ID A0A2K6TGD6_SAIBB Unreviewed; 457 AA.
AC A0A2K6TGD6;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE SubName: Full=SPARC related modular calcium binding 2 {ECO:0000313|Ensembl:ENSSBOP00000018709.1};
GN Name=SMOC2 {ECO:0000313|Ensembl:ENSSBOP00000018709.1};
OS Saimiri boliviensis boliviensis (Bolivian squirrel monkey).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Platyrrhini; Cebidae;
OC Saimiriinae; Saimiri.
OX NCBI_TaxID=39432 {ECO:0000313|Ensembl:ENSSBOP00000018709.1, ECO:0000313|Proteomes:UP000233220};
RN [1] {ECO:0000313|Ensembl:ENSSBOP00000018709.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
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_010329609.1; XM_010331307.1.
DR AlphaFoldDB; A0A2K6TGD6; -.
DR STRING; 39432.ENSSBOP00000018709; -.
DR Ensembl; ENSSBOT00000035525.1; ENSSBOP00000018709.1; ENSSBOG00000025977.1.
DR GeneID; 101044259; -.
DR CTD; 64094; -.
DR GeneTree; ENSGT00390000018436; -.
DR OMA; MSRCVAE; -.
DR OrthoDB; 5388426at2759; -.
DR Proteomes; UP000233220; Unplaced.
DR GO; GO:0062023; C:collagen-containing extracellular matrix; IEA:InterPro.
DR GO; GO:0005615; C:extracellular space; IEA:Ensembl.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:2000573; P:positive regulation of DNA biosynthetic process; IEA:Ensembl.
DR GO; GO:2001028; P:positive regulation of endothelial cell chemotaxis; IEA:Ensembl.
DR GO; GO:0045743; P:positive regulation of fibroblast growth factor receptor signaling pathway; IEA:Ensembl.
DR GO; GO:0045931; P:positive regulation of mitotic cell cycle; IEA:Ensembl.
DR GO; GO:1900748; P:positive regulation of vascular endothelial growth factor signaling pathway; IEA:Ensembl.
DR GO; GO:0035470; P:positive regulation of vascular wound healing; IEA:Ensembl.
DR CDD; cd16241; EFh_SPARC_SMOC2; 1.
DR CDD; cd00104; KAZAL_FS; 1.
DR CDD; cd00191; TY; 2.
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; 2.
DR InterPro; IPR011992; EF-hand-dom_pair.
DR InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR InterPro; IPR002048; EF_hand_dom.
DR InterPro; IPR002350; Kazal_dom.
DR InterPro; IPR036058; Kazal_dom_sf.
DR InterPro; IPR037640; SMOC2_EC.
DR InterPro; IPR019577; SPARC/Testican_Ca-bd-dom.
DR InterPro; IPR000716; Thyroglobulin_1.
DR InterPro; IPR036857; Thyroglobulin_1_sf.
DR PANTHER; PTHR12352; SECRETED MODULAR CALCIUM-BINDING PROTEIN; 1.
DR PANTHER; PTHR12352:SF21; SPARC-RELATED MODULAR CALCIUM-BINDING PROTEIN 2; 1.
DR Pfam; PF07648; Kazal_2; 1.
DR Pfam; PF10591; SPARC_Ca_bdg; 1.
DR Pfam; PF16597; Thyroglob_assoc; 1.
DR Pfam; PF00086; Thyroglobulin_1; 2.
DR SMART; SM00280; KAZAL; 1.
DR SMART; SM00211; TY; 2.
DR SUPFAM; SSF47473; EF-hand; 1.
DR SUPFAM; SSF100895; Kazal-type serine protease inhibitors; 1.
DR SUPFAM; SSF57610; Thyroglobulin type-1 domain; 2.
DR PROSITE; PS00018; EF_HAND_1; 2.
DR PROSITE; PS50222; EF_HAND_2; 2.
DR PROSITE; PS51465; KAZAL_2; 1.
DR PROSITE; PS00484; THYROGLOBULIN_1_1; 2.
DR PROSITE; PS51162; THYROGLOBULIN_1_2; 2.
PE 4: Predicted;
KW Calcium {ECO:0000256|ARBA:ARBA00022837};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW ProRule:PRU00500}; Extracellular matrix {ECO:0000256|ARBA:ARBA00022530};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000233220};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
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..457
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5014473058"
FT DOMAIN 34..86
FT /note="Kazal-like"
FT /evidence="ECO:0000259|PROSITE:PS51465"
FT DOMAIN 87..153
FT /note="Thyroglobulin type-1"
FT /evidence="ECO:0000259|PROSITE:PS51162"
FT DOMAIN 224..292
FT /note="Thyroglobulin type-1"
FT /evidence="ECO:0000259|PROSITE:PS51162"
FT DOMAIN 358..393
FT /note="EF-hand"
FT /evidence="ECO:0000259|PROSITE:PS50222"
FT DOMAIN 395..430
FT /note="EF-hand"
FT /evidence="ECO:0000259|PROSITE:PS50222"
FT REGION 147..167
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 208..241
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 426..457
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 208..231
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 429..444
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 124..131
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00500"
FT DISULFID 133..153
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00500"
FT DISULFID 262..269
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00500"
SQ SEQUENCE 457 AA; 50934 MW; 5FA22EA02742E58D CRC64;
MLLPQLCWLP LLAGLLPPAP AQKFSALTFL RVDQDKDKDC SLDCAGSPQK PLCASDGRTF
LSRCEFQRAK CKDPQLEIAY RGNCKDVSRC VAERKYTQEQ ARKEFQQVFI PECNGDGTYS
QVQCHSYTGY CWCVTPNGRP ISGTAVAHKT PRCPGSTNEK LPQREGTGKT VSLQIFSVLN
SDDASAPALE TQPQGDEEDI ASRYPTLWTE QVKSRQNKTN KNSASSCDQE HQSALEEAKQ
PKNDDVVIPE CAHGGLYKPV QCHPSTGYCW CVLVDTGRPI PGTSTRYEQP KCDNTARAHP
AKARDLYRGR QLQGCPGAKK HEFLTSVLDA LSTDMVHAVS DPSSSSARLS EPDPSHTLEE
RVVRWYFKLL DKNSSGDIGK KEMKPFKRFL RKKSKPKKCV KKFVEYCDVN NDKSISVQEL
MGCLGVAKED SKADTRKRHT PRGNAESSPN RQPRRQG
//
