LAMB1_CHICK
ID LAMB1_CHICK Reviewed; 303 AA.
AC Q01635;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 112.
DE RecName: Full=Laminin subunit beta-1;
DE AltName: Full=Laminin beta-1-1 chain;
DE AltName: Full=Laminin-1 subunit beta;
DE AltName: Full=Laminin-10 subunit beta;
DE AltName: Full=Laminin-12 subunit beta;
DE AltName: Full=Laminin-2 subunit beta;
DE AltName: Full=Laminin-6 subunit beta;
DE AltName: Full=Laminin-8 subunit beta;
DE Flags: Fragment;
GN Name=LAMB1;
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).
RN [2]
RP INTERACTION WITH ITGB1.
RX PubMed=34427057; DOI=10.1002/jcsm.12767;
RA Luo W., Lin Z., Chen J., Chen G., Zhang S., Liu M., Li H., He D., Liang S.,
RA Luo Q., Zhang D., Nie Q., Zhang X.;
RT "TMEM182 interacts with integrin beta 1 and regulates myoblast
RT differentiation and muscle regeneration.";
RL J. Cachexia Sarcopenia Muscle 12:1704-1723(2021).
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. Beta-1 is a
CC subunit of laminin-1 (laminin-111 or EHS laminin), laminin-2 (laminin-
CC 211 or merosin), laminin-6 (laminin-311 or K-laminin), laminin-8
CC (laminin-411), laminin-10 (laminin-511) and laminin-12 (laminin-213)
CC (By similarity). Interacts with ITGB1 (PubMed:34427057). {ECO:0000250,
CC ECO:0000269|PubMed:34427057}.
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC matrix, basement membrane. Note=Major component.
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DR EMBL; L00962; AAA48935.1; -; mRNA.
DR PIR; B45067; B45067.
DR AlphaFoldDB; Q01635; -.
DR SMR; Q01635; -.
DR STRING; 9031.ENSGALP00000012817; -.
DR VEuPathDB; HostDB:geneid_396478; -.
DR eggNOG; KOG0994; Eukaryota.
DR InParanoid; Q01635; -.
DR OrthoDB; 65841at2759; -.
DR PhylomeDB; Q01635; -.
DR Proteomes; UP000000539; Unplaced.
DR GO; GO:0005604; C:basement membrane; ISS:AgBase.
DR GO; GO:0005615; C:extracellular space; ISS:AgBase.
DR GO; GO:0043256; C:laminin complex; IBA:GO_Central.
DR GO; GO:0005606; C:laminin-1 complex; ISS:AgBase.
DR GO; GO:0043259; C:laminin-10 complex; ISS:AgBase.
DR GO; GO:0005607; C:laminin-2 complex; ISS:AgBase.
DR GO; GO:0043257; C:laminin-8 complex; ISS:AgBase.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISS:AgBase.
DR GO; GO:0005201; F:extracellular matrix structural constituent; ISS:AgBase.
DR GO; GO:0005178; F:integrin binding; IBA:GO_Central.
DR GO; GO:0009887; P:animal organ morphogenesis; IBA:GO_Central.
DR GO; GO:0070831; P:basement membrane assembly; IBA:GO_Central.
DR GO; GO:0016477; P:cell migration; IBA:GO_Central.
DR GO; GO:0007162; P:negative regulation of cell adhesion; ISS:AgBase.
DR GO; GO:0031175; P:neuron projection development; ISS:AgBase.
DR GO; GO:0030335; P:positive regulation of cell migration; ISS:AgBase.
DR GO; GO:0034446; P:substrate adhesion-dependent cell spreading; ISS:AgBase.
DR GO; GO:0009888; P:tissue development; IBA:GO_Central.
DR CDD; cd00055; EGF_Lam; 1.
DR InterPro; IPR008211; Laminin_N.
DR InterPro; IPR002049; LE_dom.
DR Pfam; PF00053; Laminin_EGF; 2.
DR Pfam; PF00055; Laminin_N; 1.
DR SMART; SM00180; EGF_Lam; 1.
DR SMART; SM00136; LamNT; 1.
DR PROSITE; PS00022; EGF_1; 1.
DR PROSITE; PS01248; EGF_LAM_1; 1.
DR PROSITE; PS50027; EGF_LAM_2; 2.
DR PROSITE; PS51117; LAMININ_NTER; 1.
PE 1: Evidence at protein level;
KW Basement membrane; Cell adhesion; Disulfide bond; Extracellular matrix;
KW Glycoprotein; Laminin EGF-like domain; Reference proteome; Repeat;
KW Secreted.
FT CHAIN <1..>303
FT /note="Laminin subunit beta-1"
FT /id="PRO_0000086853"
FT DOMAIN <1..202
FT /note="Laminin N-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00466"
FT DOMAIN 203..266
FT /note="Laminin EGF-like 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DOMAIN 267..>303
FT /note="Laminin EGF-like 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT REGION 202..>303
FT /note="Domain V"
FT /evidence="ECO:0000250"
FT CARBOHYD 52
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 288
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 203..212
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 205..230
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 232..241
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 244..264
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 267..276
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 269..294
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT NON_TER 1
FT NON_TER 303
SQ SEQUENCE 303 AA; 34828 MW; 46985091A82824A4 CRC64;
HLQEDKKCFI CDSEDPFHDT LNPDSHRIEN VVTTFAPNRL KLWWQSENGL ENVTIQLNLE
AEFHFTHLIM TFKTFRPAAM LIERSSDFGK TWQVYRYFAY DCESSFPGIS TGPMKKVDDI
ICDSRYSDIE PSTEGEVIYR VLDPAFRIED PYSPRIQNLL KITNLRVKFT KLHTLGDNLL
DSRMEIREKY YYAIYDMVVR GNCFCYGHAS ECAPVEGFSE EVEGMVHGHC MCRHNTKGLN
CEQCLDFYHD LPWRPAEGRN SNACKKCNCN GHSTQCHFDM AVYMATGNTS GGVCDDCQHN
TGG
