ID A0A3B4H4S9_9CICH Unreviewed; 417 AA.
AC A0A3B4H4S9;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE SubName: Full=SPARC (osteonectin), cwcv and kazal like domains proteoglycan 2 {ECO:0000313|Ensembl:ENSPNYP00000028416.1};
GN Name=SPOCK2 {ECO:0000313|Ensembl:ENSPNYP00000028416.1};
OS Pundamilia nyererei.
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Cichlomorphae; Cichliformes; Cichlidae; African cichlids;
OC Pseudocrenilabrinae; Haplochromini; Pundamilia.
OX NCBI_TaxID=303518 {ECO:0000313|Ensembl:ENSPNYP00000028416.1, ECO:0000313|Proteomes:UP000261460};
RN [1] {ECO:0000313|Ensembl:ENSPNYP00000028416.1}
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 AlphaFoldDB; A0A3B4H4S9; -.
DR STRING; 303518.ENSPNYP00000028416; -.
DR Ensembl; ENSPNYT00000029108.1; ENSPNYP00000028416.1; ENSPNYG00000021382.1.
DR GeneTree; ENSGT00940000157107; -.
DR Proteomes; UP000261460; Unplaced.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR CDD; cd16238; EFh_SPARC_TICN2; 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: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 Secreted {ECO:0000256|ARBA:ARBA00022525};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..417
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5017285910"
FT DOMAIN 123..174
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..417
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; 46215 MW; 6BBD068F7B573AB5 CRC64;
MVAVRVIACL CLLVGVSLQV DVKSGKEAGK AGNFMEDEQW LSTISQYSRK IKHWNRFRDV
SDDYIKNMEE NVGSDETLDT TKDPCQNVKC SRHKVCIAQG YQRAMCVNRK KLEHRGKQSG
QMEVHEGSCK PCPVAASSPV CGSDGHNYAS ECKLEQQACL TGKDLSVMCS GFCPCSTASV
SITNADTKHE SCTGQDLADL GDRLRDWFQL LHGNAKQNNS GKPGAGTASA LDKSLVASCK
DSIGWMFSKL DTNNDLYLDH AELAAINLDK YEVCIRPFFN SCDSYKDGKV STAEWCLCFW
REKPPCLAEL ERIQVQEAAK KKPGMYIPSC DEDGYYRKVQ CDQSRGECWC ADQHGGEMMG
TRIHGNPNCD EVMGYSGDFG SGVGWEDEEE KEAEDNGEEA EEEEEEEGEA DDGGYIW
//
