ID A0A060WCD6_ONCMY Unreviewed; 868 AA.
AC A0A060WCD6;
DT 03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT 03-SEP-2014, sequence version 1.
DT 24-JAN-2024, entry version 55.
DE RecName: Full=Nidogen-2 {ECO:0008006|Google:ProtNLM};
GN ORFNames=GSONMT00072350001 {ECO:0000313|EMBL:CDQ64968.1};
OS Oncorhynchus mykiss (Rainbow trout) (Salmo gairdneri).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Protacanthopterygii; Salmoniformes;
OC Salmonidae; Salmoninae; Oncorhynchus.
OX NCBI_TaxID=8022 {ECO:0000313|EMBL:CDQ64968.1, ECO:0000313|Proteomes:UP000193380};
RN [1] {ECO:0000313|EMBL:CDQ64968.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=24755649; DOI=10.1038/ncomms4657;
RA Berthelot C., Brunet F., Chalopin D., Juanchich A., Bernard M., Noel B.,
RA Bento P., Da Silva C., Labadie K., Alberti A., Aury J.M., Louis A.,
RA Dehais P., Bardou P., Montfort J., Klopp C., Cabau C., Gaspin C.,
RA Thorgaard G.H., Boussaha M., Quillet E., Guyomard R., Galiana D., Bobe J.,
RA Volff J.N., Genet C., Wincker P., Jaillon O., Roest Crollius H.,
RA Guiguen Y.;
RT "The rainbow trout genome provides novel insights into evolution after
RT whole-genome duplication in vertebrates.";
RL Nat. Commun. 5:3657-3657(2014).
RN [2] {ECO:0000313|EMBL:CDQ64968.1}
RP NUCLEOTIDE SEQUENCE.
RA Genoscope - CEA;
RL Submitted (MAR-2014) to the EMBL/GenBank/DDBJ databases.
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; FR904489; CDQ64968.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A060WCD6; -.
DR STRING; 8022.A0A060WCD6; -.
DR PaxDb; 8022-A0A060WCD6; -.
DR Proteomes; UP000193380; Unassembled WGS sequence.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0048513; P:animal organ development; IEA:UniProt.
DR CDD; cd00054; EGF_CA; 3.
DR CDD; cd00191; TY; 5.
DR Gene3D; 2.10.25.10; Laminin; 4.
DR Gene3D; 4.10.800.10; Thyroglobulin type-1; 5.
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; IPR009030; Growth_fac_rcpt_cys_sf.
DR InterPro; IPR000033; LDLR_classB_rpt.
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; 2.
DR Pfam; PF07645; EGF_CA; 2.
DR Pfam; PF00058; Ldl_recept_b; 2.
DR Pfam; PF00086; Thyroglobulin_1; 5.
DR SMART; SM00181; EGF; 4.
DR SMART; SM00179; EGF_CA; 4.
DR SMART; SM00135; LY; 4.
DR SMART; SM00211; TY; 5.
DR SUPFAM; SSF57196; EGF/Laminin; 1.
DR SUPFAM; SSF57184; Growth factor receptor domain; 1.
DR SUPFAM; SSF57610; Thyroglobulin type-1 domain; 5.
DR SUPFAM; SSF63825; YWTD domain; 1.
DR PROSITE; PS00010; ASX_HYDROXYL; 1.
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; PS00484; THYROGLOBULIN_1_1; 4.
DR PROSITE; PS51162; THYROGLOBULIN_1_2; 5.
PE 4: Predicted;
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}; Reference proteome {ECO:0000313|Proteomes:UP000193380};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Secreted {ECO:0000256|ARBA:ARBA00022525}.
FT DOMAIN 8..49
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 50..92
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 93..135
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 136..172
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 184..261
FT /note="Thyroglobulin type-1"
FT /evidence="ECO:0000259|PROSITE:PS51162"
FT DOMAIN 271..341
FT /note="Thyroglobulin type-1"
FT /evidence="ECO:0000259|PROSITE:PS51162"
FT DOMAIN 351..421
FT /note="Thyroglobulin type-1"
FT /evidence="ECO:0000259|PROSITE:PS51162"
FT DOMAIN 431..500
FT /note="Thyroglobulin type-1"
FT /evidence="ECO:0000259|PROSITE:PS51162"
FT DOMAIN 513..581
FT /note="Thyroglobulin type-1"
FT /evidence="ECO:0000259|PROSITE:PS51162"
FT REPEAT 651..694
FT /note="LDL-receptor class B"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT REPEAT 695..737
FT /note="LDL-receptor class B"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT REPEAT 738..782
FT /note="LDL-receptor class B"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT REGION 180..208
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 248..286
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 326..369
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 408..449
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 487..512
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 261..282
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 342..360
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 424..440
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 230..237
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00500"
FT DISULFID 310..317
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00500"
FT DISULFID 390..397
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00500"
FT DISULFID 469..476
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00500"
FT DISULFID 551..558
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00500"
SQ SEQUENCE 868 AA; 95581 MW; F705AD7794BFA873 CRC64;
MEPPELVQVN PCYSGTHDCD TTAQCLPGEG QQYQCQCATG YMGDGRNCYD VDECVEGLSL
CGAHAQCVNL PGSHRCQCQS GYKFGFDGRT CIDVDECVEG IGLCGANAHC VNLPGSHRCQ
CQSGYEFDID GRTCIDLDEC RSQPCHPQAT CSNTLGSFQC QCQYDFQGDG FQCVPSNGHP
ERPKTQCEQH RDSLQGGLSP RGPRPVPGGL APGAFVPQCD EQGQYRALQC HGSTGHCWCV
DSRGQERAGT RTLPRTPPTN CDRPDHTERP KTQCEHHRDS VQTTSPEGYS IVEGFLPQCD
EQGQYRALQC HGSTGHCWCV DNRGQERAGT RKPPGTGQPN CDEPDRPERP KTHCEQHKDS
VQTTSPEGYP ILGVFVPECD EQGQYRALQC HGSTGYCWCV DSRGQERAGT RKGPGTGQPN
CDVPDHPERP KTHCEHQRDS LQTTSPEGNV DGAFVPQCDE QGQYRALQCH GATGHCWCVD
SRGQERAGTR KPPGTSQPNC DEPAVVPPTQ RPETVCERWR ASLVDHYGGL PRPHHYLPQC
DPQGQFNPIQ CYGDSSYCWC VDRDGREVAG TRSHDVVKPA CVPTVAPPTM HPLPRPDVTP
PPSGTSLLYA QGQQIGALPL NGTLMDSERS STLLALHGSI VVGIDYDCRE KKVYWTDLAG
RTINRARLEP GAEPETLINT GLTSPEGLAV DVVRRAMFWV DSTPDKIERA NLDGSGRQTL
FDTDMVNPRA IIVDSSTGTL YWTDWNREAP KIERSSVDGH SRKVLVKDGI GLPNALTFDT
ATRQVCWADA GTKRLECIAS DGTGRRVIHS NLNYPFSMVF YANHFYFTDW RRDGVIALSR
DSSQFTDEYL PDQRSHLYGV TIATTHCL
//
