ID G3SRU1_LOXAF Unreviewed; 1408 AA.
AC G3SRU1;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 24-JAN-2024, entry version 79.
DE SubName: Full=Nidogen 2 {ECO:0000313|Ensembl:ENSLAFP00000002630.3};
GN Name=NID2 {ECO:0000313|Ensembl:ENSLAFP00000002630.3};
OS Loxodonta africana (African elephant).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Afrotheria; Proboscidea; Elephantidae; Loxodonta.
OX NCBI_TaxID=9785 {ECO:0000313|Ensembl:ENSLAFP00000002630.3, ECO:0000313|Proteomes:UP000007646};
RN [1] {ECO:0000313|Ensembl:ENSLAFP00000002630.3, ECO:0000313|Proteomes:UP000007646}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Isolate ISIS603380 {ECO:0000313|Ensembl:ENSLAFP00000002630.3,
RC ECO:0000313|Proteomes:UP000007646};
RA Di Palma F., Heiman D., Young S., Johnson J., Lander E.S., Lindblad-Toh K.;
RT "The Genome Sequence of Loxodonta africana (African elephant).";
RL Submitted (JUN-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSLAFP00000002630.3}
RP IDENTIFICATION.
RC STRAIN=Isolate ISIS603380 {ECO:0000313|Ensembl:ENSLAFP00000002630.3};
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; 9785.ENSLAFP00000002630; -.
DR Ensembl; ENSLAFT00000003167.3; ENSLAFP00000002630.3; ENSLAFG00000003163.3.
DR eggNOG; KOG1214; Eukaryota.
DR GeneTree; ENSGT00940000157901; -.
DR HOGENOM; CLU_003163_1_0_1; -.
DR InParanoid; G3SRU1; -.
DR OMA; TCEHNHG; -.
DR TreeFam; TF320666; -.
DR Proteomes; UP000007646; Unassembled WGS sequence.
DR GO; GO:0005604; C:basement membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:Ensembl.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
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; 2.
DR Gene3D; 2.40.155.10; Green fluorescent protein; 1.
DR Gene3D; 2.10.25.10; Laminin; 4.
DR Gene3D; 4.10.800.10; Thyroglobulin type-1; 2.
DR Gene3D; 2.120.10.30; TolB, C-terminal domain; 1.
DR InterPro; IPR011042; 6-blade_b-propeller_TolB-like.
DR InterPro; IPR026823; cEGF.
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; PF12662; cEGF; 1.
DR Pfam; PF12947; EGF_3; 1.
DR Pfam; PF07645; EGF_CA; 1.
DR Pfam; PF07474; G2F; 1.
DR Pfam; PF00058; Ldl_recept_b; 2.
DR Pfam; PF06119; NIDO; 1.
DR Pfam; PF00086; Thyroglobulin_1; 2.
DR SMART; SM00181; EGF; 5.
DR SMART; SM00179; EGF_CA; 4.
DR SMART; SM00682; G2F; 1.
DR SMART; SM00135; LY; 4.
DR SMART; SM00539; NIDO; 1.
DR SMART; SM00211; TY; 2.
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; 2.
DR SUPFAM; SSF63825; YWTD domain; 1.
DR PROSITE; PS00010; ASX_HYDROXYL; 2.
DR PROSITE; PS01186; EGF_2; 3.
DR PROSITE; PS50026; EGF_3; 4.
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; 2.
DR PROSITE; PS51162; THYROGLOBULIN_1_2; 2.
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:UP000007646};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Secreted {ECO:0000256|ARBA:ARBA00022525}.
FT DOMAIN 111..277
FT /note="NIDO"
FT /evidence="ECO:0000259|PROSITE:PS51220"
FT DOMAIN 555..785
FT /note="Nidogen G2 beta-barrel"
FT /evidence="ECO:0000259|PROSITE:PS50993"
FT DOMAIN 786..827
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 828..870
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 875..918
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 919..955
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 969..1037
FT /note="Thyroglobulin type-1"
FT /evidence="ECO:0000259|PROSITE:PS51162"
FT DOMAIN 1049..1117
FT /note="Thyroglobulin type-1"
FT /evidence="ECO:0000259|PROSITE:PS51162"
FT REPEAT 1187..1230
FT /note="LDL-receptor class B"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT REPEAT 1231..1273
FT /note="LDL-receptor class B"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT REPEAT 1274..1318
FT /note="LDL-receptor class B"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT REGION 1..65
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 325..467
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1025..1047
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 1006..1013
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00500"
FT DISULFID 1087..1094
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00500"
SQ SEQUENCE 1408 AA; 154204 MW; BFA191E9A4F67A9E CRC64;
AGAQPLVGWL AGPGTRSATG QHTGRSRVAA LPPRRGLPLT GRRGGDRSLA GRRMPRPSSG
EAGNPPLHFY ESQVQGPSYV GTNGIISTQD FPRETQYVDD DFPTDFPAIA PFLADIDTSQ
GRGRILYRED TSPAVLGLAA RYVRAGFPRS ITRFAPTHAF LATWEQVGAY EEVTRGAPPS
GELNTFQAVL VSDESDTYAL FLYPANGLQF FGTRPKESYN VQLELPARVG FCRGEADDLK
REGPYFSLTS TEQSVKNLYQ LSNLGISGVW AFHIGSTSPL DNVRPATLGG DLSKAHSLAS
LEHSFSHTAA LESDYTEDNL DYYDENEEEA EYPPSEPEEA GNGHGSVDVS FPVKVDSRPS
GGDVSPPNSD LAALLPHPTP SDWPFYPETE SATWDPQTKE GKIGTPGLNG RVEASEQIET
RSSAPPETDR DSLDPPQKAL PYAENEHLQP YPDGGVVPSE TDVPAARPGE VVPPHYPLPD
HTAPRSSRRF VVGVEDNISS NTEVFTYNAA NKETCEQNHR QCSQHAFCTD YTTGFCCHCQ
TRFYGNGKYC LPEGAPQRVN GKVSGHLRVG HTPVHFTDVD LHAYIVGNDG RAYTAISHIP
QPAAQALLPL TPIGGLFGWL FALEKPGSEN GFSITGATFT HDMEVTFYPG EEKVHITQTA
EGLDPENYLS VKTNIQGQVP YIPANFTAHI APYKELYHYS DSVVTSTSSR DYSLTFGAIN
QTLSYRIHQN ITYQTCRHAP RHQAIPTTQQ LNVDRAFALY NDEERVLRFA VTNQVGHVEV
DSDPAPVNPC YDGSHTCDTT AQCHPGTGLA YTCECAPGYQ GDGRNCVDVN ECATGVHHCG
PNSVCINLKG SYKCECRSGY EFADDRHTCI VIAPPPNPCE DGSHTCAPAG QARCIHHGGS
TFTCACLPGY VGTGHQCTDV DECLENRCHP AATCYNTPGS FSCRCQPGYH GDGFQCTPAL
DPEDSVSGLK PCEHQQRYVQ VQPAYPGSPL HIPQCDEQGN FLPLQCHSST GFCWCVDQRG
HEIPGTRTPP GSTPPHCGAP GSEPTQRPQT VCERWRESLL EHYGGTARDD QYVPQCDDLG
QFIPLQCHGK SDFCWCVDKD GREVEGTRSQ PGTTPACIPT VAPPMVRPTP RPDVTPPSVG
TFLVYAQGQQ IGHLPLNGTR LQKDAAKTLL SLHGSIVVGI DYDCRERMVY WTDVAGRTIS
RASLEPGAEP ETVINTGLIS PEGLAIDHFR RTMYWTDSGL DKIESSKLDG SERRVLFHTE
LVNPRAITVD PIRGNLYWTD WNREAPKIET SSLNGENRRI LVNKDIGLPN GLTFDPFSKL
LCWADAGTKK LECTLPDGTG RRVIQHNLNY PFSIVSYADH FYHTDWRRDG VISVNKDSGQ
FTDEYLPEQR SHLYGITAVY PYCPTGNE
//