ID   LAMB1_HYDVU             Reviewed;         171 AA.
AC   Q27262; Q25181; Q27344;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 2.
DT   03-AUG-2022, entry version 82.
DE   RecName: Full=Laminin subunit beta-1;
DE   Flags: Precursor; Fragments;
OS   Hydra vulgaris (Hydra) (Hydra attenuata).
OC   Eukaryota; Metazoa; Cnidaria; Hydrozoa; Hydroidolina; Anthoathecata;
OC   Aplanulata; Hydridae; Hydra.
OX   NCBI_TaxID=6087;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=8026633; DOI=10.1006/dbio.1994.1201;
RA   Sarras M.P. Jr., Yan L., Grens A., Zhang X., Agbas A., Huff J.K.,
RA   St John P.L., Abrahamson D.R.;
RT   "Cloning and biological function of laminin in Hydra vulgaris.";
RL   Dev. Biol. 164:312-324(1994).
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; Z47545; CAA87592.1; -; mRNA.
DR   EMBL; Z47546; CAA87593.1; -; mRNA.
DR   EMBL; U18998; AAB60621.1; -; mRNA.
DR   EMBL; U18999; AAB60623.1; -; mRNA.
DR   EMBL; U19000; AAB60622.1; -; mRNA.
DR   PIR; S57894; S57894.
DR   AlphaFoldDB; Q27262; -.
DR   Proteomes; UP000694840; Unplaced.
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   CDD; cd00055; EGF_Lam; 1.
DR   InterPro; IPR002049; LE_dom.
DR   Pfam; PF00053; Laminin_EGF; 2.
DR   SMART; SM00180; EGF_Lam; 2.
DR   PROSITE; PS01248; EGF_LAM_1; 2.
DR   PROSITE; PS50027; EGF_LAM_2; 2.
PE   2: Evidence at transcript level;
KW   Basement membrane; Cell adhesion; Disulfide bond; Extracellular matrix;
KW   Glycoprotein; Laminin EGF-like domain; Reference proteome; Repeat;
KW   Secreted; Signal.
FT   SIGNAL          1..29
FT                   /evidence="ECO:0000255"
FT   CHAIN           30..>171
FT                   /note="Laminin subunit beta-1"
FT                   /id="PRO_0000017067"
FT   DOMAIN          <66..102
FT                   /note="Laminin EGF-like 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT   DOMAIN          103..160
FT                   /note="Laminin EGF-like 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT   DOMAIN          161..>171
FT                   /note="Laminin EGF-like 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT   CARBOHYD        130
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        59..69
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT   DISULFID        72..81
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT   DISULFID        84..100
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT   DISULFID        103..118
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT   DISULFID        105..128
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT   DISULFID        131..140
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT   DISULFID        143..158
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT   NON_CONS        65..66
FT                   /evidence="ECO:0000305"
FT   NON_TER         171
SQ   SEQUENCE   171 AA;  18510 MW;  25AE31A3E7CC899C CRC64;
     MNGRTQNLWF STFRLVIVYA LFFAKLCFGQ EECLRGGCYP ATGDLLVGRE NRITATSTCG
     LKERTTGVCN NCLHNTKGTN CQLCKDGYYG NALLGTENVC QRCQCPGGSS GNQFSNTCEL
     RDVGKVFCTN CSEGFTGTQC EKCDNGYYGN PLIQGGTCKK CLCNGNINSA S