ID A0A226N1K9_CALSU Unreviewed; 1419 AA.
AC A0A226N1K9;
DT 25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT 25-OCT-2017, sequence version 1.
DT 28-JAN-2026, entry version 28.
DE RecName: Full=Laminin G domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=ASZ78_010232 {ECO:0000313|EMBL:OXB61476.1};
OS Callipepla squamata (Scaled quail).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Odontophoridae;
OC Callipepla.
OX NCBI_TaxID=9009 {ECO:0000313|EMBL:OXB61476.1, ECO:0000313|Proteomes:UP000198323};
RN [1] {ECO:0000313|EMBL:OXB61476.1, ECO:0000313|Proteomes:UP000198323}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Texas {ECO:0000313|EMBL:OXB61476.1,
RC ECO:0000313|Proteomes:UP000198323};
RC TISSUE=Leg muscle {ECO:0000313|EMBL:OXB61476.1};
RA Oldeschulte D.L., Halley Y.A., Bhattarai E.K., Brashear W.A., Hill J.,
RA Metz R.P., Johnson C.D., Rollins D., Peterson M.J., Bickhart D.M.,
RA Decker J.E., Seabury C.M.;
RT "Disparate Historic Effective Population Sizes Predicted by Modern Levels
RT of Genome Diversity for the Scaled Quail (Callipepla squamata) and the
RT Northern Bobwhite (Colinus virginianus): Inferences from First and Second
RT Generation Draft Genome Assemblies for Sympatric New World Quail.";
RL Submitted (JUL-2016) 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:OXB61476.1}.
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DR EMBL; MCFN01000272; OXB61476.1; -; Genomic_DNA.
DR STRING; 9009.A0A226N1K9; -.
DR OrthoDB; 5983381at2759; -.
DR Proteomes; UP000198323; 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:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR GO; GO:0030198; P:extracellular matrix organization; IEA:TreeGrafter.
DR CDD; cd00247; Endostatin-like; 1.
DR CDD; cd00110; LamG; 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:SF906; COLLAGEN ALPHA-2(IX) CHAIN; 1.
DR Pfam; PF01391; Collagen; 5.
DR Pfam; PF20010; Collagen_trimer; 1.
DR Pfam; PF06482; Endostatin; 1.
DR Pfam; PF13385; Laminin_G_3; 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:UP000198323};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Secreted {ECO:0000256|ARBA:ARBA00022525};
KW Signal {ECO:0000256|ARBA:ARBA00022729}.
FT DOMAIN 79..267
FT /note="Thrombospondin-like N-terminal"
FT /evidence="ECO:0000259|SMART:SM00210"
FT DOMAIN 128..266
FT /note="Laminin G"
FT /evidence="ECO:0000259|SMART:SM00282"
FT REGION 268..763
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 828..848
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 866..1105
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 290..302
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 318..329
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 352..364
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 379..388
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 444..460
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 489..504
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 531..543
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 574..583
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 619..635
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 637..655
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 670..688
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 739..748
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 753..762
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 925..938
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 994..1008
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1020..1034
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1042..1051
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1062..1075
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1085..1097
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1419 AA; 144958 MW; EC46F26E1DE9E6EC CRC64;
MRMCVLPKQQ EFASRGLAHT ARCSAVPGCG AASLGGQWVA LGSVRKGTGV EGPAEVAPPC
CASGHHPLSL LFAENLSTEV SLLELIGDPP PEEILKIYGS ENNPGYVFGP NANTGQVARY
HLPSPFYRDF SLLFHIQPTT PRAGVLFAIT DSSQSIIYVG VKLSDVQMGK QQIIFYYTEP
GSQNSYAAAT FTVPTLLNQW THFAISVEED EVVLYLDCEE HERVRFERSP DEMELEEGSG
LFVAQAGGAD PDKYQGVIAD LRLVGDPRAA ERQCEEEDDT EASGDFGSGA EDRHRPSGKD
KGIPGLLDAV PVTSPPVAAG SGTRSSASSP QQVERTRVEE RLQVSTGGTG PKGEKGEKGE
RGLKGDSGSS GILGTGTAKG EKGEKGELGI KGSAGFGYPG SKGQKGEPGE PGPPGPLSRH
TDGMSVEQVT GPPGPPGPPG KDGAPGRDGE PGDPGEDGKP GEMGPQGFPG TPGESGQKGE
KGDPGMGPRG PPGPPGPPGP PGPSPKQDGL TFIDMEGSGF GGDLETLRGP RGPPGPPGPP
GVPGLPGEPG RFGMNSTDVP GPPGLPGRDG ATGPPGPEGP LGPPGKDGMP GPPGPKGERG
DVGDLGLPGA PGPKGSKGEA GPAGPPGETG LAGLPGPAGP PGQPGPPGPP GPPGPGYEAG
FGDMEGSGLP FTTGSPGPRG PSGPQGVPGL PGIKGEVGSL GQPGPPGPKG DAGVPGVDGR
PGLEGFPGPQ GPKGNRGSPG EKGERGHDGV GLPGPPGPPG PPGQVIYVSS EDVKAFGGSA
WPRGRYLPTA LCAVLLDRQL FAHCAHSLLL LLQGRPGHAG FPGPVGPKGD PGSPGIQGAP
GMKGEKGEPG VIISPDGTVV ATNVKGQKGE PGLQGPMGPT GPHGRAGMKG EIGFPGRPGR
PGMNGLKGEK GDPVDISSVL SLRGPPGPPG PPGPPGPPGS VVYSSNNGFS DASRPAIPGF
HQFPGQKGEK GDMGAPGPPG QFPYDLSRFS ASLRGDKGEA GPKGEKGEPG GSTLYGPSVT
GPPGPQGYPG PPGPKGDSIV GPPGPPGPQG PPGIGYEGRQ GPPGPPGPPG PPSFPGPHRQ
AISIPGPPGP PGPPGPPGTS GTSLGLRTVP TYQAMLSTAH ELPEGGLIFL DDRQELYVRV
RGGFRRVLLE EHTLVPGSAL DNEVYDKLPS IHYGGAQQPV HPLRNHSPPP TARPWRGDEV
VANQHRLPQP PLLQQHELLN SYYIHRWPDP APVAAHVHQD FQPALHLVAL NTPLSGGMRG
IRGADFQCFQ QARQVGLAGT FRAFLSSRLQ DLYSIVRRAD RTAVPIVNLR DEVLFSNWEA
LFTGSEAPLR AGARILSFDG RDILRDSAWP QKSIWHGSDA KGRRLPESYC EAWRTEERGT
SGQASSLSSG KLLEQSASSC QHAFVVLCIE NSFMTAAKK
//
