ID A0A3B5B9D1_9TELE Unreviewed; 456 AA.
AC A0A3B5B9D1;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE SubName: Full=SPARC (osteonectin), cwcv and kazal like domains proteoglycan 1 {ECO:0000313|Ensembl:ENSSPAP00000022357.1};
GN Name=SPOCK1 {ECO:0000313|Ensembl:ENSSPAP00000022357.1};
OS Stegastes partitus (bicolor damselfish).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Pomacentridae; Stegastes.
OX NCBI_TaxID=144197 {ECO:0000313|Ensembl:ENSSPAP00000022357.1, ECO:0000313|Proteomes:UP000261400};
RN [1] {ECO:0000313|Ensembl:ENSSPAP00000022357.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC matrix {ECO:0000256|ARBA:ARBA00004498}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00500}.
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DR AlphaFoldDB; A0A3B5B9D1; -.
DR STRING; 144197.ENSSPAP00000022357; -.
DR Ensembl; ENSSPAT00000022712.1; ENSSPAP00000022357.1; ENSSPAG00000016889.1.
DR GeneTree; ENSGT00940000158371; -.
DR Proteomes; UP000261400; Unplaced.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR CDD; cd00104; KAZAL_FS; 1.
DR CDD; cd00191; TY; 1.
DR Gene3D; 3.30.60.30; -; 1.
DR Gene3D; 1.10.238.10; EF-hand; 1.
DR Gene3D; 4.10.800.10; Thyroglobulin type-1; 1.
DR InterPro; IPR011992; EF-hand-dom_pair.
DR InterPro; IPR002350; Kazal_dom.
DR InterPro; IPR036058; Kazal_dom_sf.
DR InterPro; IPR019577; SPARC/Testican_Ca-bd-dom.
DR InterPro; IPR000716; Thyroglobulin_1.
DR InterPro; IPR036857; Thyroglobulin_1_sf.
DR PANTHER; PTHR13866; SPARC OSTEONECTIN; 1.
DR PANTHER; PTHR13866:SF17; TESTICAN-1; 1.
DR Pfam; PF07648; Kazal_2; 1.
DR Pfam; PF10591; SPARC_Ca_bdg; 1.
DR Pfam; PF00086; Thyroglobulin_1; 1.
DR SMART; SM00280; KAZAL; 1.
DR SMART; SM00211; TY; 1.
DR SUPFAM; SSF47473; EF-hand; 1.
DR SUPFAM; SSF100895; Kazal-type serine protease inhibitors; 1.
DR SUPFAM; SSF57610; Thyroglobulin type-1 domain; 1.
DR PROSITE; PS51465; KAZAL_2; 1.
DR PROSITE; PS00484; THYROGLOBULIN_1_1; 1.
DR PROSITE; PS51162; THYROGLOBULIN_1_2; 1.
PE 4: Predicted;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW ProRule:PRU00500}; Extracellular matrix {ECO:0000256|ARBA:ARBA00022530};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00022974};
KW Heparan sulfate {ECO:0000256|ARBA:ARBA00023207};
KW Proteoglycan {ECO:0000256|ARBA:ARBA00022974};
KW Secreted {ECO:0000256|ARBA:ARBA00022525};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..21
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 22..456
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5017306929"
FT DOMAIN 142..193
FT /note="Kazal-like"
FT /evidence="ECO:0000259|PROSITE:PS51465"
FT DOMAIN 325..391
FT /note="Thyroglobulin type-1"
FT /evidence="ECO:0000259|PROSITE:PS51162"
FT REGION 60..91
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 384..456
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 439..456
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 363..370
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00500"
SQ SEQUENCE 456 AA; 50841 MW; CBE6E6534E885BBD CRC64;
MFFFLLPVVA LLLSGETLVS GNSNEKWLGT VAQYNKDRSW NRFRDDDYFK SWAPAKSLDQ
ERVAEPGRYG DPGTKSHAGS AKTTVQDGPD ATKDPCLKVR CPPHKVCVSH DYQTAICTNH
KQPAHSVKPR KGSAGHKHRL EAGAHGKCRL CSSLQSTPVC GSDGHTYSSK CKLEFQSCLS
GKTISVKCDG LCPCLPGQHL SKLPHHTEKA ACTDTELHSL AARLKDWFGV LHLDANRDLK
SSDSFDSAAG HFDTSILPIC KDSLGWMFNK LDMNFDLLLD QSELSAIYLD KYELCMKPLF
NSCDSFKDGK LSNNEWCYCF QKPEGLPCQT EKSRIQNQSR RKSLIGSYIP RCTDEGYFKP
TQCHGSTGQC WCVDKYGNEI AGSRKQGNPN CDEDQETSGD FGSGGAVILL DDQEEEPSQS
GRSRQKKRRG RIHPRGTIED DEDEDEDKDD EIGYVW
//
