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Database: UniProt
Entry: G3PLY6_GASAC
LinkDB: G3PLY6_GASAC
Original site: G3PLY6_GASAC 
ID   G3PLY6_GASAC            Unreviewed;      1522 AA.
AC   G3PLY6;
DT   16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT   16-NOV-2011, sequence version 1.
DT   24-JAN-2024, entry version 82.
DE   SubName: Full=Nidogen 2a (osteonidogen) {ECO:0000313|Ensembl:ENSGACP00000018617.1};
OS   Gasterosteus aculeatus (Three-spined stickleback).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Eupercaria; Perciformes; Cottioidei; Gasterosteales; Gasterosteidae;
OC   Gasterosteus.
OX   NCBI_TaxID=69293 {ECO:0000313|Ensembl:ENSGACP00000018617.1, ECO:0000313|Proteomes:UP000007635};
RN   [1] {ECO:0000313|Ensembl:ENSGACP00000018617.1, ECO:0000313|Proteomes:UP000007635}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Lindblad-Toh K., Mauceli E., Grabherr M., Chang J.L., Lander E.S.;
RL   Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSGACP00000018617.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (JUL-2023) to UniProtKB.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004370}.
CC       Secreted, extracellular space, extracellular matrix, basement membrane
CC       {ECO:0000256|ARBA:ARBA00004302}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00076}.
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DR   STRING; 69293.ENSGACP00000018617; -.
DR   Ensembl; ENSGACT00000018653.1; ENSGACP00000018617.1; ENSGACG00000014091.1.
DR   eggNOG; KOG1214; Eukaryota.
DR   GeneTree; ENSGT00940000157901; -.
DR   InParanoid; G3PLY6; -.
DR   OMA; TCEHNHG; -.
DR   TreeFam; TF320666; -.
DR   Proteomes; UP000007635; Unassembled WGS sequence.
DR   Bgee; ENSGACG00000014091; Expressed in embryo and 6 other cell types or tissues.
DR   GO; GO:0005604; C:basement membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   GO; GO:0048513; P:animal organ development; IEA:UniProt.
DR   GO; GO:0007160; P:cell-matrix adhesion; IEA:InterPro.
DR   CDD; cd00054; EGF_CA; 3.
DR   CDD; cd00255; nidG2; 1.
DR   CDD; cd00191; TY; 4.
DR   Gene3D; 2.40.155.10; Green fluorescent protein; 1.
DR   Gene3D; 2.10.25.10; Laminin; 3.
DR   Gene3D; 4.10.800.10; Thyroglobulin type-1; 4.
DR   Gene3D; 2.120.10.30; TolB, C-terminal domain; 1.
DR   InterPro; IPR011042; 6-blade_b-propeller_TolB-like.
DR   InterPro; IPR001881; EGF-like_Ca-bd_dom.
DR   InterPro; IPR000742; EGF-like_dom.
DR   InterPro; IPR000152; EGF-type_Asp/Asn_hydroxyl_site.
DR   InterPro; IPR018097; EGF_Ca-bd_CS.
DR   InterPro; IPR024731; EGF_dom.
DR   InterPro; IPR006605; G2_nidogen/fibulin_G2F.
DR   InterPro; IPR009017; GFP.
DR   InterPro; IPR009030; Growth_fac_rcpt_cys_sf.
DR   InterPro; IPR000033; LDLR_classB_rpt.
DR   InterPro; IPR003886; NIDO_dom.
DR   InterPro; IPR000716; Thyroglobulin_1.
DR   InterPro; IPR036857; Thyroglobulin_1_sf.
DR   PANTHER; PTHR12352:SF3; NIDOGEN-2; 1.
DR   PANTHER; PTHR12352; SECRETED MODULAR CALCIUM-BINDING PROTEIN; 1.
DR   Pfam; PF12947; EGF_3; 1.
DR   Pfam; PF07645; EGF_CA; 1.
DR   Pfam; PF07474; G2F; 1.
DR   Pfam; PF00058; Ldl_recept_b; 3.
DR   Pfam; PF06119; NIDO; 1.
DR   Pfam; PF00086; Thyroglobulin_1; 4.
DR   SMART; SM00181; EGF; 4.
DR   SMART; SM00179; EGF_CA; 3.
DR   SMART; SM00682; G2F; 1.
DR   SMART; SM00135; LY; 4.
DR   SMART; SM00539; NIDO; 1.
DR   SMART; SM00211; TY; 4.
DR   SUPFAM; SSF57196; EGF/Laminin; 1.
DR   SUPFAM; SSF54511; GFP-like; 1.
DR   SUPFAM; SSF57184; Growth factor receptor domain; 1.
DR   SUPFAM; SSF57610; Thyroglobulin type-1 domain; 4.
DR   SUPFAM; SSF63825; YWTD domain; 1.
DR   PROSITE; PS00010; ASX_HYDROXYL; 2.
DR   PROSITE; PS01186; EGF_2; 4.
DR   PROSITE; PS50026; EGF_3; 3.
DR   PROSITE; PS01187; EGF_CA; 1.
DR   PROSITE; PS51120; LDLRB; 3.
DR   PROSITE; PS51220; NIDO; 1.
DR   PROSITE; PS50993; NIDOGEN_G2; 1.
DR   PROSITE; PS00484; THYROGLOBULIN_1_1; 4.
DR   PROSITE; PS51162; THYROGLOBULIN_1_2; 4.
PE   4: Predicted;
KW   Basement membrane {ECO:0000256|ARBA:ARBA00022869};
KW   Cell adhesion {ECO:0000256|ARBA:ARBA00022889};
KW   Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW   ProRule:PRU00500};
KW   EGF-like domain {ECO:0000256|ARBA:ARBA00022536, ECO:0000256|PROSITE-
KW   ProRule:PRU00076}; Extracellular matrix {ECO:0000256|ARBA:ARBA00022869};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007635};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Secreted {ECO:0000256|ARBA:ARBA00022525}; Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           22..1522
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5003449809"
FT   DOMAIN          99..266
FT                   /note="NIDO"
FT                   /evidence="ECO:0000259|PROSITE:PS51220"
FT   DOMAIN          506..736
FT                   /note="Nidogen G2 beta-barrel"
FT                   /evidence="ECO:0000259|PROSITE:PS50993"
FT   DOMAIN          738..779
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50026"
FT   DOMAIN          780..822
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50026"
FT   DOMAIN          871..909
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50026"
FT   DOMAIN          919..989
FT                   /note="Thyroglobulin type-1"
FT                   /evidence="ECO:0000259|PROSITE:PS51162"
FT   DOMAIN          999..1069
FT                   /note="Thyroglobulin type-1"
FT                   /evidence="ECO:0000259|PROSITE:PS51162"
FT   DOMAIN          1079..1149
FT                   /note="Thyroglobulin type-1"
FT                   /evidence="ECO:0000259|PROSITE:PS51162"
FT   DOMAIN          1162..1230
FT                   /note="Thyroglobulin type-1"
FT                   /evidence="ECO:0000259|PROSITE:PS51162"
FT   REPEAT          1301..1344
FT                   /note="LDL-receptor class B"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT   REPEAT          1345..1387
FT                   /note="LDL-receptor class B"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT   REPEAT          1388..1432
FT                   /note="LDL-receptor class B"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT   REGION          301..400
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          975..1017
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1053..1097
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1136..1156
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        301..324
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        333..352
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        986..1011
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1069..1091
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   DISULFID        958..965
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00500"
FT   DISULFID        1038..1045
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00500"
FT   DISULFID        1118..1125
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00500"
FT   DISULFID        1200..1207
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00500"
SQ   SEQUENCE   1522 AA;  167056 MW;  93806EE2979D4A1C CRC64;
     RLGMLAACLL CWSCGVCLVS AIRRTDMYPY GPQSGDQVLA EGDDETSRVL PLSRPLTFYR
     TRFSQLYVAT NGIISAQDLP MEKQYVDDGF PTDFPAVAPF LADIDTSGGR GQIYYRVTET
     PGVLNRVAQE VHQGFPDAKF TPTVAVVATW ENVAAYEEQT RTTGPSSKVN TFQAVIGYDE
     TDSYVIFLYP EGGLNFFGTR PKESYNVEIE LPARVGFSRG EIPYLIFSRI EGPHYSVTSN
     EQSVKNLYQV GNTGIPGVWL FHTGNSYYFD NIVPASFSGL LDTPPAGGLS LDTTTAEYEE
     IEDNPDNTFG TDNQEEEDDY LLTDGDPEFQ TGPTGDHSAS PDAPSSPSEE PSRQAVYDIG
     NVPLTSEPKY NSEPGERQYA PPNSPERAPV GGAQQQPQVT QNQLCIEMTY RVSPANPSDL
     HFKNERRFSP GGHVGQRGRG MMWIFDTGRD EIMIQYTTEN KETCASSRFQ QECSQNAFCS
     DYATGFCCHC RPGFYGNGRH CLPEGAPQRV SGKVNGTVTV GSTPVELNNI DLHAYIVVGD
     GRAYTAISEV PEPVGWALMP LAPIGELFGW LFALELPNSQ AGFKITGAEF TRHAEAIFYP
     GNQRLSIVQT GHGIDNHNHL NVDTVVSGSV PFLPSGSEVT MDPFKEIYQY YPSVATSYSV
     REFSVVSAER GSESFSFQLK QNITYRDCRH DNRAGVPETL QITMERVFVM YVKEERILRY
     AITNKISPVG AEPTEPELVN PCYAGNHDCD TTAQCLPQQG QDFLCQCATG YRGDGRNCYD
     VDECAEGSSS CGAHAQCVNL PGSHSCQCQG GFEFGFDRRS CVGIHIFVPA QAQHDQQRTA
     AKAREHSGGA GRWATNGRAG VGMRGLMFSL DIDECSSSPC HISARCINAL GSFQCQCEPG
     FYGDGFHCSQ QEDEPERPKT HCEHHRDSVQ TTSSEGYPIV GAYVPQCDHN GRYIPSQCHG
     STGHCWCVDV RGQEKAGTRT PPGTPPKDCD RSDEPERPKT HCEHHRDRVQ TSSPEGYPVV
     GAYVPQCDAG GQYTPLQCHG STGHCWCVDS RGQERTGTRT PPGAPPTDCD KPDEPERPKT
     HCEHHRDRVQ TTSPEGYPIV GAYVPQCDDN GRYASLQCHG STGHCWCVDS TGQERAGTRT
     PPGSPPKDCD RPVPVAPTEH PESVCERWRA SLIEHYGGKP QPEQYVPQCE QDGQFSPVQC
     YGETTYCWCV DQDGREVPGT RSYDIVKPAC LPSAAPPTVR PLPRPDVTPP PNADITLLYA
     QGQKIGALPL NGTRLDAARS KTLLTLHGSI VVGIAHDCKE NHVYWTDLSA RTINRASMAA
     GAEPEILINT NLVSPEGLAV DAKRRLMFWV DSNPDVIESA NLDGSGRRTL FSTDLVNPRA
     IIVVSSTGTL YWTDWNREAP KIESASVDGQ NRRVVVTDGV GLPNALTYDS SSGQVCWADA
     GTKRLECVSP DGSGRRVVHP SLNYPFSMVY YGNHFYYTDW RRDGVIAVSK ESSQITDEYL
     PDQRSHLYGI AIATTHCLSG NL
//
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