ID K7FAA0_PELSI Unreviewed; 448 AA.
AC K7FAA0;
DT 09-JAN-2013, integrated into UniProtKB/TrEMBL.
DT 09-JAN-2013, sequence version 1.
DT 27-MAR-2024, entry version 62.
DE SubName: Full=SPARC (osteonectin), cwcv and kazal like domains proteoglycan 3 {ECO:0000313|Ensembl:ENSPSIP00000004960.1};
GN Name=SPOCK3 {ECO:0000313|Ensembl:ENSPSIP00000004960.1};
OS Pelodiscus sinensis (Chinese softshell turtle) (Trionyx sinensis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Testudinata; Testudines; Cryptodira; Trionychia;
OC Trionychidae; Pelodiscus.
OX NCBI_TaxID=13735 {ECO:0000313|Ensembl:ENSPSIP00000004960.1, ECO:0000313|Proteomes:UP000007267};
RN [1] {ECO:0000313|Proteomes:UP000007267}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Daiwa-1 {ECO:0000313|Proteomes:UP000007267};
RG Soft-shell Turtle Genome Consortium;
RL Submitted (OCT-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000007267}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Daiwa-1 {ECO:0000313|Proteomes:UP000007267};
RX PubMed=23624526; DOI=10.1038/ng.2615;
RA Wang Z., Pascual-Anaya J., Zadissa A., Li W., Niimura Y., Huang Z., Li C.,
RA White S., Xiong Z., Fang D., Wang B., Ming Y., Chen Y., Zheng Y.,
RA Kuraku S., Pignatelli M., Herrero J., Beal K., Nozawa M., Li Q., Wang J.,
RA Zhang H., Yu L., Shigenobu S., Wang J., Liu J., Flicek P., Searle S.,
RA Wang J., Kuratani S., Yin Y., Aken B., Zhang G., Irie N.;
RT "The draft genomes of soft-shell turtle and green sea turtle yield insights
RT into the development and evolution of the turtle-specific body plan.";
RL Nat. Genet. 45:701-706(2013).
RN [3] {ECO:0000313|Ensembl:ENSPSIP00000004960.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-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 EMBL; AGCU01010248; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AGCU01010249; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AGCU01010250; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AGCU01010251; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AGCU01010252; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AGCU01010253; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AGCU01010254; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AGCU01010255; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AGCU01010256; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AGCU01010257; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; K7FAA0; -.
DR Ensembl; ENSPSIT00000004988.1; ENSPSIP00000004960.1; ENSPSIG00000004633.1.
DR eggNOG; KOG3555; Eukaryota.
DR GeneTree; ENSGT00940000157828; -.
DR HOGENOM; CLU_037217_1_0_1; -.
DR OMA; PQTAVCI; -.
DR TreeFam; TF317779; -.
DR Proteomes; UP000007267; Unassembled WGS sequence.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0005539; F:glycosaminoglycan binding; IEA:Ensembl.
DR CDD; cd16239; EFh_SPARC_TICN3; 1.
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: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; 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 Reference proteome {ECO:0000313|Proteomes:UP000007267};
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..448
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003901483"
FT DOMAIN 132..185
FT /note="Kazal-like"
FT /evidence="ECO:0000259|PROSITE:PS51465"
FT DOMAIN 321..389
FT /note="Thyroglobulin type-1"
FT /evidence="ECO:0000259|PROSITE:PS51162"
FT REGION 402..448
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 407..448
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 361..368
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00500"
SQ SEQUENCE 448 AA; 50402 MW; AB9E8F8909194068 CRC64;
MLKVAAFMCV CAAAWYNPAL AAAAGGRSDS GNFLDDKQWL TTVSQYDKEV GQWNKFRDVQ
DDYFRTWSPG KPFDQGKALD PAKDPCLKMK CSRHKVCIAQ DQQTAVCISH RRLTHRYSMK
EAGLGHKQWR GGPISSNCKQ CPVVYTSPVC GSDGHTYSSQ VQCKLEYQAC VSGKQISVKC
EGRCPCPSDN PTSIGRNDQR GTVCSDLEFR EVANRLRDWF KALHESGIQN KKTRIVQRPE
RSSIGFDTSI LPICKDSLGW MFNRLDTNYD LLLDQSELGS IYLDNNEQCT KTFFNSCDTY
KDSLISNNEW CYCFQRQQGT DPPCQMELSN IHKQQGGKKL LGAGQYIPLC DEDGYYKPSQ
CHGSTGLCWC VDRYGNEVTG SRTNGAADCG KAIDLEISGD FASGDFHEWT DDEDDEDDIM
NDEDEIDDDE EEDEGDDDDD DDDHDGYI
//
