ID A0A060XB92_ONCMY Unreviewed; 1294 AA.
AC A0A060XB92;
DT 03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT 03-SEP-2014, sequence version 1.
DT 08-OCT-2025, entry version 46.
DE RecName: Full=Laminin G domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=GSONMT00022102001 {ECO:0000313|EMBL:CDQ74579.1};
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:CDQ74579.1, ECO:0000313|Proteomes:UP000193380};
RN [1] {ECO:0000313|EMBL:CDQ74579.1}
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:CDQ74579.1}
RP NUCLEOTIDE SEQUENCE.
RA Genoscope - CEA;
RL Submitted (MAR-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC matrix {ECO:0000256|ARBA:ARBA00004498}.
CC -!- SIMILARITY: Belongs to the multiplexin collagen family.
CC {ECO:0000256|ARBA:ARBA00061275}.
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DR EMBL; FR904983; CDQ74579.1; -; Genomic_DNA.
DR STRING; 8022.A0A060XB92; -.
DR PaxDb; 8022-A0A060XB92; -.
DR Proteomes; UP000193380; Unassembled WGS sequence.
DR GO; GO:0005581; C:collagen trimer; IEA:UniProtKB-KW.
DR GO; GO:0031012; C:extracellular matrix; IEA:TreeGrafter.
DR GO; GO:0005615; C:extracellular space; IEA:TreeGrafter.
DR GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR CDD; cd00247; Endostatin-like; 1.
DR FunFam; 3.10.100.10:FF:000008; collagen alpha-1(XVIII) chain isoform X1; 1.
DR FunFam; 3.40.1620.70:FF:000003; Collagen type XVIII alpha 1; 1.
DR FunFam; 2.60.120.200:FF:000039; Collagen XV alpha 1 chain; 1.
DR Gene3D; 2.60.120.200; -; 1.
DR Gene3D; 3.40.1620.70; -; 1.
DR Gene3D; 3.10.100.10; Mannose-Binding Protein A, subunit A; 1.
DR InterPro; IPR016186; C-type_lectin-like/link_sf.
DR InterPro; IPR008160; Collagen.
DR InterPro; IPR050149; Collagen_superfamily.
DR InterPro; IPR010515; Collagenase_NC10/endostatin.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR016187; CTDL_fold.
DR InterPro; IPR001791; Laminin_G.
DR InterPro; IPR048287; TSPN-like_N.
DR InterPro; IPR045463; XV/XVIII_trimerization_dom.
DR PANTHER; PTHR24023; COLLAGEN ALPHA; 1.
DR PANTHER; PTHR24023:SF1082; COLLAGEN TRIPLE HELIX REPEAT; 1.
DR Pfam; PF01391; Collagen; 2.
DR Pfam; PF20010; Collagen_trimer; 1.
DR Pfam; PF06482; Endostatin; 1.
DR SMART; SM00282; LamG; 1.
DR SMART; SM00210; TSPN; 1.
DR SUPFAM; SSF56436; C-type lectin-like; 1.
DR SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 1.
PE 3: Inferred from homology;
KW Cell adhesion {ECO:0000256|ARBA:ARBA00022889};
KW Collagen {ECO:0000256|ARBA:ARBA00023119};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW Extracellular matrix {ECO:0000256|ARBA:ARBA00022530};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Hydroxylation {ECO:0000256|ARBA:ARBA00023278};
KW Proteoglycan {ECO:0000256|ARBA:ARBA00022974};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Secreted {ECO:0000256|ARBA:ARBA00022525};
KW Signal {ECO:0000256|ARBA:ARBA00022729}.
FT DOMAIN 2..148
FT /note="Thrombospondin-like N-terminal"
FT /evidence="ECO:0000259|SMART:SM00210"
FT DOMAIN 7..147
FT /note="Laminin G"
FT /evidence="ECO:0000259|SMART:SM00282"
FT REGION 154..175
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 187..209
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 303..393
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 465..497
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 512..548
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 635..681
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 884..904
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 917..1018
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 325..338
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 649..664
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 670..681
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 917..929
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 978..992
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1000..1009
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1294 AA; 136459 MW; 4B709C15A625D297 CRC64;
MPDPFFRDFA IIVTIRPSSK QGGVLFAITD AQQKVVQLGL ALTPVEDETQ RIQLYYTEGG
EESSHSQQVA SFKLPDMRNK WTRFTLSVQD QEVRLYMDCD DFQAETFHRS SRQLSFEPSS
GIFVGNAGGT GLEKFVGSIQ QLVIKPDPRA AVEQCEEDDP YASGDGSGDD TLHDRETDDK
LMNMERKKET AQPEDMLSVP VRAPPTESPE LELDEYTVHL TPTNKAHQEM LLEGGEGSVC
CLKISNIPQW LALIEASLVN PIGVAFSSQD PTKQRSQGRA KIITSNVPQT LICFKCLNST
QCSPADPQGR PLSYGQKGER GEPGPMGPAG PRGPPGPSNP SEDRSGHGQP GPRGPQGPSG
APGVPGKDGQ PGSKGEDGDP GQRGPYGFPG LAGEVGVKGD KSYHVLFCTG GHRSRLTGAS
RPSRTTQISQ CTEDALGSGF GDLDDTEFIR RTKSFGVTLK RKGGINESGV ASEGSFPGQP
GSPGPPGRDG LVGKPGPPVR SLSVPLKWVC SSSQGVSGDP GLTGATGPMG PEGKTGDPGP
RGLPGPPGPP GGGFFFPIIL LSCFVSINSE CNNVVCWCLQ DVEGSGKNDM VLGTELKGPQ
VIEIGICVCL LGHWWMCLHL CSVSFQGEPG ASGPEGLQGL AGLPGARGLK GDKGDPGPKG
ECGPDGHNVP GPPGPPGPPG PIINLQELLL NNTEGMFNIT EIRGPPGPMV RQFAFIAISC
MGNDANYSFT SVIGLPGFQG PPGMKGAKGE AGVTIAADGT VLTSVRGPRG PKGIKGERGF
PGAYGVMGPI GPTGQKGEYG FPGRPVSAFC QPSAGDQGDA IGQPVRIAIL KHDFMRVQYN
QLRPVTGLNG TVFPVRPRPF CKTPVSLSQW SHTPVLYFCE GGRRRNGGAK GEKGDVGLPG
MPGEPDDILP EGFVGEKGDM GYEGMKGDQG EPGLPGPPGL PGRSGLVGPK GESVIGTVGH
PGAPGEPGVL GIGRPGSRGP PGPAGPPGPP PVYGSAVSIP GPPGPPGPPG ITGYENPVST
YRNTNSLIRE SHRAAEGSMA YVSDKGELYV RTRDGWRKVQ LGELILVPAE SPSSAVSQAL
SRPGDRTIPH RPHSQELVGT SYVPNYNVLP HTVHSVPALH LVALNAPFSG DMRGIRGADF
QCYQQARAMG LTATYRAFLS SHLQDLATIV KKGDRYNMPV INLKGEVIYS SWMNIFSGNG
GVFDPSIPIY SFEGRNVMTD PTWPQKLVWH GSSTVGIRMT TNYCEAWRAG DMAVMGQASL
LQTGRLLGQH TRSCSNHFIV LCIENSYIDH RRSN
//
