ID A0A226MK50_CALSU Unreviewed; 1485 AA.
AC A0A226MK50;
DT 25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT 25-OCT-2017, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE RecName: Full=Laminin subunit gamma-1 {ECO:0008006|Google:ProtNLM};
GN ORFNames=ASZ78_007103 {ECO:0000313|EMBL:OXB55429.1};
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:OXB55429.1, ECO:0000313|Proteomes:UP000198323};
RN [1] {ECO:0000313|EMBL:OXB55429.1, ECO:0000313|Proteomes:UP000198323}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Texas {ECO:0000313|EMBL:OXB55429.1,
RC ECO:0000313|Proteomes:UP000198323};
RC TISSUE=Leg muscle {ECO:0000313|EMBL:OXB55429.1};
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, basement membrane {ECO:0000256|ARBA:ARBA00004302}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00460}.
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:OXB55429.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; MCFN01000748; OXB55429.1; -; Genomic_DNA.
DR STRING; 9009.A0A226MK50; -.
DR Proteomes; UP000198323; Unassembled WGS sequence.
DR GO; GO:0005604; C:basement membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR CDD; cd00055; EGF_Lam; 10.
DR Gene3D; 2.60.120.260; Galactose-binding domain-like; 1.
DR Gene3D; 2.10.25.10; Laminin; 9.
DR Gene3D; 1.10.287.950; Methyl-accepting chemotaxis protein; 1.
DR InterPro; IPR000742; EGF-like_dom.
DR InterPro; IPR000034; Laminin_IV.
DR InterPro; IPR008211; Laminin_N.
DR InterPro; IPR002049; LE_dom.
DR PANTHER; PTHR10574:SF270; LAMININ SUBUNIT GAMMA-1; 1.
DR PANTHER; PTHR10574; NETRIN/LAMININ-RELATED; 1.
DR Pfam; PF00052; Laminin_B; 1.
DR Pfam; PF00053; Laminin_EGF; 10.
DR Pfam; PF00055; Laminin_N; 1.
DR PRINTS; PR00011; EGFLAMININ.
DR SMART; SM00181; EGF; 7.
DR SMART; SM00180; EGF_Lam; 10.
DR SMART; SM00281; LamB; 1.
DR SMART; SM00136; LamNT; 1.
DR SUPFAM; SSF57196; EGF/Laminin; 9.
DR SUPFAM; SSF58104; Methyl-accepting chemotaxis protein (MCP) signaling domain; 1.
DR PROSITE; PS01248; EGF_LAM_1; 5.
DR PROSITE; PS50027; EGF_LAM_2; 6.
DR PROSITE; PS51115; LAMININ_IVA; 1.
DR PROSITE; PS51117; LAMININ_NTER; 1.
PE 4: Predicted;
KW Basement membrane {ECO:0000256|ARBA:ARBA00022869};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW ProRule:PRU00460}; Extracellular matrix {ECO:0000256|ARBA:ARBA00022869};
KW Laminin EGF-like domain {ECO:0000256|ARBA:ARBA00023292,
KW ECO:0000256|PROSITE-ProRule:PRU00460}; Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000198323};
KW Secreted {ECO:0000256|ARBA:ARBA00022869};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 6..30
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 37..58
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 1..237
FT /note="Laminin N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51117"
FT DOMAIN 294..349
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 350..396
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 397..446
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 473..664
FT /note="Laminin IV type A"
FT /evidence="ECO:0000259|PROSITE:PS51115"
FT DOMAIN 706..761
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 762..812
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 813..863
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT COILED 911..1020
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1056..1231
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1330..1392
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1434..1468
FT /evidence="ECO:0000256|SAM:Coils"
FT DISULFID 322..331
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 350..362
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 370..379
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 417..426
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 730..739
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 785..794
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 813..825
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 815..832
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 834..843
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
SQ SEQUENCE 1485 AA; 163881 MW; DF919C68E14BF4FE CRC64;
MSAEENYSVL VACLFALKSM GLFISSACFL TFGSFTLSLL GSTVLVLLAA AHPIGWIWRS
SKPQTRSAAQ LFSFSVVSCW SLSHNSLLSS AGKAFDITYV RLKFHTSRPE SFAIYKRTRE
DGPWVPYQYY SGSCESTYNK VNRGFIRTGE DEQQALCTDE FSDISPLTGG NVAFSTLEGR
PSAYNFDNSP VLQEWVTATD IRVSLNRLNT FGDEVFNDPK VLKSYYYAIS DFAVGGRCKC
NGHASECIRN ELGKLVCNCK HNTFGDDCEK CLPFFNDRPW RRATAESANE CLPCDCNGRS
QECYFDPELY RSTGHGGHCS GCRDNTDGAH CERCRDGFYR LSSEEGCLPC SCNPVGSLST
QCDSYGQCSC KPGVMGEKCD RCQPGFHSLS EAGCRPCSCN PAGSTGECNM ETGRCACKDN
VEGFHCERCK PGFFHLDPSN PRGCTPCFCF GHSSVCTNAV GYSVYSITSS FQFGEDEWHA
EQRDGSQVPL QWSSETQDIS VISDSYFPIY FVAPSKFLGN QVLSYGQNLT FSFRVDRRDT
RLSAEDLVLE GAGLRVSVPL IAQGNTYPSE NPLTYTFRLH EAADYPWRPA LSAFDFQKLL
HNLTAIKIRG TYSERSVCDC RDNTAGSQCE KCSDGYYGDA TAGTALDCQP CPCPGGSSCA
VVPRTREVVC TSCHTGTTGK RCELCDDAYF GDPLGENGAV RPCRLCQCND NIDPNAVGNC
NRHTGECLKC IYNTAGFYCD RCKDGFFGNP LAPNPADKCR ACHCNPYGTV NQQTSCNQVT
GQCECLPHVT ERDCSACEPG FFNLQSGRGC ERCDCHALGS TNGQCDIWTG QCECQPGVTG
QRCDRCEANH FGLAFPTACD CDPEGSRALQ CREDGRCECK EGFVGNRCDQ CEENYFYNRS
WPGCQECPAC YRLVKDKVAE QRERLQELEN LIANLGTGGE TVTDQAFEER LKQAERDVME
LLQEAQNSKD VDQGLMDRLR DINSTLTSQL SRLRNIQNTV QETENLAEQA RGRVEDTEDL
IAMASDMLEK AKMAADNVSI TAPESSGDPN NMTLLAEEAR RLAERHKQEA DKIVRIAKAA
NDTSTEAYQL LLKTLAGENQ TARDIDELNQ KYNQARNISR DLERQANSVL EEAEEAGNKA
LQIYANLTNL PTVDTTGLES EANKIKKEAE ELDQLIARKL KDYEDLREDM KGKELEVKNL
LEKGKTEQQT ADQLLARADA AKALAEEAAR KGNGTLQEAN TILSNLKDFD KRVNDNKTAA
EEALKKIPAI TQTIAEANNK TRQAELALGN AAADAREAKT RADDAEKIAS AVQKSAAATR
AEADKTFSDV TGLAKEVDDM MKQLQEAEKE LKRKQDDADQ DMMMAGMASQ AAQEAEDNAR
KAKNSVNSLL AVVNDLLDQL GQLETVDLNK LNEIEGTLNS AKNQMKGSDL DQKVAFLERE
ARKQDDAIQS YNRDIEEILK DISNLEDIKK TLPSGCFNTP SIEKP
//