ID A0A3B3QG67_9TELE Unreviewed; 420 AA.
AC A0A3B3QG67;
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 3 {ECO:0000313|Ensembl:ENSPKIP00000004585.1};
OS Paramormyrops kingsleyae.
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Osteoglossocephala;
OC Osteoglossomorpha; Osteoglossiformes; Mormyridae; Paramormyrops.
OX NCBI_TaxID=1676925 {ECO:0000313|Ensembl:ENSPKIP00000004585.1, ECO:0000313|Proteomes:UP000261540};
RN [1] {ECO:0000313|Ensembl:ENSPKIP00000004585.1}
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; A0A3B3QG67; -.
DR STRING; 1676925.ENSPKIP00000004585; -.
DR Ensembl; ENSPKIT00000028569.1; ENSPKIP00000004585.1; ENSPKIG00000021579.1.
DR GeneTree; ENSGT00940000157828; -.
DR Proteomes; UP000261540; 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; IPR002048; EF_hand_dom.
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:SF21; TESTICAN-3; 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; PS50222; EF_HAND_2; 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..18
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 19..420
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5017256188"
FT DOMAIN 122..173
FT /note="Kazal-like"
FT /evidence="ECO:0000259|PROSITE:PS51465"
FT DOMAIN 266..301
FT /note="EF-hand"
FT /evidence="ECO:0000259|PROSITE:PS50222"
FT DOMAIN 300..366
FT /note="Thyroglobulin type-1"
FT /evidence="ECO:0000259|PROSITE:PS51162"
FT REGION 368..420
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 380..398
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 399..420
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 338..345
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00500"
SQ SEQUENCE 420 AA; 47005 MW; E1A84726BB8A55AB CRC64;
LVRDTAFLCL SVLQMLNAAL LSVCAVVASQ LLGVACRSDG GNFLDDKWLT GRWDKFRDEP
GTWNPGKPFD QALDPAKDPC QKVKCGRHKV CVAQDYQTAS CISQRQMRKS ESGFKDVGLS
QNPLFSKCKQ CPVVHPSPVC GADGHTYSTK CKLEYQACIS GKQISVKCTG QCPCQTNKSK
TRAEKKVCSE VELKEAVSRL RDWFKVLHEN GNQNRKVQVQ RLERSRFDTS ILPICKDSLG
WMFSRLDTNY DLLLDQSELS SLYLDKNEHC IKSFFISCDT YGDGLISNNE WCSCFQRHEE
PPCQSELSSI TTQQAGKKLL GLYIPSCDED GYFKPHQCHG SSGQCWCVDR YGNELARSRT
ARPADCGVEL ESSGDLGSGD LREFSDDEDD KGRVLNDEDE MVDDDEDEGD DEVDDEGYVS
//