ID A0A2D0RJY8_ICTPU Unreviewed; 291 AA.
AC A0A2D0RJY8;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 29.
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_017330240.1};
OS Ictalurus punctatus (Channel catfish) (Silurus punctatus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Siluriformes;
OC Ictaluridae; Ictalurus.
OX NCBI_TaxID=7998 {ECO:0000313|RefSeq:XP_017330240.1};
RN [1] {ECO:0000313|RefSeq:XP_017330240.1}
RP IDENTIFICATION.
RC TISSUE=Blood {ECO:0000313|RefSeq:XP_017330240.1};
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_017330240.1; XM_017474751.3.
DR AlphaFoldDB; A0A2D0RJY8; -.
DR STRING; 7998.ENSIPUP00000001609; -.
DR Ensembl; ENSIPUT00000001706; ENSIPUP00000001628; ENSIPUG00000001149.
DR GeneID; 108269144; -.
DR KEGG; ipu:108269144; -.
DR CTD; 6678; -.
DR OMA; IWKFCEL; -.
DR OrthoDB; 4695638at2759; -.
DR Proteomes; UP000221080; Chromosome 8.
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; cd16235; EFh_SPARC_SPARC; 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; SPARC OSTEONECTIN; 1.
DR PANTHER; PTHR13866:SF26; SPARC PRECURSOR; 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 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..291
FT /note="SPARC"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5012406753"
FT DOMAIN 82..139
FT /note="Kazal-like"
FT /evidence="ECO:0000259|PROSITE:PS51465"
FT DISULFID 60..71
FT /evidence="ECO:0000256|PIRSR:PIRSR637641-50"
FT DISULFID 65..81
FT /evidence="ECO:0000256|PIRSR:PIRSR637641-50"
FT DISULFID 83..118
FT /evidence="ECO:0000256|PIRSR:PIRSR637641-50"
FT DISULFID 89..111
FT /evidence="ECO:0000256|PIRSR:PIRSR637641-50"
FT DISULFID 100..137
FT /evidence="ECO:0000256|PIRSR:PIRSR637641-50"
FT DISULFID 143..253
FT /evidence="ECO:0000256|PIRSR:PIRSR637641-50"
FT DISULFID 261..277
FT /evidence="ECO:0000256|PIRSR:PIRSR637641-50"
SQ SEQUENCE 291 AA; 33147 MW; 4E6BD30BF30EC9DC CRC64;
MRVWIVFLLC LAGKALAAPA EEEPVIDEQV EVGSNPVQVE TGEFDEAIEV VEDVAAENPC
LNYHCKKGKV CELDDNNEPL CVCQDPLTCP APVGEFEHVC GTDNKTYDSS CHFFATKCAL
EGTKKGHKLH LDYIGPCKYI APCLENELGE FPLRMRDWLK NVMVTLYERD EDNNLLNEKQ
KLRVKKIFEN EKRLQAGDHS LDLLVLDFEK NYNMYVFPVH WQFGQLDQHP SDGFLSHTEL
APLRAPLIPM EHCTTSFFEA CDADQDKYIA LEEWANCFGI KEQDVDKDLI V
//
