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Database: UniProt
Entry: A0A2K6D867_MACNE
LinkDB: A0A2K6D867_MACNE
Original site: A0A2K6D867_MACNE 
ID   A0A2K6D867_MACNE        Unreviewed;       439 AA.
AC   A0A2K6D867;
DT   28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT   28-MAR-2018, sequence version 1.
DT   27-MAR-2024, entry version 32.
DE   SubName: Full=SPARC (osteonectin), cwcv and kazal like domains proteoglycan 1 {ECO:0000313|Ensembl:ENSMNEP00000032096.1};
GN   Name=SPOCK1 {ECO:0000313|Ensembl:ENSMNEP00000032096.1};
OS   Macaca nemestrina (Pig-tailed macaque).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Cercopithecinae; Macaca.
OX   NCBI_TaxID=9545 {ECO:0000313|Ensembl:ENSMNEP00000032096.1, ECO:0000313|Proteomes:UP000233120};
RN   [1] {ECO:0000313|Ensembl:ENSMNEP00000032096.1}
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   RefSeq; XP_011714785.1; XM_011716483.1.
DR   AlphaFoldDB; A0A2K6D867; -.
DR   STRING; 9545.ENSMNEP00000032096; -.
DR   Ensembl; ENSMNET00000056529.1; ENSMNEP00000032096.1; ENSMNEG00000039411.1.
DR   GeneID; 105467102; -.
DR   CTD; 6695; -.
DR   GeneTree; ENSGT00940000158371; -.
DR   OMA; GQESPKH; -.
DR   OrthoDB; 4174283at2759; -.
DR   Proteomes; UP000233120; Unplaced.
DR   Bgee; ENSMNEG00000039411; Expressed in cerebellum and 7 other cell types or tissues.
DR   GO; GO:0005615; C:extracellular space; IEA:Ensembl.
DR   GO; GO:0005509; F:calcium ion binding; IEA:Ensembl.
DR   GO; GO:0004869; F:cysteine-type endopeptidase inhibitor activity; IEA:Ensembl.
DR   GO; GO:0008191; F:metalloendopeptidase inhibitor activity; IEA:Ensembl.
DR   GO; GO:0010812; P:negative regulation of cell-substrate adhesion; IEA:Ensembl.
DR   GO; GO:0010977; P:negative regulation of neuron projection development; IEA:Ensembl.
DR   CDD; cd16237; EFh_SPARC_TICN1; 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: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   Reference proteome {ECO:0000313|Proteomes:UP000233120};
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..439
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5014336195"
FT   DOMAIN          130..181
FT                   /note="Kazal-like"
FT                   /evidence="ECO:0000259|PROSITE:PS51465"
FT   DOMAIN          310..376
FT                   /note="Thyroglobulin type-1"
FT                   /evidence="ECO:0000259|PROSITE:PS51162"
FT   REGION          397..439
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        397..421
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        422..439
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   DISULFID        348..355
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00500"
SQ   SEQUENCE   439 AA;  49155 MW;  D35171DCB8ACBC03 CRC64;
     MPAIAVLAAA AAAWCFLQVE SRHLDALAGG AGPNHGNFLD NDQWLSTVSQ YDRDKYWNRF
     RDDDYFRNWN PNKPFDQALD PSKDPCLKVK CSPHKVCVTQ DYQTALCVSR KHLLPRQKKG
     NVAHKHWVGP SNLVKCKPCP VAQSAMVCGS DGHSYTSKCK LEFHACSTGK SLTTLCDGPC
     PCLPEPEPPK HKAERSACTD KELRNLASRL KDWFGALHED ANRVIKPTSS NTAQGRFDTS
     ILPICKDSLG WMFNKLDMNY DLLLDHSEIN AIYLDKYEPC IKPLFNSCDS FKDGKLSNNE
     WCYCFQKPGG LPCQNEMNRI QKLSKGKSLL GAFIPRCNEE GYYKATQCHG STGQCWCVDK
     YGNELAGSRK QGAVSCEEEQ ETSGDFGSGG SVVLLDDLED ERELGPKDKE GKLRVHTRAV
     TEDDEDEDDD KEDEVGYIW
//
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