ID W5N2B6_LEPOC Unreviewed; 1401 AA.
AC W5N2B6;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 27-MAR-2024, entry version 65.
DE SubName: Full=Nidogen 2 {ECO:0000313|Ensembl:ENSLOCP00000014775.1};
GN Name=NID2 {ECO:0000313|Ensembl:ENSLOCP00000014775.1};
OS Lepisosteus oculatus (Spotted gar).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Holostei; Semionotiformes; Lepisosteidae;
OC Lepisosteus.
OX NCBI_TaxID=7918 {ECO:0000313|Ensembl:ENSLOCP00000014775.1, ECO:0000313|Proteomes:UP000018468};
RN [1] {ECO:0000313|Proteomes:UP000018468}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Di Palma F., Alfoldi J., Johnson J., Berlin A., Gnerre S., Jaffe D.,
RA MacCallum I., Young S., Walker B.J., Lander E.S., Lindblad-Toh K.;
RT "The Draft Genome of Lepisosteus oculatus.";
RL Submitted (DEC-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSLOCP00000014775.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-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 EMBL; AHAT01019078; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_015206360.1; XM_015350874.1.
DR Ensembl; ENSLOCT00000014804.1; ENSLOCP00000014775.1; ENSLOCG00000012006.1.
DR GeneID; 102697886; -.
DR KEGG; loc:102697886; -.
DR CTD; 322921; -.
DR GeneTree; ENSGT00940000157901; -.
DR HOGENOM; CLU_003163_1_0_1; -.
DR OrthoDB; 25347at2759; -.
DR Proteomes; UP000018468; Linkage group LG7.
DR Bgee; ENSLOCG00000012006; Expressed in larva and 11 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; 2.
DR CDD; cd00255; nidG2; 1.
DR CDD; cd00191; TY; 3.
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; 3.
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; 2.
DR Pfam; PF06119; NIDO; 1.
DR Pfam; PF00086; Thyroglobulin_1; 3.
DR SMART; SM00181; EGF; 4.
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; 3.
DR SUPFAM; SSF54511; GFP-like; 1.
DR SUPFAM; SSF57184; Growth factor receptor domain; 2.
DR SUPFAM; SSF57610; Thyroglobulin type-1 domain; 3.
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; 3.
DR PROSITE; PS51162; THYROGLOBULIN_1_2; 3.
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:UP000018468};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Secreted {ECO:0000256|ARBA:ARBA00022525}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..22
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 23..1401
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004869174"
FT DOMAIN 100..267
FT /note="NIDO"
FT /evidence="ECO:0000259|PROSITE:PS51220"
FT DOMAIN 481..521
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 525..754
FT /note="Nidogen G2 beta-barrel"
FT /evidence="ECO:0000259|PROSITE:PS50993"
FT DOMAIN 753..794
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 795..837
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 838..874
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 883..955
FT /note="Thyroglobulin type-1"
FT /evidence="ECO:0000259|PROSITE:PS51162"
FT DOMAIN 964..1033
FT /note="Thyroglobulin type-1"
FT /evidence="ECO:0000259|PROSITE:PS51162"
FT DOMAIN 1043..1110
FT /note="Thyroglobulin type-1"
FT /evidence="ECO:0000259|PROSITE:PS51162"
FT REPEAT 1180..1223
FT /note="LDL-receptor class B"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT REPEAT 1224..1266
FT /note="LDL-receptor class B"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT REPEAT 1267..1311
FT /note="LDL-receptor class B"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT REGION 289..430
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 942..962
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 306..324
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 396..410
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 924..931
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00500"
FT DISULFID 1002..1009
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00500"
SQ SEQUENCE 1401 AA; 154730 MW; F481322F76C99A83 CRC64;
MWDKVLTVFF LKLSWTVYIA SAIQRTDLFP YGTQSGDLIL QEGDDETSEV LRLKKPMFFY
EAQFSELYVA TNGIISAQDL PRETQYVDDG FPTDFPVIAP FLADIDTSKG KGTVFYRLDE
SPSVLLRAGE EVKRGFPDSN FTPTHAVIAT WENVGLYEEL TRNSEPSNRV NTFQAVLAYD
ETNTYALFLY PEDGLQFFGT RPKESYNVHL ELPARVGFSR GEITYLIFSR TEGPYYSVTS
TEQTVKDLYQ VGNSGVPGLW LFHMGSSFTL PNVVPAVAGG VHAEHGPVAP ALESASNGPL
QPEPDYPEED YPEEDYEGET DLEYPTTDLP DLASKKPTVL LPSYPGTQEL GPASVQPPPY
SVAENGPDSE LDRLYPEASN TDLQTEPPRM EVPATQASLS RASRPRANPQ LRNLPSEDGK
APEPSTSQPA PAELDLLSVY PIGEVVPILE STPPHNPGGH VVSVDEVVNF DSGVIEYSTE
NKETCSKFQQ HCSQYGYCTD YSSGFCCHCQ SGYYGNGRHC LPNGAPQRVN GRVSGQVSVG
ATPVDLSSVD LHAYVVVSDG RAYTAISQIP EPAGWALMPL STIGGLFGWL LALELQGSEN
GFSVTGAEFT RYAEVTFYPG NQRLSIVQTA QGLDSHNYLT VDTRINGEIP FVPPGATVQI
EPFKETYHYH PSVVTSSSVH QYKVMSLEQG SETFSYQLRQ NVTYRDCRHG PQGGPAMRQL
SVERVFIMYT KEEHTLRFAV TSQIGPFGVE PTPVNPCYKG THECDTSAQC LPGEGTQYQC
QCATGYRGDG RNCFDIDECT EGLSSCGAHS VCINLQGSHR CECQNGYEFG FDKRTCIDID
ECRTQRCHPH AICYNTLGSY DCQCLSGYEG DGFQCILHPV RPKTQCEQHR DGLQGGLRPR
GHRPSVGTFV PQCDEEGNYR PLQCHGSTGH CWCVDSSGQE RVGTRTPPGT PPVDCMTATS
ERPRTQCEQH RDGLLSSLAT TPIRGAFVPQ CDERGSYRPL QCHSSTEYCW CVDSNGQERA
GTRTPPGTAL PDCDLPGPLQ RPETVCERWK ASLIEQYGGQ PAAHQFLPQC DELGQFKPLQ
CYGENYCWCV DKDGREVPGT RSQDTVKPAC VPTVAPPIVR PTPRPDVTPP PKGTALLYAQ
GQQIGTLPLN GTDMDKQRAS VLLALHGSIV VGIDYDCREK KVYWTDLAGR TINRASLELG
AEPETVINTG LLSPEGLAID SQRRTMFWVD SGLDKIEKAR LDGGERKVMF DTDLVNPRAI
VVDSLHGNLY WTDWNREGPK IESCTVEGHN RRVLVRDGIG LPNALTFDPL TKQLCWADAG
TKRLECIAPD GTERRIIHSN LNYPFSLVAY SNHFYYTDWR RDGVIGLSRG TSQFTDTYLP
DQRSHLYGIT VAYSSCVPGR K
//
