GenomeNet

Database: UniProt
Entry: A0A3Q2DW03_CYPVA
LinkDB: A0A3Q2DW03_CYPVA
Original site: A0A3Q2DW03_CYPVA 
ID   A0A3Q2DW03_CYPVA        Unreviewed;       361 AA.
AC   A0A3Q2DW03;
DT   10-APR-2019, integrated into UniProtKB/TrEMBL.
DT   10-APR-2019, sequence version 1.
DT   27-MAR-2024, entry version 24.
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};
OS   Cyprinodon variegatus (Sheepshead minnow).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Ovalentaria; Atherinomorphae; Cyprinodontiformes; Cyprinodontidae;
OC   Cyprinodon.
OX   NCBI_TaxID=28743 {ECO:0000313|Ensembl:ENSCVAP00000023094.1, ECO:0000313|Proteomes:UP000265020};
RN   [1] {ECO:0000313|Ensembl:ENSCVAP00000023094.1}
RP   IDENTIFICATION.
RG   Ensembl;
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   AlphaFoldDB; A0A3Q2DW03; -.
DR   STRING; 28743.ENSCVAP00000023094; -.
DR   Ensembl; ENSCVAT00000007621.1; ENSCVAP00000023094.1; ENSCVAG00000006179.1.
DR   GeneTree; ENSGT00510000046787; -.
DR   OMA; CKGVRCG; -.
DR   Proteomes; UP000265020; 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; 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; PF07648; Kazal_2; 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:UP000265020};
KW   Secreted {ECO:0000256|ARBA:ARBA00022525};
KW   Signal {ECO:0000256|ARBA:ARBA00022729}.
FT   DOMAIN          152..209
FT                   /note="Kazal-like"
FT                   /evidence="ECO:0000259|PROSITE:PS51465"
FT   DISULFID        130..141
FT                   /evidence="ECO:0000256|PIRSR:PIRSR637641-50"
FT   DISULFID        135..151
FT                   /evidence="ECO:0000256|PIRSR:PIRSR637641-50"
FT   DISULFID        153..188
FT                   /evidence="ECO:0000256|PIRSR:PIRSR637641-50"
FT   DISULFID        159..181
FT                   /evidence="ECO:0000256|PIRSR:PIRSR637641-50"
FT   DISULFID        170..207
FT                   /evidence="ECO:0000256|PIRSR:PIRSR637641-50"
FT   DISULFID        213..323
FT                   /evidence="ECO:0000256|PIRSR:PIRSR637641-50"
FT   DISULFID        331..347
FT                   /evidence="ECO:0000256|PIRSR:PIRSR637641-50"
SQ   SEQUENCE   361 AA;  40536 MW;  3E534C6163EF94C8 CRC64;
     MQTGGDGRGL GDGGGKSHVH TGTSHWKCLL SKLVSQLDLP GAPHTADFSP HCPCSAKLKS
     LKMRVWIVFL LCLAGHAIAA PTEEEPLVEE LVTEEAVVEE PEVGANPVQV EVGEFDEAIE
     VDDVAAENPC LNYHCKKGKV CEVDESNTPL CVCQDPSTCP PAEGEFEHVC GTDNKTYDSS
     CHFFATKCTL EGTKKGHKLH LDYIGPCKYI EPCLDTELNE FPLRMRDWLK NVLVTLYERD
     EDNNLLTEKQ KLRVKKIYEN EKRLQAGDHS LDLLARDFKK NYNMFIFPVH WQFGQLDQHP
     VDGYLTHSEL APLRAPLIPM EHCTTRFFET CDADGDKYIA LEEWASCFGI KEQDVDKDLI
     I
//
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