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Database: UniProt
Entry: A0A2K5KT36_CERAT
LinkDB: A0A2K5KT36_CERAT
Original site: A0A2K5KT36_CERAT 
ID   A0A2K5KT36_CERAT        Unreviewed;       424 AA.
AC   A0A2K5KT36;
DT   28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT   28-MAR-2018, sequence version 1.
DT   27-MAR-2024, entry version 34.
DE   SubName: Full=SPARC (osteonectin), cwcv and kazal like domains proteoglycan 2 {ECO:0000313|Ensembl:ENSCATP00000003862.1};
GN   Name=SPOCK2 {ECO:0000313|Ensembl:ENSCATP00000003862.1};
OS   Cercocebus atys (Sooty mangabey) (Cercocebus torquatus atys).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Cercopithecinae; Cercocebus.
OX   NCBI_TaxID=9531 {ECO:0000313|Ensembl:ENSCATP00000003862.1, ECO:0000313|Proteomes:UP000233060};
RN   [1] {ECO:0000313|Ensembl:ENSCATP00000003862.1}
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_011940772.1; XM_012085382.1.
DR   AlphaFoldDB; A0A2K5KT36; -.
DR   STRING; 9531.ENSCATP00000003862; -.
DR   Ensembl; ENSCATT00000016393.1; ENSCATP00000003862.1; ENSCATG00000014283.1.
DR   GeneID; 105597299; -.
DR   KEGG; caty:105597299; -.
DR   CTD; 9806; -.
DR   GeneTree; ENSGT00940000157107; -.
DR   OMA; CDEVMGY; -.
DR   OrthoDB; 4174283at2759; -.
DR   Proteomes; UP000233060; Unplaced.
DR   Bgee; ENSCATG00000014283; Expressed in cerebellum and 12 other cell types or tissues.
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:UP000233060};
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..424
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5014320762"
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          387..424
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        390..417
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   DISULFID        348..355
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00500"
SQ   SEQUENCE   424 AA;  46824 MW;  F3E5493835472AEA CRC64;
     MRAPGCGRLV LPLLLLTAAA LAEGDAKGLK EGETPGNFME DEQWLSSISQ YSGKIKHWNR
     FRDEVEDDYI KSWEDNQQGD EALDTTKDPC QKVKCSRHKV CIAQGYQRAM CISRKKLEHR
     IKQPTVKLHG NKDSICKPCH MAQLASVCGS DGHTYSSVCK LEQQACLSNK QLAVRCEGPC
     PCPTEQAATS TADGKPETCT GQDLADLGDR LRDWFQLLHE NSKQNGSASS AASPASGLDK
     SLGASCKDSI GWMFSKLDTS ADLFLDQTEL AAINLDKYEV CIRPFFNSCD TYKDGRVSTA
     EWCFCFWREK PPCLAELERV QIQEAAKKKP GIFIPSCDED GYYRKMQCDQ SSGDCWCVDQ
     LGLELTGTRT HGSPDCDDIV GFSGDFGSGV GWEDEEEKET EEAGEEAEEE EGEAGEADDG
     GYIW
//
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