ID   LAMB_HIRME              Reviewed;         400 AA.
AC   Q25092;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   25-MAY-2022, entry version 72.
DE   RecName: Full=Laminin subunit B;
DE   Flags: Fragment;
OS   Hirudo medicinalis (Medicinal leech).
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Annelida; Clitellata;
OC   Hirudinea; Hirudinida; Hirudiniformes; Hirudinidae; Hirudo.
OX   NCBI_TaxID=6421;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=7643070; DOI=10.1002/neu.480270102;
RA   Luebke A.E., Dickerson I.M., Muller K.J.;
RT   "In situ hybridization reveals transient laminin B-chain expression by
RT   individual glial and muscle cells in embryonic leech central nervous
RT   system.";
RL   J. Neurobiol. 27:1-14(1995).
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 {ECO:0000250}.
CC   -!- TISSUE SPECIFICITY: Individual glial and muscle cells.
CC   -!- DEVELOPMENTAL STAGE: Embryonic development.
CC   -!- DOMAIN: The alpha-helical domains I and II are thought to interact with
CC       other laminin chains to form a coiled coil structure.
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DR   EMBL; U34921; AAC46862.1; -; mRNA.
DR   AlphaFoldDB; Q25092; -.
DR   SMR; Q25092; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR   CDD; cd00055; EGF_Lam; 2.
DR   InterPro; IPR002049; LE_dom.
DR   Pfam; PF00053; Laminin_EGF; 2.
DR   SMART; SM00180; EGF_Lam; 2.
DR   PROSITE; PS00022; EGF_1; 2.
DR   PROSITE; PS01248; EGF_LAM_1; 2.
DR   PROSITE; PS50027; EGF_LAM_2; 2.
PE   2: Evidence at transcript level;
KW   Coiled coil; Disulfide bond; Extracellular matrix; Glycoprotein;
KW   Laminin EGF-like domain; Repeat; Secreted.
FT   CHAIN           <1..>400
FT                   /note="Laminin subunit B"
FT                   /id="PRO_0000086855"
FT   DOMAIN          <1..5
FT                   /note="Laminin EGF-like 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT   DOMAIN          6..53
FT                   /note="Laminin EGF-like 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT   DOMAIN          54..100
FT                   /note="Laminin EGF-like 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT   REGION          101..>400
FT                   /note="Domain II and I"
FT   REGION          369..400
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          140..235
FT                   /evidence="ECO:0000255"
FT   COILED          353..>400
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        369..392
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        160
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        175
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        216
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        266
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        283
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        310
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        356
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        6..18
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT   DISULFID        8..25
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT   DISULFID        27..36
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT   DISULFID        39..51
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT   DISULFID        54..66
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT   DISULFID        56..73
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT   DISULFID        75..84
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT   DISULFID        87..98
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT   DISULFID        101
FT                   /note="Interchain"
FT                   /evidence="ECO:0000305"
FT   DISULFID        104
FT                   /note="Interchain"
FT                   /evidence="ECO:0000305"
FT   NON_TER         1
FT   NON_TER         400
SQ   SEQUENCE   400 AA;  43262 MW;  4330ABE05A61B012 CRC64;
     EGCKPCECDK SGSRLEQCNL YDGQCDCVDG RGGRDCSQCP EMSWGDPFLG CKSCTCNPDG
     ARSLYCNKVT GQCECPRGVT GLNCDRCDRG TYGALPQCIP CGECFDNWDK LIAQLRDEAA
     AQLRIGTEIK LSGPPGAFAK EFEELEQVLM DMKSHVNSAN VSSDQLENID QELDNLSSKL
     KDLKPNLASH GSRTGEASVK ISELYSRVLN LQSEFNKSSA KTKELRENAL EIQEQDVSGA
     YASIQESLVK SSALQAKLTD AENSKNISVY FRTSVEHFLQ NSNFSDANSE NGNENSLDKV
     VEFMKAVDEN VSSINTELCG GTGSPCHEDC GGAMCGKCGG ELCGDGAVTK AVEAKNTSRK
     AEELIKSKYR STSSTLSELE NSNKQCKQAT AEAKNNAHEA