ID A0A1S3A3L5_ERIEU Unreviewed; 303 AA.
AC A0A1S3A3L5;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE RecName: Full=SPARC {ECO:0000256|ARBA:ARBA00019049};
DE AltName: Full=Osteonectin {ECO:0000256|ARBA:ARBA00032081};
DE AltName: Full=Secreted protein acidic and rich in cysteine {ECO:0000256|ARBA:ARBA00031976};
GN Name=SPARC {ECO:0000313|RefSeq:XP_007528828.1};
OS Erinaceus europaeus (Western European hedgehog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Eulipotyphla; Erinaceidae; Erinaceinae;
OC Erinaceus.
OX NCBI_TaxID=9365 {ECO:0000313|Proteomes:UP000079721, ECO:0000313|RefSeq:XP_007528828.1};
RN [1] {ECO:0000313|RefSeq:XP_007528828.1}
RP IDENTIFICATION.
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- FUNCTION: Appears to regulate cell growth through interactions with the
CC extracellular matrix and cytokines. Binds calcium and copper, several
CC types of collagen, albumin, thrombospondin, PDGF and cell membranes.
CC There are two calcium binding sites; an acidic domain that binds 5 to 8
CC Ca(2+) with a low affinity and an EF-hand loop that binds a Ca(2+) ion
CC with a high affinity. {ECO:0000256|ARBA:ARBA00025574}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004370}.
CC Secreted, extracellular space, extracellular matrix, basement membrane
CC {ECO:0000256|ARBA:ARBA00004302}.
CC -!- SIMILARITY: Belongs to the SPARC family.
CC {ECO:0000256|ARBA:ARBA00006404}.
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DR RefSeq; XP_007528828.1; XM_007528766.2.
DR AlphaFoldDB; A0A1S3A3L5; -.
DR GeneID; 103118537; -.
DR CTD; 6678; -.
DR eggNOG; KOG4004; Eukaryota.
DR OrthoDB; 4695638at2759; -.
DR Proteomes; UP000079721; Unplaced.
DR GO; GO:0005604; C:basement membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005615; C:extracellular space; IEA:InterPro.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR CDD; cd16231; EFh_SPARC_like; 1.
DR CDD; cd01328; FSL_SPARC; 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; IPR019577; SPARC/Testican_Ca-bd-dom.
DR InterPro; IPR037641; SPARC_FS.
DR PANTHER; PTHR13866:SF6; SPARC; 1.
DR PANTHER; PTHR13866; SPARC OSTEONECTIN; 1.
DR Pfam; PF09289; FOLN; 1.
DR Pfam; PF00050; Kazal_1; 1.
DR Pfam; PF10591; SPARC_Ca_bdg; 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 Basement membrane {ECO:0000256|ARBA:ARBA00022869};
KW Calcium {ECO:0000256|ARBA:ARBA00022837};
KW Copper {ECO:0000256|ARBA:ARBA00023008};
KW Disulfide bond {ECO:0000256|PIRSR:PIRSR637641-50};
KW Extracellular matrix {ECO:0000256|ARBA:ARBA00022530};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000079721};
KW Secreted {ECO:0000256|ARBA:ARBA00022525};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..17
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 18..303
FT /note="SPARC"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5010277124"
FT DOMAIN 94..151
FT /note="Kazal-like"
FT /evidence="ECO:0000259|PROSITE:PS51465"
FT DISULFID 72..83
FT /evidence="ECO:0000256|PIRSR:PIRSR637641-50"
FT DISULFID 77..93
FT /evidence="ECO:0000256|PIRSR:PIRSR637641-50"
FT DISULFID 95..130
FT /evidence="ECO:0000256|PIRSR:PIRSR637641-50"
FT DISULFID 101..123
FT /evidence="ECO:0000256|PIRSR:PIRSR637641-50"
FT DISULFID 112..149
FT /evidence="ECO:0000256|PIRSR:PIRSR637641-50"
FT DISULFID 155..265
FT /evidence="ECO:0000256|PIRSR:PIRSR637641-50"
FT DISULFID 273..289
FT /evidence="ECO:0000256|PIRSR:PIRSR637641-50"
SQ SEQUENCE 303 AA; 34570 MW; E5877C38CC0CD015 CRC64;
MRTWIFFLLC LAGRAMAAPQ QEALPDETEV VEETVAEVAE VTVGANPVQV EVGEFEEGAE
EAEEEVVMEN PCQNHHCKHG KVCELDESNT PMCVCQDPTS CPAPVGDFEK VCSNDNKTFD
SSCHFFATKC TLEGTKKGHK LHLDYIGPCK YIAPCLDSEL TEFPLRMRDW LKNVLVTLYE
RDEGNNLLTE KQKLRVKKIH ENEKRLEAGD HPVELLARDF EKNYNMYIFP VHWQFGQLDQ
HPVDGYLSHT ELAPLRAPLI PMEHCTTRFF ETCDLDNDKY IALDEWAGCF GIKEQDIDKD
LVI
//
