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Database: UniProt
Entry: W5M6Y0_LEPOC
LinkDB: W5M6Y0_LEPOC
Original site: W5M6Y0_LEPOC 
ID   W5M6Y0_LEPOC            Unreviewed;       418 AA.
AC   W5M6Y0;
DT   16-APR-2014, integrated into UniProtKB/TrEMBL.
DT   16-APR-2014, sequence version 1.
DT   27-MAR-2024, entry version 56.
DE   SubName: Full=SPARC (osteonectin), cwcv and kazal like domains proteoglycan 3 {ECO:0000313|Ensembl:ENSLOCP00000004138.1};
OS   Lepisosteus oculatus (Spotted gar).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Holostei; Semionotiformes; Lepisosteidae;
OC   Lepisosteus.
OX   NCBI_TaxID=7918 {ECO:0000313|Ensembl:ENSLOCP00000004138.1, ECO:0000313|Proteomes:UP000018468};
RN   [1] {ECO:0000313|Proteomes:UP000018468}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Di Palma F., Alfoldi J., Johnson J., Berlin A., Gnerre S., Jaffe D.,
RA   MacCallum I., Young S., Walker B.J., Lander E.S., Lindblad-Toh K.;
RT   "The Draft Genome of Lepisosteus oculatus.";
RL   Submitted (DEC-2011) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSLOCP00000004138.1}
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; AHAT01018539; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AHAT01018540; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   RefSeq; XP_015199814.1; XM_015344328.1.
DR   AlphaFoldDB; W5M6Y0; -.
DR   STRING; 7918.ENSLOCP00000004138; -.
DR   Ensembl; ENSLOCT00000004146.1; ENSLOCP00000004138.1; ENSLOCG00000003489.1.
DR   GeneID; 102685110; -.
DR   CTD; 50859; -.
DR   eggNOG; KOG3555; Eukaryota.
DR   GeneTree; ENSGT00940000157828; -.
DR   HOGENOM; CLU_037217_1_0_1; -.
DR   InParanoid; W5M6Y0; -.
DR   OMA; PQTAVCI; -.
DR   OrthoDB; 4174283at2759; -.
DR   Proteomes; UP000018468; Linkage group LG4.
DR   Bgee; ENSLOCG00000003489; Expressed in camera-type eye and 10 other cell types or tissues.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
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; 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   Reference proteome {ECO:0000313|Proteomes:UP000018468};
KW   Secreted {ECO:0000256|ARBA:ARBA00022525};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           23..418
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5004865642"
FT   DOMAIN          120..171
FT                   /note="Kazal-like"
FT                   /evidence="ECO:0000259|PROSITE:PS51465"
FT   DOMAIN          264..299
FT                   /note="EF-hand"
FT                   /evidence="ECO:0000259|PROSITE:PS50222"
FT   DOMAIN          298..364
FT                   /note="Thyroglobulin type-1"
FT                   /evidence="ECO:0000259|PROSITE:PS51162"
FT   REGION          396..418
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   DISULFID        336..343
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00500"
SQ   SEQUENCE   418 AA;  47038 MW;  22923CAAC425A6AB CRC64;
     MLSTALLCIC AVACSQVVGA AARSDTANFL DDKWLTGRWD KFRDEPGTWN PGKPFDQAST
     ILWSDVHILS HQALDPTRDP CLKVKCSRHK VCVAQDYQTA NCVSQRRMTH SMKEGVLTQK
     PGSSKCKQCS FVHPSPVCGT DGHTYSTKCK LEYQACISGK QISMKCPGYC PCLSNKSKNK
     VEKKTCSDME LREVVSRLRD WFKVLHENGS QNKKVKIQRP ERSRFDTSIL PICKDSLGWM
     FNRLDTNFDL LLDQSELASL YLDKNEHCTK SFFNSCDTYR DGLISNNEWC SCFQRQQDPP
     CQTELSSIQR QQAGKKFLGL YIPSCDEDGY YTSTQCHGSI GQCWCVDRYG NEIVGSRTHG
     PLDCGVDVDA SGDFGSGHFH ELSDDEDGEV DILNDEDEIV DDDEDEGDDE DDEEGYIS
//
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