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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
 
 
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