ID M3XT26_MUSPF Unreviewed; 667 AA.
AC M3XT26;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 62.
DE RecName: Full=SPARC-like protein 1 {ECO:0000256|PIRNR:PIRNR002574};
GN Name=SPARCL1 {ECO:0000313|Ensembl:ENSMPUP00000002226.1,
GN ECO:0000313|RefSeq:XP_004756168.1};
OS Mustela putorius furo (European domestic ferret) (Mustela furo).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Musteloidea; Mustelidae;
OC Mustelinae; Mustela.
OX NCBI_TaxID=9669 {ECO:0000313|Ensembl:ENSMPUP00000002226.1};
RN [1] {ECO:0000313|Ensembl:ENSMPUP00000002226.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (MAR-2023) to UniProtKB.
RN [2] {ECO:0000313|RefSeq:XP_004756168.1}
RP IDENTIFICATION.
RC TISSUE=Brain {ECO:0000313|RefSeq:XP_004756168.1};
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC matrix {ECO:0000256|PIRNR:PIRNR002574}.
CC -!- SIMILARITY: Belongs to the SPARC family.
CC {ECO:0000256|ARBA:ARBA00006404, ECO:0000256|PIRNR:PIRNR002574}.
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DR EMBL; AEYP01040849; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AEYP01040850; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AEYP01040851; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_004756168.1; XM_004756111.3.
DR STRING; 9669.ENSMPUP00000002226; -.
DR Ensembl; ENSMPUT00000002272.1; ENSMPUP00000002226.1; ENSMPUG00000002250.1.
DR GeneID; 101674240; -.
DR KEGG; mpuf:101674240; -.
DR CTD; 8404; -.
DR eggNOG; KOG4004; Eukaryota.
DR GeneTree; ENSGT00510000046787; -.
DR HOGENOM; CLU_026297_0_1_1; -.
DR OMA; CKRGHVC; -.
DR OrthoDB; 4695638at2759; -.
DR Proteomes; UP000000715; Unplaced.
DR GO; GO:0062023; C:collagen-containing extracellular matrix; IEA:InterPro.
DR GO; GO:0005615; C:extracellular space; IEA:UniProtKB-UniRule.
DR GO; GO:0098978; C:glutamatergic synapse; IEA:Ensembl.
DR GO; GO:0005509; F:calcium ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0007165; P:signal transduction; IEA:UniProtKB-UniRule.
DR GO; GO:0099560; P:synaptic membrane adhesion; IEA:Ensembl.
DR CDD; cd16231; EFh_SPARC_like; 1.
DR Gene3D; 3.30.60.30; -; 1.
DR Gene3D; 1.10.238.10; EF-hand; 1.
DR InterPro; IPR011992; EF-hand-dom_pair.
DR InterPro; IPR018247; EF_Hand_1_Ca_BS.
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 PANTHER; PTHR13866; SPARC OSTEONECTIN; 1.
DR PANTHER; PTHR13866:SF16; SPARC-LIKE PROTEIN 1; 1.
DR Pfam; PF09289; FOLN; 1.
DR Pfam; PF07648; Kazal_2; 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; SSF47473; EF-hand; 1.
DR SUPFAM; SSF57196; EGF/Laminin; 1.
DR SUPFAM; SSF100895; Kazal-type serine protease inhibitors; 1.
DR PROSITE; PS00018; EF_HAND_1; 1.
DR PROSITE; PS51465; KAZAL_2; 1.
DR PROSITE; PS00612; OSTEONECTIN_1; 1.
DR PROSITE; PS00613; OSTEONECTIN_2; 1.
PE 3: Inferred from homology;
KW Calcium {ECO:0000256|ARBA:ARBA00022837, ECO:0000256|PIRNR:PIRNR002574};
KW Extracellular matrix {ECO:0000256|ARBA:ARBA00022530,
KW ECO:0000256|PIRNR:PIRNR002574};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRNR:PIRNR002574};
KW Reference proteome {ECO:0000313|Proteomes:UP000000715};
KW Secreted {ECO:0000256|ARBA:ARBA00022525, ECO:0000256|PIRNR:PIRNR002574};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..16
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 17..667
FT /note="SPARC-like protein 1"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5041198393"
FT DOMAIN 458..514
FT /note="Kazal-like"
FT /evidence="ECO:0000259|PROSITE:PS51465"
FT REGION 65..360
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 386..427
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 65..93
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 149..164
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 178..206
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 219..246
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 252..268
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 286..327
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 667 AA; 75903 MW; 300E26AC5E45C85C CRC64;
MKTVPFFLYI LGAAAAIPTN ARFLSDHTKP TADSLSSIQQ AEILTTPNNT AIPMLRVEDA
ENEKEIAGSV DHPNHKAEKS SELKSKEENY DQSADQDQSY SPELRLQDEE ESESDLSENL
EYIPSEGTLD LQEDGGEPQK KKVPENIDSL APNISSTIDP NQQESITKTE KEQEQPINDL
HPQLNRSNKD SQDVSDQGNQ EQDPNIPNGE EEGEEEPGEV GTHNDNQERG RELPKEQSNS
KEEEDSTQSD DVLEESSQPT QVSKMQKDEF DQGNQEQEED SSNAEMEDET ASKINKHNQD
AEWQSQEEKP DVISNQEEID KKSVSEALPV EPTEAGNIMP TNHGANADAD DDPRHDASDD
YEFIPSETFI EAERSQSIAY NLKYEEEKER ERAHENGNVD ASEPGEYQEA KKAESSPKED
ESSYEDNRMV HGRDSCMNFQ CKRGHICKAD QQGKPHCVCQ DSVTCPPTKL LDQVCGTDNQ
TYASSCHLFA TKCKLEGTKK GHQLQLDYFG ACKSIPICTD FEVTQFPLRM RDWLKNILMQ
LYEANPEHAG YLNEKQRNKV KKIYLDEKRL LAGDHSIDLL LRDFKKNYHM YVYPVHWQFG
ELDQHPMDRV LTHSELAPLR ASLVPMEHCI TRFFEECDPN KDKHITLMEW GHCFGIKEED
IDENLLF
//
