESHK
QDPGIPNEEK EEEEDPEDVG APSDNQEEEK EPPEEQPTSK WEGNGDQSED ILQESSQPTQ
ISKTKNDFEQ GSQGQEGDSN AEGEDKAAGS KEHLPHTEWQ GQEGRAGLDA IGNRKDTDEE
KAVSTEPTDA AVVPRNHGAS DNGGGDDSKH GASDDYFIPS QEFLEAERMH SLSYYLKYGE
ETPDESENRS EAGDNQGAKK AESSPNAEPS DEGNSRGHSA DSCMNFQCKR GHTCKTDQHG
KPHCVCQDPE TCPPAKILDQ ACGTDNQTYA SSCHLFATKC MLEGTKKGHQ LQLDYFGACK
SIPACTDFEV AQFPLRMRDW LKNILMQLYE PNPKHGGYLN EKQRSKVKKI YLDEKRLLAG
DHPIELLLRD FKKNYHMYVY PVHWQFNELD QHPADRILTH SELAPLRASL VPMEHCITRF
FEECDPNKDK HITLKEWGHC FGIKEEDIDE NLLF
