SPRL1_COTJA
ID SPRL1_COTJA Reviewed; 676 AA.
AC P23499;
DT 01-NOV-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1991, sequence version 1.
DT 03-AUG-2022, entry version 108.
DE RecName: Full=SPARC-like protein 1;
DE AltName: Full=QR1 protein;
DE Flags: Precursor;
GN Name=SPARCL1; Synonyms=QR1;
OS Coturnix japonica (Japanese quail) (Coturnix coturnix japonica).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Perdicinae; Coturnix.
OX NCBI_TaxID=93934;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=2034690; DOI=10.1073/pnas.88.10.4503;
RA Guermah M., Crisanti P., Laugier D., Dezelee P., Bidou L., Pessac B.,
RA Calothy G.;
RT "Transcription of a quail gene expressed in embryonic retinal cells is shut
RT off sharply at hatching.";
RL Proc. Natl. Acad. Sci. U.S.A. 88:4503-4507(1991).
CC -!- FUNCTION: Could play a role in the late stage of neuroretina
CC morphogenesis.
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC matrix {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Glial (Mueller) cells of the neuroretina.
CC -!- DEVELOPMENTAL STAGE: Is transcribed at late phase of retinal
CC development in the embryo, and is shut off sharply at hatching.
CC -!- SIMILARITY: Belongs to the SPARC family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; M61908; AAA49499.1; -; mRNA.
DR EMBL; M61908; AAA49500.1; -; mRNA.
DR PIR; A39379; A39379.
DR AlphaFoldDB; P23499; -.
DR SMR; P23499; -.
DR Proteomes; UP000694412; Unplaced.
DR GO; GO:0062023; C:collagen-containing extracellular matrix; IEA:InterPro.
DR GO; GO:0005615; C:extracellular space; IEA:InterPro.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0007165; P:signal transduction; IEA:InterPro.
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 2: Evidence at transcript level;
KW Calcium; Disulfide bond; Extracellular matrix; Glycoprotein; Metal-binding;
KW Reference proteome; Secreted; Signal.
FT SIGNAL 1..16
FT CHAIN 17..676
FT /note="SPARC-like protein 1"
FT /id="PRO_0000020315"
FT DOMAIN 444..466
FT /note="Follistatin-like"
FT DOMAIN 462..523
FT /note="Kazal-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT DOMAIN 634..669
FT /note="EF-hand"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT REGION 35..151
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 173..369
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 385..437
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 35..50
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 69..90
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 91..124
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 181..200
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 201..225
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 239..312
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 326..369
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 395..412
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 413..427
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 647
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 649
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 651
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 658
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT CARBOHYD 182
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 318
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 396
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 413
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 435
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 488
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 445..456
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT DISULFID 450..466
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT DISULFID 468..502
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT DISULFID 474..495
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT DISULFID 484..521
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT DISULFID 527..638
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT DISULFID 646..662
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
SQ SEQUENCE 676 AA; 78143 MW; 60A96717828CCADA CRC64;
MKTVLLLICL LGSAFTTPTD PLNYQFGAHG QKTAEKHKYT HSEMPEEENT GFVNKGDVLS
GHRTIKAEVP VLDTQKDEPW ASRRQGQGDG EHQTKNSLRS INFLTLHSNP GLASDNQESN
SGSSREQHSS EHHQPRRHRK HGNMAGQWAL RGESPVDALG LVRERNTWKY NKNTVGLDEN
NNGSEEEEAG EEEDEEWGEE TDYRDMKHRA RGTSHGREYR RWQNENSRPS GEFLRDSSLP
VRITKRHGEK FSMEEESQEK LYKEGKLPLS KKNHNEDQGE KRQSEESKEH FQVVNQRKHR
AVTKRQDKEG SNAEEDDNDS GDDGEEDLGN VWREAVYEEE ERMQSNDQDS ITNKQKEEIT
AGDDSGVYRE MQDYKGDKIK DVTHSEDNHY HHEPPNSSSK QQLQTSSSVE SMNSTEHEDE
VKTTGGSYHE ESARNSTGKA LPDLCRNFHC KRGKVCQADK QGKPSCICQD PAACPSTKDY
KRVCGTDNKT YDGTCQLFGT KCQLEGTKMG RQLHLDYMGA CKHIPHCTDY EVNQFPLRMR
DWLKNILMQY YERDQDTSAF LTEKQRNKVK KIYLNEKRLV SGEHPVELLL HDFEKNYHMY
LYPVHWQFYQ LDQHPVDRSL THSELAPLRA SLVPMEHCIT RFFQECDGDQ DKLITLKEWC
HCFAIKEEDI NENLLF
