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Database: UniProt
Entry: LAMA3_MOUSE
LinkDB: LAMA3_MOUSE
Original site: LAMA3_MOUSE 
ID   LAMA3_MOUSE             Reviewed;        3330 AA.
AC   Q61789; E9PUR4; O08751; Q61788; Q61966; Q9JHQ7;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   16-OCT-2013, sequence version 4.
DT   05-JUN-2019, entry version 180.
DE   RecName: Full=Laminin subunit alpha-3;
DE   AltName: Full=Epiligrin subunit alpha;
DE   AltName: Full=Kalinin subunit alpha;
DE   AltName: Full=Laminin-5 subunit alpha;
DE   AltName: Full=Laminin-6 subunit alpha;
DE   AltName: Full=Laminin-7 subunit alpha;
DE   AltName: Full=Nicein subunit alpha;
DE   Flags: Precursor;
GN   Name=Lama3;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A), AND NUCLEOTIDE SEQUENCE [MRNA]
RP   OF 765-3330 (ISOFORM B).
RC   STRAIN=BALB/cJ; TISSUE=Lung;
RX   PubMed=7665604; DOI=10.1074/jbc.270.37.21820;
RA   Galliano M.-F., Aberdam D., Aguzzi A., Ortonne J.-P., Meneguzzi G.;
RT   "Cloning and complete primary structure of the mouse laminin alpha 3
RT   chain. Distinct expression pattern of the laminin alpha 3A and alpha
RT   3B chain isoforms.";
RL   J. Biol. Chem. 270:21820-21826(1995).
RN   [2]
RP   SEQUENCE REVISION.
RA   Aberdam D.;
RL   Submitted (APR-1997) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 1-58 (ISOFORM B), AND PROTEIN SEQUENCE
RP   OF 32-38.
RX   PubMed=11829758; DOI=10.1042/0264-6021:3620213;
RA   Garbe J.H., Gohring W., Mann K., Timpl R., Sasaki T.;
RT   "Complete sequence, recombinant analysis and binding to laminins and
RT   sulphated ligands of the N-terminal domains of laminin alpha3B and
RT   alpha5 chains.";
RL   Biochem. J. 362:213-221(2002).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 50-776 (ISOFORM B).
RC   STRAIN=ICR;
RX   PubMed=9151674; DOI=10.1083/jcb.137.3.685;
RA   Miner J.H., Patton B.L., Lentz S.I., Gilbert D.J., Snider W.D.,
RA   Jenkins N.A., Copeland N.G., Sanes J.R.;
RT   "The laminin alpha chains: expression, developmental transitions, and
RT   chromosomal locations of alpha1-5, identification of heterotrimeric
RT   laminins 8-11, and cloning of a novel alpha3 isoform.";
RL   J. Cell Biol. 137:685-701(1997).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 1813-2531 (ISOFORM B).
RC   TISSUE=Lung;
RX   PubMed=8012114; DOI=10.1007/BF00360551;
RA   Aberdam D., Galliano M.-F., Mattei M.-G., Pisani-Spadafora A.,
RA   Ortonne J.-P., Meneguzzi G.;
RT   "Assignment of mouse nicein genes to chromosomes 1 and 18.";
RL   Mamm. Genome 5:229-233(1994).
RN   [7]
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
RT   expression.";
RL   Cell 143:1174-1189(2010).
CC   -!- FUNCTION: Binding to cells via a high affinity receptor, laminin
CC       is thought to mediate the attachment, migration and organization
CC       of cells into tissues during embryonic development by interacting
CC       with other extracellular matrix components.
CC   -!- FUNCTION: Laminin-5 is thought to be involved in (1) cell adhesion
CC       via integrin alpha-3/beta-1 in focal adhesion and integrin alpha-
CC       6/beta-4 in hemidesmosomes, (2) signal transduction via tyrosine
CC       phosphorylation of pp125-FAK and p80, (3) differentiation of
CC       keratinocytes. {ECO:0000250}.
CC   -!- SUBUNIT: Laminin is a complex glycoprotein, consisting of three
CC       different polypeptide chains (alpha, beta, gamma), which are bound
CC       to each other by disulfide bonds into a cross-shaped molecule
CC       comprising one long and three short arms with globules at each
CC       end. Alpha-3 is a subunit of laminin-5 (laminin-332 or
CC       epiligrin/kalinin/nicein), laminin-6 (laminin-311 or K-laminin)
CC       and laminin-7 (laminin-321 or KS-laminin).
CC   -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC       matrix, basement membrane. Note=Major component.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=B;
CC         IsoId=Q61789-1; Sequence=Displayed;
CC       Name=A;
CC         IsoId=Q61789-2; Sequence=VSP_003038, VSP_003039;
CC   -!- TISSUE SPECIFICITY: Basal membrane of the upper alimentary tract
CC       and urinary and nasal epithelia, salivary glands and teeth (both
CC       variants). Isoform A is predominantly expressed in skin, hair
CC       follicles and developing neurons of the trigeminal ganglion.
CC       Isoform B was found in bronchi, alveoli, stomach, intestinal
CC       crypts, whisker pads, CNS, telencephalic neuroectoderm, thalamus,
CC       Rathke pouch and periventricular subependymal germinal layer.
CC   -!- DOMAIN: The alpha-helical domains I and II are thought to interact
CC       with other laminin chains to form a coiled coil structure.
CC   -!- DOMAIN: Domains IV and G are globular.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAA58837.1; Type=Frameshift; Positions=Several; Evidence={ECO:0000305};
DR   EMBL; X84013; CAA58836.1; -; mRNA.
DR   EMBL; X84014; CAA58837.1; ALT_FRAME; mRNA.
DR   EMBL; AC102131; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC102248; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC139027; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC157909; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AJ293592; CAB99254.2; -; mRNA.
DR   EMBL; U88353; AAC53179.1; -; mRNA.
DR   EMBL; L20478; AAA68091.1; -; mRNA.
DR   CCDS; CCDS50222.1; -. [Q61789-1]
DR   CCDS; CCDS84360.1; -. [Q61789-2]
DR   RefSeq; NP_001334390.1; NM_001347461.1. [Q61789-2]
DR   RefSeq; NP_034810.1; NM_010680.1. [Q61789-1]
DR   SMR; Q61789; -.
DR   ComplexPortal; CPX-3012; Laminin-332 complex variant A. [Q61789-2]
DR   ComplexPortal; CPX-3013; Laminin-311 complex variant A. [Q61789-2]
DR   ComplexPortal; CPX-3014; Laminin-321 complex. [Q61789-2]
DR   ComplexPortal; CPX-3164; Laminin-332 complex variant B. [Q61789-1]
DR   ComplexPortal; CPX-3167; Laminin-311 complex variant B. [Q61789-1]
DR   STRING; 10090.ENSMUSP00000089703; -.
DR   iPTMnet; Q61789; -.
DR   PhosphoSitePlus; Q61789; -.
DR   PaxDb; Q61789; -.
DR   PeptideAtlas; Q61789; -.
DR   PRIDE; Q61789; -.
DR   Ensembl; ENSMUST00000092070; ENSMUSP00000089703; ENSMUSG00000024421. [Q61789-1]
DR   Ensembl; ENSMUST00000188815; ENSMUSP00000140104; ENSMUSG00000024421. [Q61789-2]
DR   GeneID; 16774; -.
DR   KEGG; mmu:16774; -.
DR   UCSC; uc008ecf.2; mouse. [Q61789-1]
DR   UCSC; uc008ech.1; mouse. [Q61789-2]
DR   CTD; 3909; -.
DR   MGI; MGI:99909; Lama3.
DR   eggNOG; KOG1836; Eukaryota.
DR   eggNOG; ENOG410XRDC; LUCA.
DR   GeneTree; ENSGT00940000155638; -.
DR   HOGENOM; HOG000048708; -.
DR   InParanoid; Q61789; -.
DR   KO; K06240; -.
DR   OMA; WVAPPSY; -.
DR   OrthoDB; 2342at2759; -.
DR   TreeFam; TF335359; -.
DR   Reactome; R-MMU-1474228; Degradation of the extracellular matrix.
DR   Reactome; R-MMU-2022090; Assembly of collagen fibrils and other multimeric structures.
DR   Reactome; R-MMU-2214320; Anchoring fibril formation.
DR   Reactome; R-MMU-3000157; Laminin interactions.
DR   Reactome; R-MMU-446107; Type I hemidesmosome assembly.
DR   Reactome; R-MMU-8874081; MET activates PTK2 signaling.
DR   PRO; PR:Q61789; -.
DR   Proteomes; UP000000589; Chromosome 18.
DR   Bgee; ENSMUSG00000024421; Expressed in 119 organ(s), highest expression level in molar tooth.
DR   Genevisible; Q61789; MM.
DR   GO; GO:0005604; C:basement membrane; IDA:MGI.
DR   GO; GO:0005913; C:cell-cell adherens junction; ISO:MGI.
DR   GO; GO:0062023; C:collagen-containing extracellular matrix; HDA:BHF-UCL.
DR   GO; GO:0005783; C:endoplasmic reticulum; ISO:MGI.
DR   GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR   GO; GO:0030056; C:hemidesmosome; ISO:MGI.
DR   GO; GO:0005608; C:laminin-3 complex; ISO:MGI.
DR   GO; GO:0005610; C:laminin-5 complex; IDA:MGI.
DR   GO; GO:0005178; F:integrin binding; IBA:GO_Central.
DR   GO; GO:0009887; P:animal organ morphogenesis; IBA:GO_Central.
DR   GO; GO:0016477; P:cell migration; IBA:GO_Central.
DR   GO; GO:0098609; P:cell-cell adhesion; ISO:MGI.
DR   GO; GO:0035987; P:endodermal cell differentiation; IEA:Ensembl.
DR   GO; GO:0031581; P:hemidesmosome assembly; ISO:MGI.
DR   GO; GO:0007229; P:integrin-mediated signaling pathway; IBA:GO_Central.
DR   GO; GO:0001738; P:morphogenesis of a polarized epithelium; IBA:GO_Central.
DR   GO; GO:0030155; P:regulation of cell adhesion; IEA:InterPro.
DR   GO; GO:0030334; P:regulation of cell migration; IEA:InterPro.
DR   GO; GO:0045995; P:regulation of embryonic development; IEA:InterPro.
DR   GO; GO:0009888; P:tissue development; IBA:GO_Central.
DR   Gene3D; 2.60.120.1490; -; 1.
DR   InterPro; IPR013320; ConA-like_dom_sf.
DR   InterPro; IPR000742; EGF-like_dom.
DR   InterPro; IPR009254; Laminin_aI.
DR   InterPro; IPR010307; Laminin_dom_II.
DR   InterPro; IPR002049; Laminin_EGF.
DR   InterPro; IPR001791; Laminin_G.
DR   InterPro; IPR000034; Laminin_IV.
DR   InterPro; IPR008211; Laminin_N.
DR   InterPro; IPR038684; Laminin_N_sf.
DR   Pfam; PF00052; Laminin_B; 1.
DR   Pfam; PF00053; Laminin_EGF; 13.
DR   Pfam; PF00054; Laminin_G_1; 1.
DR   Pfam; PF02210; Laminin_G_2; 4.
DR   Pfam; PF06008; Laminin_I; 1.
DR   Pfam; PF06009; Laminin_II; 1.
DR   Pfam; PF00055; Laminin_N; 1.
DR   SMART; SM00181; EGF; 8.
DR   SMART; SM00180; EGF_Lam; 14.
DR   SMART; SM00281; LamB; 1.
DR   SMART; SM00282; LamG; 5.
DR   SMART; SM00136; LamNT; 1.
DR   SUPFAM; SSF49899; SSF49899; 5.
DR   PROSITE; PS00022; EGF_1; 11.
DR   PROSITE; PS01186; EGF_2; 1.
DR   PROSITE; PS01248; EGF_LAM_1; 12.
DR   PROSITE; PS50027; EGF_LAM_2; 13.
DR   PROSITE; PS50025; LAM_G_DOMAIN; 5.
DR   PROSITE; PS51115; LAMININ_IVA; 1.
DR   PROSITE; PS51117; LAMININ_NTER; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Basement membrane; Cell adhesion; Coiled coil;
KW   Complete proteome; Direct protein sequencing; Disulfide bond;
KW   Extracellular matrix; Glycoprotein; Laminin EGF-like domain;
KW   Reference proteome; Repeat; Secreted; Signal.
FT   SIGNAL        1     31       {ECO:0000269|PubMed:11829758}.
FT   CHAIN        32   3330       Laminin subunit alpha-3.
FT                                /FTId=PRO_0000017059.
FT   DOMAIN       40    295       Laminin N-terminal. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00466}.
FT   DOMAIN      296    350       Laminin EGF-like 1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00460}.
FT   DOMAIN      353    420       Laminin EGF-like 2. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00460}.
FT   DOMAIN      423    464       Laminin EGF-like 3. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00460}.
FT   DOMAIN      488    530       Laminin EGF-like 4. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00460}.
FT   DOMAIN      533    576       Laminin EGF-like 5. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00460}.
FT   DOMAIN      582    625       Laminin EGF-like 6. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00460}.
FT   DOMAIN      628    678       Laminin EGF-like 7. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00460}.
FT   DOMAIN      681    725       Laminin EGF-like 8. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00460}.
FT   DOMAIN     1309   1352       Laminin EGF-like 9. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00460}.
FT   DOMAIN     1353   1401       Laminin EGF-like 10.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00460}.
FT   DOMAIN     1402   1452       Laminin EGF-like 11.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00460}.
FT   DOMAIN     1453   1462       Laminin EGF-like 12; first part.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00460}.
FT   DOMAIN     1466   1650       Laminin IV type A. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00458}.
FT   DOMAIN     1651   1683       Laminin EGF-like 12; second part.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00460}.
FT   DOMAIN     1684   1730       Laminin EGF-like 13.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00460}.
FT   DOMAIN     1731   1783       Laminin EGF-like 14.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00460}.
FT   DOMAIN     1784   1818       Laminin EGF-like 15; truncated.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00460}.
FT   DOMAIN     2386   2587       Laminin G-like 1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00122}.
FT   DOMAIN     2594   2756       Laminin G-like 2. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00122}.
FT   DOMAIN     2763   2923       Laminin G-like 3. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00122}.
FT   DOMAIN     2983   3147       Laminin G-like 4. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00122}.
FT   DOMAIN     3154   3327       Laminin G-like 5. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00122}.
FT   REGION      295    725       Domain V.
FT   REGION      793   1262       Domain IV 1 (domain IV B).
FT   REGION     1263   1462       Domain III B.
FT   REGION     1651   1818       Domain III A.
FT   REGION     1819   2385       Domain II and I.
FT   COILED     1851   1980       {ECO:0000255}.
FT   COILED     2012   2057       {ECO:0000255}.
FT   COILED     2088   2165       {ECO:0000255}.
FT   COILED     2211   2238       {ECO:0000255}.
FT   COILED     2318   2383       {ECO:0000255}.
FT   MOTIF      2274   2276       Cell attachment site. {ECO:0000255}.
FT   CARBOHYD    139    139       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    445    445       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   1354   1354       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   1673   1673       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   2159   2159       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   2261   2261       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   2332   2332       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   2361   2361       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   2498   2498       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   2580   2580       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   2747   2747       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   3094   3094       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   3270   3270       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   DISULFID    296    305       {ECO:0000250}.
FT   DISULFID    298    316       {ECO:0000250}.
FT   DISULFID    318    327       {ECO:0000250}.
FT   DISULFID    330    350       {ECO:0000250}.
FT   DISULFID    353    362       {ECO:0000250}.
FT   DISULFID    355    387       {ECO:0000250}.
FT   DISULFID    390    399       {ECO:0000250}.
FT   DISULFID    402    420       {ECO:0000250}.
FT   DISULFID    423    433       {ECO:0000250}.
FT   DISULFID    425    440       {ECO:0000250}.
FT   DISULFID    442    451       {ECO:0000250}.
FT   DISULFID    454    464       {ECO:0000250}.
FT   DISULFID    488    500       {ECO:0000250}.
FT   DISULFID    490    506       {ECO:0000250}.
FT   DISULFID    508    517       {ECO:0000250}.
FT   DISULFID    520    530       {ECO:0000250}.
FT   DISULFID    533    545       {ECO:0000250}.
FT   DISULFID    535    552       {ECO:0000250}.
FT   DISULFID    554    563       {ECO:0000250}.
FT   DISULFID    566    583       {ECO:0000250}.
FT   DISULFID    628    642       {ECO:0000250}.
FT   DISULFID    630    649       {ECO:0000250}.
FT   DISULFID    651    660       {ECO:0000250}.
FT   DISULFID    663    678       {ECO:0000250}.
FT   DISULFID    681    693       {ECO:0000250}.
FT   DISULFID    683    700       {ECO:0000250}.
FT   DISULFID    702    711       {ECO:0000250}.
FT   DISULFID   1309   1316       {ECO:0000250}.
FT   DISULFID   1311   1323       {ECO:0000250}.
FT   DISULFID   1325   1334       {ECO:0000250}.
FT   DISULFID   1337   1350       {ECO:0000250}.
FT   DISULFID   1353   1368       {ECO:0000250}.
FT   DISULFID   1355   1375       {ECO:0000250}.
FT   DISULFID   1377   1386       {ECO:0000250}.
FT   DISULFID   1389   1399       {ECO:0000250}.
FT   DISULFID   1402   1414       {ECO:0000250}.
FT   DISULFID   1404   1421       {ECO:0000250}.
FT   DISULFID   1423   1432       {ECO:0000250}.
FT   DISULFID   1435   1450       {ECO:0000250}.
FT   DISULFID   1684   1693       {ECO:0000250}.
FT   DISULFID   1686   1700       {ECO:0000250}.
FT   DISULFID   1703   1712       {ECO:0000250}.
FT   DISULFID   1715   1728       {ECO:0000250}.
FT   DISULFID   1731   1743       {ECO:0000250}.
FT   DISULFID   1733   1752       {ECO:0000250}.
FT   DISULFID   1754   1763       {ECO:0000250}.
FT   DISULFID   1766   1781       {ECO:0000250}.
FT   DISULFID   1819   1819       Interchain. {ECO:0000305}.
FT   DISULFID   1822   1822       Interchain. {ECO:0000305}.
FT   DISULFID   2557   2587       {ECO:0000250}.
FT   DISULFID   2733   2756       {ECO:0000250}.
FT   DISULFID   2891   2923       {ECO:0000250}.
FT   DISULFID   3124   3147       {ECO:0000250}.
FT   DISULFID   3299   3327       {ECO:0000250}.
FT   VAR_SEQ       1   1619       Missing (in isoform A).
FT                                {ECO:0000303|PubMed:7665604}.
FT                                /FTId=VSP_003038.
FT   VAR_SEQ    1620   1662       FTETQRLTLGEVGLEEASDTGSGPRAHLVEMCACPPDYTGD
FT                                SC -> MLPAVRWSAWSTGWLWIFGAALGQCLGYGSEQQRV
FT                                AFLQRPSQNHLQASYMELRPS (in isoform A).
FT                                {ECO:0000303|PubMed:7665604}.
FT                                /FTId=VSP_003039.
FT   CONFLICT    982    982       A -> R (in Ref. 1; CAA58837).
FT                                {ECO:0000305}.
FT   CONFLICT   1150   1150       W -> R (in Ref. 1; CAA58837).
FT                                {ECO:0000305}.
FT   CONFLICT   1224   1224       E -> K (in Ref. 1; CAA58837).
FT                                {ECO:0000305}.
FT   CONFLICT   1272   1272       G -> GH (in Ref. 1; CAA58837).
FT                                {ECO:0000305}.
FT   CONFLICT   1291   1291       R -> S (in Ref. 1; CAA58837).
FT                                {ECO:0000305}.
FT   CONFLICT   1398   1398       E -> K (in Ref. 1; CAA58837).
FT                                {ECO:0000305}.
FT   CONFLICT   1466   1466       H -> R (in Ref. 1; CAA58837).
FT                                {ECO:0000305}.
FT   CONFLICT   1479   1479       R -> V (in Ref. 1; CAA58837).
FT                                {ECO:0000305}.
FT   CONFLICT   1488   1488       V -> F (in Ref. 1; CAA58837).
FT                                {ECO:0000305}.
FT   CONFLICT   1527   1528       SS -> II (in Ref. 1; CAA58837).
FT                                {ECO:0000305}.
FT   CONFLICT   1608   1608       S -> P (in Ref. 1; CAA58837).
FT                                {ECO:0000305}.
FT   CONFLICT   1983   1984       KK -> QN (in Ref. 1; CAA58836/CAA58837
FT                                and 6; AAA68091). {ECO:0000305}.
FT   CONFLICT   1987   1987       Q -> G (in Ref. 1; CAA58836/CAA58837 and
FT                                6; AAA68091). {ECO:0000305}.
FT   CONFLICT   2463   2463       R -> G (in Ref. 1; CAA58836/CAA58837 and
FT                                6; AAA68091). {ECO:0000305}.
FT   CONFLICT   2488   2488       F -> S (in Ref. 1; CAA58836/CAA58837 and
FT                                6; AAA68091). {ECO:0000305}.
FT   CONFLICT   2617   2620       NFMQ -> KLSW (in Ref. 1; CAA58836/
FT                                CAA58837). {ECO:0000305}.
FT   CONFLICT   2724   2725       NI -> PL (in Ref. 1; CAA58836/CAA58837).
FT                                {ECO:0000305}.
FT   CONFLICT   3257   3257       D -> Y (in Ref. 1; CAA58836/CAA58837).
FT                                {ECO:0000305}.
SQ   SEQUENCE   3330 AA;  366227 MW;  993EB20BACDD6C59 CRC64;
     MAVALGRAPR SLPLLLTLLL LLLLRMSPSW SVVGQDHPMS SRSLHPPYFN LAQAARIWAT
     ATCGERDPEV SRPRPELFCK LVGGPAAQGS GHTIQGQFCD YCNSEDSRKA HPASHAIDGS
     ERWWQSPPLS SGTQYNQVNL TLDLGQLFHV AYILIKFANS PRPDLWILER SVDFGSTYSP
     WQYFAHSRRD CVEQFGQEAN MAITQDDQML CVTEYSRIVP LENGEIVVSL INGRPGAKKF
     AFSDTLREFT KATNIRLRFL RTNTLLGHLI SKAERDPTVT RRYYYSIKDI SVGGRCVCNG
     HAEACSADNP EKQFRCECQH HTCGDTCNRC CAGYNQRRWQ PAGQEQHNEC EACNCHGHAV
     DCYYDPDVEH QQASLNSKGV YAGGGVCINC QHNTAGVNCE KCAKGYFRPH GVPVDALHGC
     IPCSCDPERA DDCDQGSGHC HCKPNFSGDY CETCADGYYN FPFCLRIPVF PNYTPSPEDP
     VAGNIKGCDC NLEGVLPEIC DDRGRCLCRP GVEGPQCDSC RSGSYSFPIC QACQCSTIGS
     YPVPCDPGNG QCDCLPGITG RQCDRCLSGA YDFPYCQGSG SVCHPAGTLD SSLGYCQCKQ
     HVASPTCSVC KPLYWNLAKE NPRGCSECQC HEAGTLSGIG ECGQEDGDCS CKAHVTGDAC
     DTCEDGFFSL EKSNYFGCQG CQCDIGGALT TMCSGPSGVC QCREHVEGKQ CQRPENNYYF
     PDLHHMKYEV EDGTGPNGRN LRFGFDPLVF PEFSWRGYAP MTSVQNEVRV RLSVRQSSLS
     LFRIVLRYIS PGTEAISGRI TLYSSQGDSD ALQSRKITFP PSKEPAFVTV PGNGFAGPFS
     ITPGTWIACI QVEGVLLDYL VLLPRDYYEA FTLQVPVTEP CAHTGSPQDN CLLYQHLPLT
     AFSCTLACEA RHFLLDGELR PLAMRQPTPT HPAMVDLSGR EVELQLRLRV PQVGHYVVLL
     EYATEVEQLF VVDVNLKSSG SALAGQVNIY SCKYSIPCRS VVIDSLSRTA VHELLADADI
     QLKAHMAHFL LYHICIIPAE EFSTEYLRPQ VHCIASYRQH ANPSASCVSL AHETPPTASI
     LDATSRGLFS ALPHEPSSPA DGVTLKAPQS QVTLKGLIPH LGRHVFVIHF YQAEHPGFPT
     EVIVNGGRQW SGSFLASFCP HLLGCRDQVI SDGQVEFDIS EAEVAVTVKI PDGKSLTLVR
     VLVVPAENYD YQILHKTTVD KSSEFISSCG GDSFYIDPQA ASGFCKNSAR SLVAFYHNGA
     IPCECDPAGT AGHHCSPEGG QCPCRPNVIG RQCSRCATGY YGFPYCKPCN CGRRLCEEVT
     GKCLCPPHTV RPQCEVCEMN SFNFHPVAGC DVCNCSRKGT IEAAVSECDR DSGQCRCKPR
     VTGQQCDKCA PGFYQFPECV PCSCNRDGTE PSVCDPETGA CMCKENVEGP QCQLCREGSF
     YLDPTNPKGC TKCFCFGVNT DCQSSHKQRA KFVDMMGWRL ETADGVDVPV SFNPGSNSMV
     ADLQELPPSV HSASWVAPPS YLGDKVSSYG GYLTYHAKSF GLPGDMVLLG KQPDVQLTGQ
     HMSLIHKEPS DPRPDRLHHG RVQVIEGNFR HEGSSAPVSR EELMTVLSRL ERLHIRGLHF
     TETQRLTLGE VGLEEASDTG SGPRAHLVEM CACPPDYTGD SCQGCRPGYY WDNKSLPVGR
     CVPCNCNGHS NRCQDGSGIC INCQHNTAGE HCERCQAGHY GNAIHGSCRV CPCPHTNSFA
     TGCAVDGGAV RCACKPGYTG TQCERCAPGY FGNPQKFGGS CQPCNCNSNG QLGPCDPLTG
     DCVNQEPKDG SPAEECDDCD SCVMTLLNDL ASMGEELRLV KSKLQGLSVS TGALEQIRHM
     ETQAKDLRNQ LLGFRSATSS HGSKMDDLEK ELSHLNREFE TLQEKAQVNS RKAQTLYNNI
     DQTIQSAKEL DMKIKNIVQN VHILLKQMAR PGGEGTDLPV GDWSRELAEA QRMMRDLRSR
     DFKKHLQEAE AEKMEAQLLL HRIRTWLESH QVENNGLLKN IRDSLNDYED KLQDLRSILQ
     EAAAQAKQAT GINHENEGVL GAIQRQMKEM DSLKNDFTKY LATADSSLLQ TNNLLQQMDK
     SQKEYESLAA ALNGARQELS DRVRELSRSG GKAPLVVEAE KHAQSLQELA KQLEEIKRNT
     SGDELVRCAV DAATAYENIL NAIRAAEDAA SKATSASKSA FQTVIKEDLP KRAKTLSSDS
     EELLNEAKMT QKRLQQVSPA LNSLQQTLKT VSVQKDLLDA NLTVARDDLH GIQRGDIDSV
     VIGAKSMVRE ANGITSEVLD GLNPIQTDLG RIKDSYESAR REDFSKALVD ANNSVKKLTR
     KLPDLFIKIE SINQQLLPLG NISDNVDRIR ELIQQARDAA NKVAIPMRFN GKSGVEVRLP
     NDLEDLKGYT SLSLFLQRPD LRENGGTEDM FVMYLGNKDA SKDYIGMAVV DGQLTCVYNL
     GDREAEVQID QVLTESESQE AVMDRVKFQR IYQFAKLNYT KEATSTKPKA PGVYDMESAS
     SNTLLNLDPE NAVFYVGGYP PGFELPRRLR FPPYKGCIEL DDLNENVLSL YNFKTTFNLN
     TTEVEPCRRR KEESDKNYFE GTGYARIPTQ PNAPFPNFMQ TIQTTVDRGL LFFAENQDNF
     ISLNIEDGNL MVKYKLNSEP PKEKGIRDTI NNGRDHMILI SIGKSQKRML INMNKHSIII
     EGEIFDFSTY YLGGIPIAIR ERFNISTPAF QGCMKNLKKT SGVVRLNDTV GVTKKCSEDW
     KLVRTASFSR GGQMSFTNLD VPSLDRFQLS FGFQTFQPSG TLLNHQTRTS SLLVTLEDGH
     IALSTRDSSS PIFKSPGTYM DGLLHHVSVI SDTSGLRLLI DDQVLRRNQR LASFSNAQQS
     LSMGGGYFEG CISNVFVQRM SQSPEVLDMA SKSTKRDAFL GGCSLNKPPF LMLFKSPKGF
     NKARSFNVNQ LLQDAPQAAR SIEAWQDGKS CLPPLNTKAT HRALQFGDSP TSHLLFKLPQ
     ELLKPRLQFS LDIQTTSSRG LVFHTGTRDS FVALYLSEGH VIFALGAGGK KLRLRSKERY
     HDGKWHSVVF GLSGRKVHLV VDGLRAQEGS LPGNSTISPR EQVYLGLSPS RKSKSLPQHS
     FVGCLRNFQL DSKPLDSPSA RSGVSPCLGG SLEKGIYFSQ GGGHVVLANS VSLEPALTLT
     LSIRPRSLTG VLIHIASQSG EHLSVYMEAG KVTTSMNSEA GGTVTSITPK RSLCDGQWHS
     VTVSIKQHTL HLELDTDNSY TAGQLSFPPN STRGSLHIGG VPDKLKMLTL PVWNSFFGCL
     KNIQVNHIPV PITEATDVQG SVSLNGCPDH
//
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