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Database: UniProt
Entry: F1SF45_PIG
LinkDB: F1SF45_PIG
Original site: F1SF45_PIG 
ID   F1SF45_PIG              Unreviewed;      1172 AA.
AC   F1SF45;
DT   03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT   11-DEC-2019, sequence version 4.
DT   27-MAR-2024, entry version 83.
DE   SubName: Full=Laminin subunit beta 3 {ECO:0000313|Ensembl:ENSSSCP00000016558.4};
GN   Name=LAMB3 {ECO:0000313|Ensembl:ENSSSCP00000016558.4,
GN   ECO:0000313|VGNC:VGNC:89622};
OS   Sus scrofa (Pig).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX   NCBI_TaxID=9823 {ECO:0000313|Ensembl:ENSSSCP00000016558.4, ECO:0000313|Proteomes:UP000008227};
RN   [1] {ECO:0000313|Ensembl:ENSSSCP00000016558.4, ECO:0000313|Proteomes:UP000008227}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Duroc {ECO:0000313|Ensembl:ENSSSCP00000016558.4,
RC   ECO:0000313|Proteomes:UP000008227};
RG   Porcine genome sequencing project;
RL   Submitted (NOV-2009) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSSSCP00000016558.4}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00460}.
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DR   AlphaFoldDB; F1SF45; -.
DR   SMR; F1SF45; -.
DR   STRING; 9823.ENSSSCP00000016558; -.
DR   Ensembl; ENSSSCT00000017012.4; ENSSSCP00000016558.4; ENSSSCG00000015618.4.
DR   VGNC; VGNC:89622; LAMB3.
DR   GeneTree; ENSGT00940000160731; -.
DR   HOGENOM; CLU_001560_0_0_1; -.
DR   InParanoid; F1SF45; -.
DR   ChiTaRS; LAMB3; pig.
DR   Proteomes; UP000008227; Chromosome 9.
DR   Bgee; ENSSSCG00000015618; Expressed in lung and 29 other cell types or tissues.
DR   GO; GO:0043256; C:laminin complex; IBA:GO_Central.
DR   GO; GO:0005610; C:laminin-5 complex; IEA:Ensembl.
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:0050873; P:brown fat cell differentiation; IEA:Ensembl.
DR   GO; GO:0016477; P:cell migration; IBA:GO_Central.
DR   GO; GO:0035987; P:endodermal cell differentiation; IEA:Ensembl.
DR   GO; GO:0034446; P:substrate adhesion-dependent cell spreading; IBA:GO_Central.
DR   GO; GO:0009888; P:tissue development; IBA:GO_Central.
DR   CDD; cd22303; cc_LAMB3_C; 1.
DR   CDD; cd00055; EGF_Lam; 6.
DR   Gene3D; 2.60.120.260; Galactose-binding domain-like; 1.
DR   Gene3D; 2.10.25.10; Laminin; 4.
DR   Gene3D; 2.170.300.10; Tie2 ligand-binding domain superfamily; 1.
DR   InterPro; IPR000742; EGF-like_dom.
DR   InterPro; IPR008211; Laminin_N.
DR   InterPro; IPR002049; LE_dom.
DR   PANTHER; PTHR10574:SF268; LAMININ SUBUNIT BETA-3; 1.
DR   PANTHER; PTHR10574; NETRIN/LAMININ-RELATED; 1.
DR   Pfam; PF00053; Laminin_EGF; 6.
DR   Pfam; PF00055; Laminin_N; 1.
DR   PRINTS; PR00011; EGFLAMININ.
DR   SMART; SM00181; EGF; 5.
DR   SMART; SM00180; EGF_Lam; 6.
DR   SMART; SM00136; LamNT; 1.
DR   SUPFAM; SSF57196; EGF/Laminin; 5.
DR   PROSITE; PS00022; EGF_1; 1.
DR   PROSITE; PS01248; EGF_LAM_1; 2.
DR   PROSITE; PS50027; EGF_LAM_2; 6.
DR   PROSITE; PS51117; LAMININ_NTER; 1.
PE   4: Predicted;
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW   ProRule:PRU00460};
KW   Laminin EGF-like domain {ECO:0000256|ARBA:ARBA00023292,
KW   ECO:0000256|PROSITE-ProRule:PRU00460};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008227};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..16
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           17..1172
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5023837191"
FT   DOMAIN          22..249
FT                   /note="Laminin N-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51117"
FT   DOMAIN          250..315
FT                   /note="Laminin EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50027"
FT   DOMAIN          316..378
FT                   /note="Laminin EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50027"
FT   DOMAIN          379..430
FT                   /note="Laminin EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50027"
FT   DOMAIN          431..480
FT                   /note="Laminin EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50027"
FT   DOMAIN          481..533
FT                   /note="Laminin EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50027"
FT   DOMAIN          534..580
FT                   /note="Laminin EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50027"
FT   COILED          846..873
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          1043..1070
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   DISULFID        281..290
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT   DISULFID        346..355
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT   DISULFID        401..410
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT   DISULFID        453..462
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT   DISULFID        481..493
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT   DISULFID        483..500
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT   DISULFID        502..511
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT   DISULFID        534..546
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT   DISULFID        536..553
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT   DISULFID        555..564
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
SQ   SEQUENCE   1172 AA;  129091 MW;  1647ED22D07DF5F5 CRC64;
     MRLLLLLCFV LNSVLCTQQA CSRGACYPPV GDLLIGRTRF LRASSTCGLT KPETYCTQYD
     EWKMKCCKCD SRLPHNYNSH RVENVISSSG PMRWWQSQND VNPVSLQLDL DSKFQLQAIT
     MDFKGPMPAG LLIERSSDFG KTWRVYQYLA ADCTSAFPRV RQGQPQSWQD ARCQPLPQRP
     DGRLDGAKVQ LKLMDLASGI QASQSQKIQE LGEITNLRVN FTRLAPLPQR GRHPPSAYYA
     VSQLRLQGSC FCHGHADRCA PNPRAPAGPS TSVQVHEVCV CQHNTAGPNC ERCAPFYNNQ
     PWSPAHDQDP HECQRCDCNG HSETCHFDPA VFAASQGTQG GVCDNCRDHT EGKNCERCQL
     HYFRNRRPGA PIQETCIPCE CDPDGAVPGA PCDPVTGQCV CKEHVQGERC DLCKPGFTGL
     TYANPQGCHR CDCSVLGARR DMPCDEESGR CLCLPHVVGP KCDQCAPHHW KLASGRGCEP
     CACDPHNSLS PQCNQFTGQC PCREGFGGLT CSTAAIRLCP DRTYEDVATG CRACDCDFRG
     TEGPGCDKAS GRCLCRPGLT GPRCDQCQRG YCDRYPVCVA CHPCFQTYDA GLQERALRLR
     SLGNATASLR PGLGFEDLSL ASQMQDAKSK MEQIQAVLGG AVVTEREVAQ VAKAIFSLRQ
     TLQALQPDLL PEEKTFLLPG DLENLDRNLN RLLVLYQSKK EQFEKISTAD PSGAFRMLSA
     AYQRSSQATQ KVSDSSRLLL RLRDGRREAE GLVQQVVREA GAGGPQLVAL KLEMASLPDL
     TSAINKLCGG SRQTPCTAGA CPGELCPRDN GTTCGSQCKG ALPRAGGAFR TAGQVAEQLR
     GFNVQLQQTR QMIQAVEEAA SKVQADARRL ETQVSTSRTR MEEDVSRTQF LIQQVRDFLS
     DPDTDAATIQ EVSEAVLALW LPTDSATVLR KMNEIQAIAA RLPNVDLVLS QTKQDIARAH
     RLQAEAEQAR SRAHAAEGQL EDVVGNLQQG TVALQEAQDT MHGTRRSLQL IQDRVAEVQQ
     VLGPAERLVM DRMEQLGGLR ARMEELSLQA RLQQAQAAQA RQLAEEASEQ ALSAQEGFER
     IKQKYAELKD RLGRSPRLGE QGGRILSVKM EAEELFGEAV AMMDRMKDME SELLRGSQAI
     LLRSADLTGL EKHVEQIRSY INERVLYYAT CK
//
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