ID A0A2P4T5F1_BAMTH Unreviewed; 1278 AA.
AC A0A2P4T5F1;
DT 23-MAY-2018, integrated into UniProtKB/TrEMBL.
DT 23-MAY-2018, sequence version 1.
DT 28-JAN-2026, entry version 29.
DE RecName: Full=Laminin G domain-containing protein {ECO:0008006|Google:ProtNLM};
DE Flags: Fragment;
GN ORFNames=CIB84_004648 {ECO:0000313|EMBL:POI31601.1};
OS Bambusicola thoracicus (Chinese bamboo-partridge) (Perdix thoracica).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Perdicinae; Bambusicola.
OX NCBI_TaxID=9083 {ECO:0000313|EMBL:POI31601.1, ECO:0000313|Proteomes:UP000237246};
RN [1] {ECO:0000313|EMBL:POI31601.1, ECO:0000313|Proteomes:UP000237246}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RTK389 {ECO:0000313|EMBL:POI31601.1};
RC TISSUE=Blood {ECO:0000313|EMBL:POI31601.1};
RA Tiley G.P., Kimball R.T., Braun E.L., Burleigh J.G.;
RT "Comparison of the Chinese Bamboo Partridge and Red Junglefowl genome
RT sequences highlights the importance of demography in genome evolution.";
RL Submitted (JAN-2018) 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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:POI31601.1}.
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DR EMBL; PPHD01008166; POI31601.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2P4T5F1; -.
DR OrthoDB; 5983381at2759; -.
DR Proteomes; UP000237246; 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:0030020; F:extracellular matrix structural constituent conferring tensile strength; IEA:TreeGrafter.
DR GO; GO:0001525; P:angiogenesis; IEA:TreeGrafter.
DR GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR GO; GO:0001886; P:endothelial cell morphogenesis; IEA:TreeGrafter.
DR GO; GO:0030198; P:extracellular matrix organization; IEA:TreeGrafter.
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:SF1034; COLLAGEN ALPHA-1(XVIII) CHAIN; 1.
DR Pfam; PF01391; Collagen; 5.
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; 2.
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 Reference proteome {ECO:0000313|Proteomes:UP000237246};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Secreted {ECO:0000256|ARBA:ARBA00022525};
KW Signal {ECO:0000256|ARBA:ARBA00022729}.
FT DOMAIN 51..239
FT /note="Thrombospondin-like N-terminal"
FT /evidence="ECO:0000259|SMART:SM00210"
FT DOMAIN 100..238
FT /note="Laminin G"
FT /evidence="ECO:0000259|SMART:SM00282"
FT REGION 297..694
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 761..780
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 798..966
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 301..314
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 333..345
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 347..359
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 360..369
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 425..441
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 521..537
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 539..557
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 683..692
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 857..870
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 926..940
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 952..966
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:POI31601.1"
SQ SEQUENCE 1278 AA; 132128 MW; 812F017142903D72 CRC64;
CGAASLGEQW VALGSVPKGN GAEGPAEVAC PCCAVCHHPL SLLFAENLST EVSLLELIGD
PPPEEILKIY GPDNNPGYVF GPNANTGQVA RYHLPSPFYR DFSLLFHIQP TTPRAGVLFA
ITDSSQSIIY VGVKLSDLQM GKQQIIFYYT EPGSQSSYPA ATFTVPTLLN QWTRFAISVE
EDEVILYLDC EEHERVRFER SPDEMELEEG SGLFVAQAGG ADPDKYQGVI ADLRLRGDPR
AAEHQCEEEE DDAEVSTERL QPGGLLLGSW AEALCLSPAE CRHLEILAAG QRTGIIPQGR
ISGTRSSAGS PQQAERTRVE ERLQVSTGGT GPKGEKGEKG ERGPKGDSGT SGILGTGTTK
GEKGEKGELG IKGSAGFGYP GSKGQKGEPG EPGPPGPLSR HTDGMSLEQV TGPPGPTGPP
GKDGAPGRDG EPGDPGEDGK PGEMGPQGFP GTPGESGQKG EKTFIDMEGS GFGGDLETLR
GPLGPPGKDG MPGPPGPKGE RGDVGDLGLP GAPGPKGSKG EAGPAGPPGE TGLAGLPGPV
GPRGPPGLPG PPGPPGPGYE VGFVSAGSVH GDGGSACGVR GTGTAQPLLS QGDMEGSGLP
LATGSPGPRG PSGPQGVPGL PGIKGEVGSL GQPGPPGPKG DAGVPGVDGR PGLEGFPGPQ
GPKGNRGSPG EKGERGQDGV GLPGPPGPPG PPGQVIYISN EDVKAFGGSA RPRGRYLPTA
HTSPIHTSAV LVDSHLFAHC VLLLQGRSGH AGFPGPVGPK GDPGSPGIQG APGMKGEKGE
PGVIISPDGT IVAANVKGQK GEPGLPGPMG PSGPHGRAGM KGEIGFPGRP GRPGMNGLKG
EKGDPVDISS VLSLRGPPGP PGPPGPPGPP GSVVYDSNNG FSDASRPAFP GFHQFPGQKG
EKGDVGAPGP PGQFPYDLSR FSASLRGDKG EAGPKGEKGE PGSSTLYGPS VTGPPGPQGY
PGPPLRTMPT YQAMLSAAHE LPEGGLIFLA DRQELYVRLR GGFRRVLLEE HTLVPSSALD
NEVYDKLPSI HYEGAQQPVH PLRNHNPPPT ARPWRGDEVV ANQHRLPQPP LLQQHELLNS
YYIHRWPDPA PVAAHVHQDF QPALHLVALN TPLSGGMRGI RGADFQCFQQ ARQVGLAGTF
RAFLSSRLQD LYSIVRRADR TAVPIVNLRD EVLFSNWEAL FTGSEAPLRA GARILSFDGR
DILQDSAWPQ KSIWHGSDAK GRRLPESYCE AWRTDERGTS GQASSLSSGK LLEQSASSCQ
QAFVVLCIEN SFMTAAKK
//
