ID   LAMB3_MOUSE             Reviewed;        1168 AA.
AC   Q61087; Q91V90;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   27-JUL-2011, sequence version 2.
DT   27-MAR-2024, entry version 184.
DE   RecName: Full=Laminin subunit beta-3;
DE   AltName: Full=Epiligrin subunit bata;
DE   AltName: Full=Kalinin B1 chain;
DE   AltName: Full=Kalinin subunit beta;
DE   AltName: Full=Laminin-5 subunit beta;
DE   AltName: Full=Nicein subunit beta;
DE   Flags: Precursor;
GN   Name=Lamb3;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=FVB/NJ; TISSUE=Lung;
RX   PubMed=7898049;
RA   Utani A., Kopp J.B., Kozak C.A., Matsuki Y., Amizuka N., Sugiyama S.,
RA   Yamada Y.;
RT   "Mouse kalinin B1 (laminin beta 3 chain): cloning and tissue
RT   distribution.";
RL   Lab. Invest. 72:300-310(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA   Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA   Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA   Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA   Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA   Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA   Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA   Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA   Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA   Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA   Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA   Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA   Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA   Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA   Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA   Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA   Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA   Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA   Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA   Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA   van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA   Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA   Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA   Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA   Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA   Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA   Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA   Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA   Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N; TISSUE=Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [5]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Lung;
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL   Cell 143:1174-1189(2010).
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-3 is a
CC       subunit of laminin-5 (laminin-332 or epiligrin/kalinin/nicein).
CC       Interacts with ECM1 (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC       matrix, basement membrane.
CC   -!- TISSUE SPECIFICITY: Found in the basement membranes (major component).
CC   -!- DOMAIN: The alpha-helical domains I and II are thought to interact with
CC       other laminin chains to form a coiled coil structure.
CC   -!- DOMAIN: Domain VI is globular.
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DR   EMBL; U43298; AAA85255.1; -; mRNA.
DR   EMBL; AK155769; BAE33428.1; -; mRNA.
DR   EMBL; CH466555; EDL12945.1; -; Genomic_DNA.
DR   EMBL; CH466555; EDL12946.1; -; Genomic_DNA.
DR   EMBL; BC008516; AAH08516.1; -; mRNA.
DR   CCDS; CCDS15637.1; -.
DR   RefSeq; NP_001264857.1; NM_001277928.1.
DR   RefSeq; NP_032510.2; NM_008484.2.
DR   RefSeq; XP_006497295.1; XM_006497232.1.
DR   RefSeq; XP_006497296.1; XM_006497233.2.
DR   AlphaFoldDB; Q61087; -.
DR   SMR; Q61087; -.
DR   BioGRID; 201103; 3.
DR   ComplexPortal; CPX-3012; Laminin-332 complex variant A.
DR   ComplexPortal; CPX-3164; Laminin-332 complex variant B.
DR   STRING; 10090.ENSMUSP00000142053; -.
DR   GlyCosmos; Q61087; 3 sites, No reported glycans.
DR   GlyGen; Q61087; 3 sites.
DR   iPTMnet; Q61087; -.
DR   PhosphoSitePlus; Q61087; -.
DR   MaxQB; Q61087; -.
DR   PaxDb; 10090-ENSMUSP00000016315; -.
DR   PeptideAtlas; Q61087; -.
DR   ProteomicsDB; 264831; -.
DR   Antibodypedia; 1958; 423 antibodies from 28 providers.
DR   DNASU; 16780; -.
DR   Ensembl; ENSMUST00000016315.16; ENSMUSP00000016315.10; ENSMUSG00000026639.19.
DR   Ensembl; ENSMUST00000159955.2; ENSMUSP00000123875.2; ENSMUSG00000026639.19.
DR   Ensembl; ENSMUST00000194677.6; ENSMUSP00000142053.2; ENSMUSG00000026639.19.
DR   GeneID; 16780; -.
DR   KEGG; mmu:16780; -.
DR   UCSC; uc007eee.1; mouse.
DR   AGR; MGI:99915; -.
DR   CTD; 3914; -.
DR   MGI; MGI:99915; Lamb3.
DR   VEuPathDB; HostDB:ENSMUSG00000026639; -.
DR   eggNOG; KOG0994; Eukaryota.
DR   GeneTree; ENSGT00940000160731; -.
DR   HOGENOM; CLU_001560_0_0_1; -.
DR   InParanoid; Q61087; -.
DR   OMA; RCLCLPH; -.
DR   OrthoDB; 90222at2759; -.
DR   PhylomeDB; Q61087; -.
DR   TreeFam; TF352481; -.
DR   BioGRID-ORCS; 16780; 1 hit in 80 CRISPR screens.
DR   ChiTaRS; Lamb3; mouse.
DR   PRO; PR:Q61087; -.
DR   Proteomes; UP000000589; Chromosome 1.
DR   RNAct; Q61087; Protein.
DR   Bgee; ENSMUSG00000026639; Expressed in molar tooth and 148 other cell types or tissues.
DR   ExpressionAtlas; Q61087; baseline and differential.
DR   GO; GO:0005604; C:basement membrane; IDA:MGI.
DR   GO; GO:0062023; C:collagen-containing extracellular matrix; HDA:BHF-UCL.
DR   GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR   GO; GO:0043256; C:laminin complex; IBA:GO_Central.
DR   GO; GO:0005610; C:laminin-5 complex; IDA:MGI.
DR   GO; GO:0044877; F:protein-containing complex binding; ISO:MGI.
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; IDA:MGI.
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; 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; 1.10.287.950; Methyl-accepting chemotaxis protein; 1.
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; 4.
DR   SMART; SM00180; EGF_Lam; 6.
DR   SMART; SM00136; LamNT; 1.
DR   SUPFAM; SSF57196; EGF/Laminin; 5.
DR   PROSITE; PS00022; EGF_1; 5.
DR   PROSITE; PS01186; EGF_2; 2.
DR   PROSITE; PS01248; EGF_LAM_1; 4.
DR   PROSITE; PS50027; EGF_LAM_2; 6.
DR   PROSITE; PS51117; LAMININ_NTER; 1.
DR   Genevisible; Q61087; MM.
PE   1: Evidence at protein level;
KW   Basement membrane; Cell adhesion; Coiled coil; Disulfide bond;
KW   Extracellular matrix; Glycoprotein; Laminin EGF-like domain;
KW   Reference proteome; Repeat; Secreted; Signal.
FT   SIGNAL          1..17
FT                   /evidence="ECO:0000255"
FT   CHAIN           18..1168
FT                   /note="Laminin subunit beta-3"
FT                   /id="PRO_0000017072"
FT   DOMAIN          22..249
FT                   /note="Laminin N-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00466"
FT   DOMAIN          250..312
FT                   /note="Laminin EGF-like 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT   DOMAIN          313..375
FT                   /note="Laminin EGF-like 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT   DOMAIN          376..427
FT                   /note="Laminin EGF-like 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT   DOMAIN          428..477
FT                   /note="Laminin EGF-like 4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT   DOMAIN          478..530
FT                   /note="Laminin EGF-like 5"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT   DOMAIN          531..577
FT                   /note="Laminin EGF-like 6"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT   REGION          576..781
FT                   /note="Domain II"
FT   REGION          723..760
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          782..812
FT                   /note="Domain alpha"
FT   REGION          813..1168
FT                   /note="Domain I"
FT   COILED          732..754
FT                   /evidence="ECO:0000255"
FT   COILED          827..879
FT                   /evidence="ECO:0000255"
FT   COILED          944..1129
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        723..737
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        220
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        601
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        806
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        250..259
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT   DISULFID        252..276
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT   DISULFID        278..287
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT   DISULFID        290..310
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT   DISULFID        313..322
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT   DISULFID        315..340
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT   DISULFID        343..352
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT   DISULFID        355..373
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT   DISULFID        376..389
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT   DISULFID        378..396
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT   DISULFID        398..407
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT   DISULFID        410..425
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT   DISULFID        428..441
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT   DISULFID        430..448
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT   DISULFID        450..459
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT   DISULFID        462..475
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT   DISULFID        478..490
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT   DISULFID        480..497
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT   DISULFID        499..508
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT   DISULFID        516..528
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT   DISULFID        531..543
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT   DISULFID        533..550
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT   DISULFID        552..561
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT   DISULFID        564..575
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT   DISULFID        578
FT                   /note="Interchain"
FT                   /evidence="ECO:0000305"
FT   DISULFID        581
FT                   /note="Interchain"
FT                   /evidence="ECO:0000305"
FT   DISULFID        1167
FT                   /note="Interchain"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        34
FT                   /note="L -> F (in Ref. 1; AAA85255)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        271
FT                   /note="Q -> R (in Ref. 1; AAA85255)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        284
FT                   /note="G -> A (in Ref. 1; AAA85255)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        320
FT                   /note="E -> L (in Ref. 1; AAA85255)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        354
FT                   /note="R -> P (in Ref. 1; AAA85255)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        361
FT                   /note="R -> W (in Ref. 1; AAA85255)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        420
FT                   /note="A -> D (in Ref. 1; AAA85255)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        525
FT                   /note="A -> P (in Ref. 1; AAA85255)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        542
FT                   /note="G -> A (in Ref. 1; AAA85255)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        646
FT                   /note="A -> P (in Ref. 1; AAA85255)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1079
FT                   /note="Q -> P (in Ref. 1; AAA85255)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1115
FT                   /note="T -> S (in Ref. 1; AAA85255)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   1168 AA;  128900 MW;  66EB2BE1AA232215 CRC64;
     MTAFFLLWLA LPGFLCAQQA CSRGACYPPV GDLLIGRTQL LRASSTCGLT KPETYCTQYG
     QWQMKCCKCD SRLPRNYNSH RVENVASSSG PMRWWQSQND VSPVSLQLDL DKRMQLQDIM
     MDFKGLTPAG MLIERSSDFG KTWRVYQYLA TDCASTFPQV HQGQPKNWQD VRCRPLSQRP
     NGHLTGGKVQ LNLMDLASAI PASQSKKIQE LGDITNLRVN FTKLAPVPQR GSYPPSAYFA
     VSQLRLQGSC FCHGHADRCA PNPGGSTTAV QVNNVCVCQH NTAGPNCDRC APFYNNRPWR
     PAEGQDTHEC QRCDCNGHSE TCHFDPAVFA ASQGTNGGVC DNCRDHTEGK NCERCQLHYF
     RNRRPSAPIH ETCIPCECDP DGAVQGAPCD RLTGQCVCKE YVQGERCDLC KPGFTGLTFA
     NPKGCHACDC SILGARKDMP CEEETGRCLC LPNVVGPKCD QCAPSHWKLA SGLGCEPCAC
     DPRNSLSSQC NQFTGQCPCR EGFGGLTCSS AAIRQCPDQT YGHVATGCRA CDCDFRGTEG
     PGCDKASGRC LCRPGFTGPR CDQCQRGHCD RYPVCVACHS CFQAYDTDLQ EQARRLHSLR
     NATEGLWTGT GLEDHGLASR LLDAKSKIEQ IRQILEGTSV TEQDVAQVAN GILSIRRTLQ
     GLPLDLPLEE EMESFSGDLG NLDRSFSRLL LMYRSKKEQF EKLSSEDPSG AFRMLTMAYE
     QSSRAAQQVS DSSSLLSQLR DSRREAEGLE RQAGGGGTGG AQLMALRLEM ASLPDLTPTI
     NKLCGRSRQT ACTPGDCPGE LCPQDNGTAC GSHCRGALPR AKGAFHMAGR VAEQLRNFNT
     QLQQTRQMIR AAEEAASRVQ ADAQRLETQV STSRLLMEED VQRTRLLIQQ VRGFLTDPDT
     DAATIQQVSE AVLALWLPTD SATVLRKMKE IQAIAARLPN VDSVLSQTKQ DIARARRLQA
     EAEQARSRAH AVEGQVDDVV GNLRQGTVAL QEAQDTMQGT GRSLRLIQER VGEVQQVLVP
     AERLVKGMKE QMSGFWARMK ELRRQAQEEQ AQAMQARQLA EGASQQAMNA QEGFKRLKQK
     YTELKDRLGQ SPVLGEQGNR ILSIKMEAEE LFGETMEMMD KMKDMESELL RGSQAIMLRS
     ADLSGLEKRV EQIRSYINGR VLYYATCK
//