ID G1S2Z1_NOMLE Unreviewed; 417 AA.
AC G1S2Z1;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 28-FEB-2018, sequence version 2.
DT 27-MAR-2024, entry version 66.
DE SubName: Full=SPARC (osteonectin), cwcv and kazal like domains proteoglycan 2 {ECO:0000313|Ensembl:ENSNLEP00000019879.2};
GN Name=SPOCK2 {ECO:0000313|Ensembl:ENSNLEP00000019879.2};
OS Nomascus leucogenys (Northern white-cheeked gibbon) (Hylobates leucogenys).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hylobatidae;
OC Nomascus.
OX NCBI_TaxID=61853 {ECO:0000313|Ensembl:ENSNLEP00000019879.2, ECO:0000313|Proteomes:UP000001073};
RN [1] {ECO:0000313|Ensembl:ENSNLEP00000019879.2, ECO:0000313|Proteomes:UP000001073}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG Gibbon Genome Sequencing Consortium;
RL Submitted (OCT-2012) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSNLEP00000019879.2}
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; ADFV01064466; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; ADFV01064467; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; ADFV01064468; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; ADFV01064469; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; ADFV01064470; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; G1S2Z1; -.
DR STRING; 61853.ENSNLEP00000019879; -.
DR Ensembl; ENSNLET00000020877.2; ENSNLEP00000019879.2; ENSNLEG00000016379.2.
DR eggNOG; KOG3555; Eukaryota.
DR GeneTree; ENSGT00940000157107; -.
DR HOGENOM; CLU_037217_1_0_1; -.
DR InParanoid; G1S2Z1; -.
DR OMA; CDEVMGY; -.
DR TreeFam; TF317779; -.
DR Proteomes; UP000001073; Chromosome 18.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR GO; GO:0005509; F:calcium ion binding; IEA:Ensembl.
DR GO; GO:0050840; F:extracellular matrix binding; IEA:Ensembl.
DR GO; GO:0005539; F:glycosaminoglycan binding; IEA:Ensembl.
DR GO; GO:1990830; P:cellular response to leukemia inhibitory factor; IEA:Ensembl.
DR GO; GO:0030198; P:extracellular matrix organization; IEA:Ensembl.
DR GO; GO:0010811; P:positive regulation of cell-substrate adhesion; IEA:Ensembl.
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:SF18; TESTICAN-2; 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:UP000001073};
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..417
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5014147958"
FT DOMAIN 127..178
FT /note="Kazal-like"
FT /evidence="ECO:0000259|PROSITE:PS51465"
FT DOMAIN 303..369
FT /note="Thyroglobulin type-1"
FT /evidence="ECO:0000259|PROSITE:PS51162"
FT REGION 380..417
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 383..410
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 341..348
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00500"
SQ SEQUENCE 417 AA; 45591 MW; 171014127EF761B8 CRC64;
MRAPGCGRLV LPLLLLAAAA LAEGDAKGLK EGETPGNFME DEQWLSSISQ YSGKIKHWNR
FRDDDYIKSW EDNQQGDEAL DTTKDPCQKV KCSRHKVCIA QGYQRAMCIS RKKLEHRIKQ
PTVKLHGNKD SICKPCHMAQ LASVCGSDGH TYSSVCKLEQ QACLSSKQLA VRCEGPCPCP
TEQAATSTAD GKPETCTGQD LADLGDRLRD WFQLLHENSK QNGSASSVAS PASGLDKSLG
ASCKDSIGWM FSKLDTSADL FLDQTELAAI NLDKYEVCIR PFFNSCDTYK DGRVSTAASL
PAEPPCLAEL ERVQIQEAAK KKPGIFIPSC DEDGYYRKMQ CDQSSGDCWC VDQLGLELTG
TRTHGSPDCD DIVGFSGDFG SGVGWEDEEE KETEEAGEEA EEEEGEAGEA DDGGYIW
//
