ID   LAMBV_CHICK             Reviewed;         198 AA.
AC   Q01636;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   27-MAR-2024, entry version 87.
DE   RecName: Full=Laminin subunit beta-1 variant;
DE   AltName: Full=Laminin beta-1-2 chain;
DE   Flags: Fragment;
OS   Gallus gallus (Chicken).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC   Phasianinae; Gallus.
OX   NCBI_TaxID=9031;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Eye;
RX   PubMed=1400373; DOI=10.1016/s0021-9258(19)36720-1;
RA   O'Rear J.J.;
RT   "A novel laminin B1 chain variant in avian eye.";
RL   J. Biol. Chem. 267:20555-20557(1992).
CC   -!- FUNCTION: Binding to cells via a high affinity receptor, laminin is
CC       thought to mediate the attachment, migration and organization of cells
CC       into tissues during embryonic development by interacting with other
CC       extracellular matrix components.
CC   -!- SUBUNIT: Laminin is a complex glycoprotein, consisting of three
CC       different polypeptide chains (alpha, beta, gamma), which are bound to
CC       each other by disulfide bonds into a cross-shaped molecule comprising
CC       one long and three short arms with globules at each end.
CC   -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC       matrix, basement membrane. Note=Major component.
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DR   EMBL; L00963; AAA49140.1; -; mRNA.
DR   PIR; A45067; A45067.
DR   AlphaFoldDB; Q01636; -.
DR   SMR; Q01636; -.
DR   VEuPathDB; HostDB:geneid_373980; -.
DR   InParanoid; Q01636; -.
DR   PhylomeDB; Q01636; -.
DR   Proteomes; UP000000539; Unassembled WGS sequence.
DR   GO; GO:0005604; C:basement membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR   GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR   Gene3D; 2.60.120.260; Galactose-binding domain-like; 1.
DR   InterPro; IPR008211; Laminin_N.
DR   PANTHER; PTHR10574:SF36; LAMININ SUBUNIT BETA-2; 1.
DR   PANTHER; PTHR10574; NETRIN/LAMININ-RELATED; 1.
DR   Pfam; PF00055; Laminin_N; 1.
DR   SMART; SM00136; LamNT; 1.
DR   PROSITE; PS51117; LAMININ_NTER; 1.
PE   2: Evidence at transcript level;
KW   Basement membrane; Cell adhesion; Disulfide bond; Extracellular matrix;
KW   Laminin EGF-like domain; Reference proteome; Secreted.
FT   CHAIN           <1..>198
FT                   /note="Laminin subunit beta-1 variant"
FT                   /id="PRO_0000086854"
FT   DOMAIN          83..>198
FT                   /note="Laminin N-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00466"
FT   REGION          1..64
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        24..40
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        41..62
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   NON_TER         1
FT   NON_TER         198
SQ   SEQUENCE   198 AA;  21830 MW;  6FD669761892C442 CRC64;
     AATTLRRGGG REPTPPATPP THARPDPTRR HPDPESRAPP HARPRSPPPP APSPPPLPPR
     PAAVRAGRDR VGRVFSRLPP GCAAGSCYPA TGDLLVGRAP RLSASSTCGL RRPQPYCIVS
     HLQEEKKCFI CDSRRPYDAR SNTDSHRIEN VLTTFAPRPK KAWWQAENGV EHVSIQLDLE
     AEFHFTHLIM TFKTFRPA
//