ID A0A2U9AVE1_SCOMX Unreviewed; 1342 AA.
AC A0A2U9AVE1;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE SubName: Full=Putative nidogen-2 {ECO:0000313|EMBL:AWO95644.1};
GN ORFNames=SMAX5B_015269 {ECO:0000313|EMBL:AWO95644.1};
OS Scophthalmus maximus (Turbot) (Psetta maxima).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Carangaria; Pleuronectiformes; Pleuronectoidei; Scophthalmidae;
OC Scophthalmus.
OX NCBI_TaxID=52904 {ECO:0000313|EMBL:AWO95644.1, ECO:0000313|Proteomes:UP000246464};
RN [1] {ECO:0000313|EMBL:AWO95644.1, ECO:0000313|Proteomes:UP000246464}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Martinez P.;
RT "Integrating genomic resources of turbot (Scophthalmus maximus) in depth
RT evaluation of genetic and physical mapping variation across individuals.";
RL Submitted (DEC-2017) to the EMBL/GenBank/DDBJ databases.
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; CP026243; AWO95644.1; -; Genomic_DNA.
DR Proteomes; UP000246464; Chromosome 1.
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; 2.
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; 2.
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; PTHR46513:SF15; NIDOGEN-2 ISOFORM X1; 1.
DR PANTHER; PTHR46513; VITELLOGENIN RECEPTOR-LIKE PROTEIN-RELATED-RELATED; 1.
DR Pfam; PF12947; EGF_3; 2.
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; 2.
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; 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; 4.
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:UP000246464};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Secreted {ECO:0000256|ARBA:ARBA00022525}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..23
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 24..1342
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5016020044"
FT DOMAIN 101..268
FT /note="NIDO"
FT /evidence="ECO:0000259|PROSITE:PS51220"
FT DOMAIN 452..492
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 496..726
FT /note="Nidogen G2 beta-barrel"
FT /evidence="ECO:0000259|PROSITE:PS50993"
FT DOMAIN 728..769
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 770..812
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 851..889
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 899..969
FT /note="Thyroglobulin type-1"
FT /evidence="ECO:0000259|PROSITE:PS51162"
FT DOMAIN 982..1050
FT /note="Thyroglobulin type-1"
FT /evidence="ECO:0000259|PROSITE:PS51162"
FT REPEAT 1121..1164
FT /note="LDL-receptor class B"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT REPEAT 1165..1207
FT /note="LDL-receptor class B"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT REPEAT 1208..1252
FT /note="LDL-receptor class B"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT REGION 283..410
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 956..976
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 305..325
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 938..945
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00500"
FT DISULFID 1020..1027
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00500"
SQ SEQUENCE 1342 AA; 147117 MW; 8F26C59CFC2508DE CRC64;
MQPGDVLAVC LLCWSCGVRV AAAVHRTDLF PYGTLSGDSV LAEGDDETSR VLSLPRPFYF
YSSLFAQLYV ATNGIISAQD LPMEKQYVDD GFPTDFPVVA PFLADIDTSG GRGQIYYRVT
ETPSVLNRVA QEVHRGFPDA KFTPTHAVVA TWENVAAYEE QSRTSGPSNK VNTFQAVIGY
DETDSYVLFL YPEGGLNFFG TRPKESYNVE IELPARVGFS RGEITYLIFS RTEGPHFSVT
GDQETVKNLN QVGNTGIPGI WLFHTGNRYS FDNIVPASIG GLLATSPTGR LPLDTTTPEY
GEFEDYPDNT FEPDNQPEED DYPLTGGDPE FQPAPAGGDH AEAPRPAGPD APFHPEEPGR
SESYGNEDVP LTSEPRYGVE PAARQYAPPH SPEAREEGGA KQNQQQQPQA PLEVVDVYPP
PQTRLSPGGH VVSVEDEDVD FDTGVIQYTT ENKETCARFQ QQCSQNSFCS DYATGYCCHC
RPGFYGNGRH CLPEGAPQRV SGKVSGTVTV GSTPVSLNNI DLHAYIVVGD GRAYTAISEV
PEPVGWALMP VAPIGELFGW LFALELPNSQ AGFKTTGAEF TRRAEITFYP GNERLSISQT
ARGLDDNNHL TVDTVVSGSV PFLPPGAEVT MDPFKETYQY YPSVATSSSV REFSVVSAER
GSESFSFQLK QNITYRDCRH DNRAAAPETL QITMERVFVM YVKEERILRY AITNKISPVG
VEPTGPELVN PCYAGNHDCD TTAQCIPLEG QAFQCQCATG YRGDGRNCYD VDECAESSSS
CGAHAQCVNL PGSHRCQCQS GYEFGYDGRT CVDTVYHHVL FPPSSCSHLV SCTRLSPKMH
FWSAQCCMFQ NVDECSSSPC HVNARCINRL GSFQCQCQPG FDGDGFYCSE QEDEPERPKT
HCEHHRDGVQ TTSPEGYPLL GVFVPQCDAN GQYTSQQCDG STGSCWCVDR RGQERAGTRT
KPGAPSVDCD KPVPVTPTQR PESVCERWRA SLIEHYGGKP EPQQYVPQCE PDGQFSPVQC
YGETTYCWCV DQDGREVPGT RSHDVVKPAC LPSVAPPTMR PLPRPDVTPP TNAGVTLLYA
QGQKIGALPL NGTRLDGTGS KTLLTLHGSI VVGIGYDCKE NQVYWTDLSA RTINRASLVP
GAEPEILINT NLVSPEGLAV DVKRRLIFWV DSTPDVIESA NLDGSGRQTL FDTDLVNPRA
IIVVSSAGTL YWTDWNREAP KIECASVDGQ NRRVVVSDGI GLPNALTFDS SSGQVCWADA
GTKRLECISP DGSGRRVIHP TLNYPFSMVY YRGHFYYTDW RRDGVIVVSK DSSQFTDEYL
PDQRSHLYGI AIATTDCLSG TH
//
