ID   LAMB2_MOUSE             Reviewed;        1799 AA.
AC   Q61292; Q62182; Q8R0Y0;
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-2;
DE   AltName: Full=Laminin-11 subunit beta;
DE   AltName: Full=Laminin-14 subunit beta;
DE   AltName: Full=Laminin-15 subunit beta;
DE   AltName: Full=Laminin-3 subunit beta;
DE   AltName: Full=Laminin-4 subunit beta;
DE   AltName: Full=Laminin-7 subunit beta;
DE   AltName: Full=Laminin-9 subunit beta;
DE   AltName: Full=S-laminin subunit beta;
DE            Short=S-LAM beta;
DE   Flags: Precursor;
GN   Name=Lamb2; Synonyms=Lams;
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 [GENOMIC DNA].
RC   STRAIN=129/J;
RX   PubMed=8662701; DOI=10.1074/jbc.271.23.13407;
RA   Durkin M.E., Gautam M., Loechel S., Sanes J.R., Merlie J.P.,
RA   Albrechtsen R., Wewer U.M.;
RT   "Structural organization of the human and mouse laminin beta2 chain genes,
RT   and alternative splicing at the 5' end of the human transcript.";
RL   J. Biol. Chem. 271:13407-13416(1996).
RN   [2]
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 (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [3]
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   [4]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 348-428.
RC   TISSUE=Lung;
RX   PubMed=8043959; DOI=10.1007/bf00356563;
RA   Aberdam D., Galliano M.-F., Mattei M.-G., Ortonne J.-P., Meneguzzi G.;
RT   "S-laminin gene (Lams) maps to F1 band of mouse chromosome 9.";
RL   Mamm. Genome 5:393-394(1994).
RN   [5]
RP   FUNCTION.
RC   STRAIN=129/J;
RX   PubMed=7885444; DOI=10.1038/374258a0;
RA   Noakes P.G., Gautam M., Mudd J., Sanes J.R., Merlie J.P.;
RT   "Aberrant differentiation of neuromuscular junctions in mice lacking s-
RT   laminin/laminin beta 2.";
RL   Nature 374:258-262(1995).
RN   [6]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Lung, Pancreas,
RC   Spleen, and Testis;
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. {ECO:0000269|PubMed:7885444}.
CC   -!- FUNCTION: Laminin-3 (S-laminin) regulates the formation of motor nerve
CC       terminals. {ECO:0000269|PubMed:7885444}.
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-2 is a
CC       subunit of laminin-3 (laminin-121 or S-laminin), laminin-4 (laminin-221
CC       or S-merosin), laminin-7 (laminin-321 or KS-laminin), laminin-9
CC       (laminin-421), laminin-11 (laminin-521), laminin-14 (laminin-423) and
CC       laminin-15 (laminin-523).
CC   -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC       matrix, basement membrane.
CC   -!- TISSUE SPECIFICITY: Neuromuscular synapse and kidney glomerulus.
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: Domains VI and IV are globular.
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DR   EMBL; U43541; AAC53535.1; -; Genomic_DNA.
DR   EMBL; U42624; AAC53535.1; JOINED; Genomic_DNA.
DR   EMBL; CH466560; EDL21291.1; -; Genomic_DNA.
DR   EMBL; CH466560; EDL21292.1; -; Genomic_DNA.
DR   EMBL; BC026051; AAH26051.1; -; mRNA.
DR   EMBL; X75928; CAA53532.1; -; mRNA.
DR   CCDS; CCDS23528.1; -.
DR   PIR; I48749; I48749.
DR   RefSeq; NP_032509.2; NM_008483.3.
DR   RefSeq; XP_006511711.1; XM_006511648.2.
DR   AlphaFoldDB; Q61292; -.
DR   SMR; Q61292; -.
DR   BioGRID; 201102; 9.
DR   ComplexPortal; CPX-3010; Laminin-121 complex.
DR   ComplexPortal; CPX-3011; Laminin-221 complex.
DR   ComplexPortal; CPX-3014; Laminin-321 complex.
DR   ComplexPortal; CPX-3017; Laminin-521 complex.
DR   ComplexPortal; CPX-3019; Laminin-423 complex.
DR   ComplexPortal; CPX-3020; Laminin-522 complex.
DR   ComplexPortal; CPX-3021; Laminin-523 complex.
DR   ComplexPortal; CPX-3031; Laminin-421 complex.
DR   IntAct; Q61292; 1.
DR   MINT; Q61292; -.
DR   STRING; 10090.ENSMUSP00000069087; -.
DR   GlyConnect; 2460; 8 N-Linked glycans (1 site).
DR   GlyCosmos; Q61292; 7 sites, 7 glycans.
DR   GlyGen; Q61292; 8 sites, 7 N-linked glycans (1 site), 1 O-linked glycan (1 site).
DR   iPTMnet; Q61292; -.
DR   PhosphoSitePlus; Q61292; -.
DR   SwissPalm; Q61292; -.
DR   MaxQB; Q61292; -.
DR   PaxDb; 10090-ENSMUSP00000069087; -.
DR   PeptideAtlas; Q61292; -.
DR   ProteomicsDB; 263696; -.
DR   Pumba; Q61292; -.
DR   Antibodypedia; 995; 428 antibodies from 30 providers.
DR   DNASU; 16779; -.
DR   Ensembl; ENSMUST00000065014.10; ENSMUSP00000069087.5; ENSMUSG00000052911.10.
DR   GeneID; 16779; -.
DR   KEGG; mmu:16779; -.
DR   UCSC; uc009rpr.2; mouse.
DR   AGR; MGI:99916; -.
DR   CTD; 3913; -.
DR   MGI; MGI:99916; Lamb2.
DR   VEuPathDB; HostDB:ENSMUSG00000052911; -.
DR   eggNOG; KOG0994; Eukaryota.
DR   GeneTree; ENSGT00940000156060; -.
DR   HOGENOM; CLU_001560_1_0_1; -.
DR   InParanoid; Q61292; -.
DR   OMA; SCRDHTG; -.
DR   OrthoDB; 90222at2759; -.
DR   PhylomeDB; Q61292; -.
DR   TreeFam; TF312903; -.
DR   BioGRID-ORCS; 16779; 1 hit in 76 CRISPR screens.
DR   ChiTaRS; Lamb2; mouse.
DR   PRO; PR:Q61292; -.
DR   Proteomes; UP000000589; Chromosome 9.
DR   RNAct; Q61292; Protein.
DR   Bgee; ENSMUSG00000052911; Expressed in humerus cartilage element and 254 other cell types or tissues.
DR   ExpressionAtlas; Q61292; baseline and differential.
DR   GO; GO:0005604; C:basement membrane; IDA:UniProtKB.
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; IDA:MGI.
DR   GO; GO:0005608; C:laminin-3 complex; IDA:MGI.
DR   GO; GO:0031594; C:neuromuscular junction; IDA:SynGO.
DR   GO; GO:0098637; C:protein complex involved in cell-matrix adhesion; NAS:ComplexPortal.
DR   GO; GO:0045202; C:synapse; IDA:MGI.
DR   GO; GO:0043083; C:synaptic cleft; IDA:SynGO.
DR   GO; GO:0005178; F:integrin binding; IPI:MGI.
DR   GO; GO:0150043; F:structural constituent of synapse-associated extracellular matrix; IDA:SynGO.
DR   GO; GO:0009887; P:animal organ morphogenesis; IBA:GO_Central.
DR   GO; GO:0014002; P:astrocyte development; IGI:MGI.
DR   GO; GO:0048677; P:axon extension involved in regeneration; IMP:MGI.
DR   GO; GO:0007411; P:axon guidance; IGI:MGI.
DR   GO; GO:0070831; P:basement membrane assembly; IBA:GO_Central.
DR   GO; GO:0016477; P:cell migration; IBA:GO_Central.
DR   GO; GO:0000902; P:cell morphogenesis; IGI:MGI.
DR   GO; GO:0072274; P:metanephric glomerular basement membrane development; IMP:MGI.
DR   GO; GO:0072249; P:metanephric podocyte development; IMP:MGI.
DR   GO; GO:0007528; P:neuromuscular junction development; IMP:MGI.
DR   GO; GO:0031175; P:neuron projection development; IDA:MGI.
DR   GO; GO:0045785; P:positive regulation of cell adhesion; NAS:ComplexPortal.
DR   GO; GO:2001046; P:positive regulation of integrin-mediated signaling pathway; NAS:ComplexPortal.
DR   GO; GO:0051149; P:positive regulation of muscle cell differentiation; NAS:ComplexPortal.
DR   GO; GO:0110011; P:regulation of basement membrane organization; NAS:ComplexPortal.
DR   GO; GO:0060041; P:retina development in camera-type eye; IGI:MGI.
DR   GO; GO:0014044; P:Schwann cell development; IDA:MGI.
DR   GO; GO:0034446; P:substrate adhesion-dependent cell spreading; IBA:GO_Central.
DR   GO; GO:0050808; P:synapse organization; IMP:MGI.
DR   GO; GO:0009888; P:tissue development; IBA:GO_Central.
DR   GO; GO:0007601; P:visual perception; IGI:MGI.
DR   CDD; cd22299; cc_LAMB2_C; 1.
DR   CDD; cd00055; EGF_Lam; 13.
DR   Gene3D; 2.60.120.260; Galactose-binding domain-like; 1.
DR   Gene3D; 2.10.25.10; Laminin; 9.
DR   Gene3D; 2.170.300.10; Tie2 ligand-binding domain superfamily; 2.
DR   InterPro; IPR000742; EGF-like_dom.
DR   InterPro; IPR013015; Laminin_IV_B.
DR   InterPro; IPR008211; Laminin_N.
DR   InterPro; IPR002049; LE_dom.
DR   PANTHER; PTHR10574:SF435; LAMININ SUBUNIT GAMMA-1; 1.
DR   PANTHER; PTHR10574; NETRIN/LAMININ-RELATED; 1.
DR   Pfam; PF00053; Laminin_EGF; 13.
DR   Pfam; PF21199; LAMININ_IV_B; 1.
DR   Pfam; PF00055; Laminin_N; 1.
DR   PRINTS; PR00011; EGFLAMININ.
DR   SMART; SM00181; EGF; 8.
DR   SMART; SM00180; EGF_Lam; 13.
DR   SMART; SM00136; LamNT; 1.
DR   SUPFAM; SSF57196; EGF/Laminin; 13.
DR   PROSITE; PS00022; EGF_1; 10.
DR   PROSITE; PS01186; EGF_2; 2.
DR   PROSITE; PS01248; EGF_LAM_1; 12.
DR   PROSITE; PS50027; EGF_LAM_2; 13.
DR   PROSITE; PS51116; LAMININ_IVB; 1.
DR   PROSITE; PS51117; LAMININ_NTER; 1.
DR   Genevisible; Q61292; 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   Phosphoprotein; Reference proteome; Repeat; Secreted; Signal.
FT   SIGNAL          1..35
FT                   /evidence="ECO:0000255"
FT   CHAIN           36..1799
FT                   /note="Laminin subunit beta-2"
FT                   /id="PRO_0000017069"
FT   DOMAIN          46..285
FT                   /note="Laminin N-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00466"
FT   DOMAIN          286..349
FT                   /note="Laminin EGF-like 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT   DOMAIN          350..412
FT                   /note="Laminin EGF-like 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT   DOMAIN          413..472
FT                   /note="Laminin EGF-like 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT   DOMAIN          473..524
FT                   /note="Laminin EGF-like 4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT   DOMAIN          525..555
FT                   /note="Laminin EGF-like 5; truncated"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT   DOMAIN          564..778
FT                   /note="Laminin IV type B"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00462"
FT   DOMAIN          784..831
FT                   /note="Laminin EGF-like 6"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT   DOMAIN          832..877
FT                   /note="Laminin EGF-like 7"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT   DOMAIN          878..927
FT                   /note="Laminin EGF-like 8"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT   DOMAIN          928..986
FT                   /note="Laminin EGF-like 9"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT   DOMAIN          987..1038
FT                   /note="Laminin EGF-like 10"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT   DOMAIN          1039..1095
FT                   /note="Laminin EGF-like 11"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT   DOMAIN          1096..1143
FT                   /note="Laminin EGF-like 12"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT   DOMAIN          1144..1190
FT                   /note="Laminin EGF-like 13"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT   REGION          1191..1410
FT                   /note="Domain II"
FT   REGION          1339..1365
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1411..1443
FT                   /note="Domain alpha"
FT   REGION          1444..1799
FT                   /note="Domain I"
FT   REGION          1679..1701
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          1257..1304
FT                   /evidence="ECO:0000255"
FT   COILED          1473..1527
FT                   /evidence="ECO:0000255"
FT   COILED          1577..1791
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        1344..1365
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         1533
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P55268"
FT   CARBOHYD        251
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        371
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        1086
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        1250
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        1309
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        1349
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        1500
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        286..295
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT   DISULFID        288..313
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT   DISULFID        315..324
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT   DISULFID        327..347
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT   DISULFID        350..359
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT   DISULFID        352..377
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT   DISULFID        380..389
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT   DISULFID        392..410
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT   DISULFID        413..426
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT   DISULFID        415..441
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT   DISULFID        443..452
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT   DISULFID        455..470
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT   DISULFID        473..487
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT   DISULFID        475..494
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT   DISULFID        496..505
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT   DISULFID        508..522
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT   DISULFID        525..537
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT   DISULFID        527..544
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT   DISULFID        546..555
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT   DISULFID        784..796
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT   DISULFID        786..803
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT   DISULFID        805..814
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT   DISULFID        817..829
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT   DISULFID        832..844
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT   DISULFID        834..851
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT   DISULFID        853..862
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT   DISULFID        865..875
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT   DISULFID        878..887
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT   DISULFID        880..894
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT   DISULFID        897..906
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT   DISULFID        909..925
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT   DISULFID        928..944
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT   DISULFID        930..955
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT   DISULFID        957..966
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT   DISULFID        969..984
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT   DISULFID        987..1001
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT   DISULFID        989..1008
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT   DISULFID        1011..1020
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT   DISULFID        1023..1036
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT   DISULFID        1039..1059
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT   DISULFID        1041..1066
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT   DISULFID        1068..1077
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT   DISULFID        1080..1093
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT   DISULFID        1096..1108
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT   DISULFID        1098..1115
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT   DISULFID        1117..1126
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT   DISULFID        1129..1141
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT   DISULFID        1144..1156
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT   DISULFID        1146..1163
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT   DISULFID        1165..1174
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT   DISULFID        1177..1188
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT   DISULFID        1191
FT                   /note="Interchain"
FT                   /evidence="ECO:0000305"
FT   DISULFID        1194
FT                   /note="Interchain"
FT                   /evidence="ECO:0000305"
FT   DISULFID        1798
FT                   /note="Interchain"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        545
FT                   /note="R -> P (in Ref. 1; AAC53535)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        581
FT                   /note="G -> V (in Ref. 1; AAC53535)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        677
FT                   /note="F -> V (in Ref. 1; AAC53535)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        956
FT                   /note="Q -> H (in Ref. 1; AAC53535)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        959
FT                   /note="E -> A (in Ref. 1; AAC53535)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        973
FT                   /note="H -> P (in Ref. 1; AAC53535)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1306
FT                   /note="L -> F (in Ref. 1; AAC53535)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1449
FT                   /note="T -> P (in Ref. 1; AAC53535)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1460
FT                   /note="T -> S (in Ref. 1; AAC53535)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1487
FT                   /note="E -> A (in Ref. 1; AAC53535)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1627
FT                   /note="W -> R (in Ref. 1; AAC53535)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   1799 AA;  196579 MW;  37CA24B9CDA0791F CRC64;
     MEWASGEPGR GRQGQPLPWE LRLGLLLSVL AATLAQAPSL DVPGCSRGSC YPATGDLLVG
     RADRLTASST CGLHSPQPYC IVSHLQDEKK CFLCDSRRPF SARDNPNSHR IQNVVTSFAP
     QRRTAWWQSE NGVPMVTIQL DLEAEFHFTH LIMTFKTFRP AAMLVERSAD FGRTWHVYRY
     FSYDCGADFP GIPLAPPRRW DDVVCESRYS EIEPSTEGEV IYRVLDPAIP IPDPYSSRIQ
     NLLKITNLRV NLTRLHTLGD NLLDPRREIR EKYYYALYEL VIRGNCFCYG HASQCAPAPG
     APAHAEGMVH GACICKHNTR GLNCEQCQDF YQDLPWHPAE DGHTHACRKC ECNGHTHSCH
     FDMAVYLASG NVSGGVCDGC QHNTAGRHCE FCRPFFYRDP TKDMRDPAVC RPCDCDPMGS
     QDGGRCDSHD DPVLGLVSGQ CRCKEHVVGT RCQQCRDGFF GLSASDPRGC QRCQCNSRGT
     VPGSSPCDSS SGTCFCKRLV TGHGCDRCLP GHWGLSHDLL GCRPCDCDVG GALDPQCDEA
     TGQCRCRQHM IGRRCEQVQP GYFRPFLDHL TWEAEAAQGQ GLEVVERLVT NRETPSWTGP
     GFVRLREGQE VEFLVTSLPR AMDYDLLLRW EPQVPEQWAE LELMVQRPGP VSAHSPCGHV
     LPKDDRIQGM LHPNTRFLVF PRPVCLEPGI SYKLKLKLIG TGGRAQPETS YSGLLIDSLV
     LQPHVLVLEM FSGGDAAALE RRTTFERYRC HEEGLMPSKA PLSETCAPLL ISVSALIYNG
     ALPCQCDPQG SLSSECSPHG GQCRCKPGVV GRRCDVCATG YYGFGPAGCQ ACQCSPDGAL
     SALCEGTSGQ CPCRPGAFGL RCDHCQRGQW GFPNCRPCVC NGRADECDTH TGACLGCRDY
     TGGEHCERCI AGFHGDPRLP YGGQCRPCPC PEGPGSQRHF ATSCHRDGYS QQIVCQCREG
     YTGLRCEACA PGHFGDPSKP GGRCQLCECS GNIDPMDPDA CDPHTGQCLR CLHNTEGPHC
     GYCKPGFHGQ AARQSCHRCT CNLLGTDPRR CPSTDLCHCD PSTGQCPCLP HVQGLNCDHC
     APNFWNFTSG RGCQPCACHP SRARGPTCNE FTGQCHCHAG FGGRTCSECQ ELYWGDPGLQ
     CRACDCDPRG IDKPQCHRST GHCSCRPGVS GVRCDQCARG FSGVFPACHP CHACFGDWDR
     VVQDLAARTR RLEQWAQELQ QTGVLGAFES SFLNMQGKLG MVQAIMSARN ASAASTAKLV
     EATEGLRHEI GKTTERLTQL EAELTAVQDE NFNANHALSG LERDGLALNL TLRQLDQHLE
     ILKHSNFLGA YDSIRHAHSQ STEAERRANA STFAVPSPVS NSADTRRRTE VLMGAQKENF
     NRQHLANQQA LGRLSAHAHT LSLTGINELV CGAPGDAPCA TSPCGGAGCR DEDGQPRCGG
     LGCSGAAATA DLALGRARHT QAELQRALVE GGGILSRVSE TRRQAEEAQQ RAQAALDKAN
     ASRGQVEQAN QELRELIQNV KDFLSQEGAD PDSIEMVATR VLDISIPASP EQIQRLASEI
     AERVRSLADV DTILAHTMGD VRRAEQLLQD AHRARSRAEG ERQKAETVQA ALEEAQRAQG
     AAQGAIWGAV VDTQNTEQTL QRVQERMAGA EKSLNSAGER ARQLDALLEA LKLKRAGNSL
     AASTAEETAG SAQSRAREAE KQLREQVGDQ YQTVRALAER KAEGVLAAQA RAEQLRDEAR
     DLLQAAQDKL QRLQELEGTY EENERALEGK AAQLDGLEAR MRSVLQAINL QVQIYNTCQ
//