ID A0A452H9N7_9SAUR Unreviewed; 297 AA.
AC A0A452H9N7;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 22.
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 Gopherus agassizii (Agassiz's desert tortoise).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Testudinata; Testudines; Cryptodira; Durocryptodira;
OC Testudinoidea; Testudinidae; Gopherus.
OX NCBI_TaxID=38772 {ECO:0000313|Ensembl:ENSGAGP00000011481.1, ECO:0000313|Proteomes:UP000291020};
RN [1] {ECO:0000313|Proteomes:UP000291020}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=28562605;
RA Tollis M., DeNardo D.F., Cornelius J.A., Dolby G.A., Edwards T.,
RA Henen B.T., Karl A.E., Murphy R.W., Kusumi K.;
RT "The Agassiz's desert tortoise genome provides a resource for the
RT conservation of a threatened species.";
RL PLoS ONE 12:e0177708-e0177708(2017).
RN [2] {ECO:0000313|Ensembl:ENSGAGP00000011481.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-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; A0A452H9N7; -.
DR STRING; 38772.ENSGAGP00000011481; -.
DR Ensembl; ENSGAGT00000013143.1; ENSGAGP00000011481.1; ENSGAGG00000008858.1.
DR Proteomes; UP000291020; Unassembled WGS sequence.
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:SF14; BM-40; 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:UP000291020};
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..297
FT /note="SPARC"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5019405645"
FT DOMAIN 88..145
FT /note="Kazal-like"
FT /evidence="ECO:0000259|PROSITE:PS51465"
FT DISULFID 66..77
FT /evidence="ECO:0000256|PIRSR:PIRSR637641-50"
FT DISULFID 71..87
FT /evidence="ECO:0000256|PIRSR:PIRSR637641-50"
FT DISULFID 89..124
FT /evidence="ECO:0000256|PIRSR:PIRSR637641-50"
FT DISULFID 95..117
FT /evidence="ECO:0000256|PIRSR:PIRSR637641-50"
FT DISULFID 106..143
FT /evidence="ECO:0000256|PIRSR:PIRSR637641-50"
FT DISULFID 149..259
FT /evidence="ECO:0000256|PIRSR:PIRSR637641-50"
FT DISULFID 267..283
FT /evidence="ECO:0000256|PIRSR:PIRSR637641-50"
SQ SEQUENCE 297 AA; 34084 MW; 659FCF4A98E3D945 CRC64;
MRAWIFFLIC LAGKALAAPE ALPDEIEVVE DPTTVEPVGV NPVQVEVGEF EEPTEDVEEI
VAENPCQNHH CKHGKICEVD DNNTPMCVCQ DPSTCPPSVG LFEKVCGTDN KTYESSCHFF
ATKCTLEGTK KGHKLHLDYI GPCKYIPPCL DTELIEFPLR MRDWLKNVLV TLYERDEDNN
LLTEKQKLKV KKIHENEKRL EAGEHTVELL ARDFEKNYNM YIFPVHWQFG QLDQHPIDGY
LSHTELAPLR APLIPMEHCT TRFFEECDLD NDKYIALEEW GSCFGIKEKD IDKDLVI
//
