LAMA_DROME
ID LAMA_DROME Reviewed; 3712 AA.
AC Q00174; Q9VRW0;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 10-MAY-2005, sequence version 2.
DT 03-AUG-2022, entry version 178.
DE RecName: Full=Laminin subunit alpha;
DE AltName: Full=Laminin A chain;
DE Flags: Precursor;
GN Name=LanA; Synonyms=lamA; ORFNames=CG10236;
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=1425586; DOI=10.1002/j.1460-2075.1992.tb05553.x;
RA Kusche-Gullberg M., Garrison K., Mackrell A.J., Fessler L.I., Fessler J.H.;
RT "Laminin A chain: expression during Drosophila development and genomic
RT sequence.";
RL EMBO J. 11:4519-4527(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND DISRUPTION PHENOTYPE.
RC TISSUE=Embryo;
RX PubMed=8223265; DOI=10.1242/dev.118.2.325;
RA Henchcliffe C., Garcia-Alonso L., Tang J., Goodman C.S.;
RT "Genetic analysis of laminin A reveals diverse functions during
RT morphogenesis in Drosophila.";
RL Development 118:325-337(1993).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley;
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [4]
RP GENOME REANNOTATION.
RC STRAIN=Berkeley;
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1762-3712.
RX PubMed=1744083; DOI=10.1016/s0021-9258(18)54439-2;
RA Garrison K., Mackrell A.J., Fessler J.H.;
RT "Drosophila laminin A chain sequence, interspecies comparison, and domain
RT structure of a major carboxyl portion.";
RL J. Biol. Chem. 266:22899-22904(1991).
RN [6]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-2196 AND ASN-2538, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=Oregon-R; TISSUE=Head;
RX PubMed=17893096; DOI=10.1093/glycob/cwm097;
RA Koles K., Lim J.-M., Aoki K., Porterfield M., Tiemeyer M., Wells L.,
RA Panin V.;
RT "Identification of N-glycosylated proteins from the central nervous system
RT of Drosophila melanogaster.";
RL Glycobiology 17:1388-1403(2007).
RN [7]
RP FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=23054837; DOI=10.1073/pnas.1206416109;
RA Tsai P.I., Wang M., Kao H.H., Cheng Y.J., Lin Y.J., Chen R.H., Chien C.T.;
RT "Activity-dependent retrograde laminin A signaling regulates synapse growth
RT at Drosophila neuromuscular junctions.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:17699-17704(2012).
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. Activates presynaptic signaling
CC involving integrin alpha-PS3/beta-nu and Fak to suppress neuromuscular
CC junction (NMJ) growth during larval development and during low crawling
CC activity, but not during higher-crawling conditions. Mediates, together
CC with integrin alpha-PS3/beta-nu, glutamate receptor-modulated NMJ
CC growth. {ECO:0000269|PubMed:23054837, ECO:0000269|PubMed:8223265}.
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.
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC matrix, basement membrane. Synapse. Cell projection, axon. Cytoplasmic
CC vesicle, secretory vesicle, synaptic vesicle. Note=Major component of
CC basement membranes. At neuromucular junctions, localizes in synaptic
CC clefts of peri-active zones and in subsynaptic reticula.
CC -!- TISSUE SPECIFICITY: Newly formed mesoderm and later prominently
CC expressed in hemocytes, which also synthesize collagen IV. Expressed in
CC muscles. {ECO:0000269|PubMed:1425586, ECO:0000269|PubMed:23054837}.
CC -!- DEVELOPMENTAL STAGE: During morphogenesis, mostly in embryo development
CC at 10-12 hours. {ECO:0000269|PubMed:1425586}.
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, IV and G are globular.
CC -!- DISRUPTION PHENOTYPE: Flies show late embryonic lethality. Certain
CC partial loss-of-function mutations give raise to escaper adults, which
CC have rough eyes associated with changes in cell fate and pattern,
CC misshappen legs and defects in wing structure.
CC {ECO:0000269|PubMed:8223265}.
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DR EMBL; M96388; AAA28662.1; -; Genomic_DNA.
DR EMBL; L07288; AAC37178.1; -; mRNA.
DR EMBL; AE014296; AAF50672.2; -; Genomic_DNA.
DR EMBL; M75882; AAA28661.1; -; mRNA.
DR PIR; S28399; S18253.
DR RefSeq; NP_476617.1; NM_057269.3.
DR SMR; Q00174; -.
DR BioGRID; 64176; 23.
DR IntAct; Q00174; 9.
DR STRING; 7227.FBpp0076722; -.
DR GlyGen; Q00174; 32 sites.
DR iPTMnet; Q00174; -.
DR PaxDb; Q00174; -.
DR PRIDE; Q00174; -.
DR EnsemblMetazoa; FBtr0077014; FBpp0076722; FBgn0002526.
DR GeneID; 38723; -.
DR KEGG; dme:Dmel_CG10236; -.
DR CTD; 38723; -.
DR FlyBase; FBgn0002526; LanA.
DR VEuPathDB; VectorBase:FBgn0002526; -.
DR eggNOG; KOG1836; Eukaryota.
DR GeneTree; ENSGT00940000167067; -.
DR HOGENOM; CLU_000301_1_0_1; -.
DR InParanoid; Q00174; -.
DR PhylomeDB; Q00174; -.
DR SignaLink; Q00174; -.
DR BioGRID-ORCS; 38723; 0 hits in 3 CRISPR screens.
DR ChiTaRS; LanA; fly.
DR GenomeRNAi; 38723; -.
DR PRO; PR:Q00174; -.
DR Proteomes; UP000000803; Chromosome 3L.
DR Bgee; FBgn0002526; Expressed in hemocyte (sensu Nematoda and Protostomia) and 63 other tissues.
DR ExpressionAtlas; Q00174; baseline and differential.
DR Genevisible; Q00174; DM.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0030424; C:axon; IEA:UniProtKB-SubCell.
DR GO; GO:0005604; C:basement membrane; IDA:FlyBase.
DR GO; GO:0062023; C:collagen-containing extracellular matrix; HDA:FlyBase.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR GO; GO:0036062; C:presynaptic periactive zone; IDA:FlyBase.
DR GO; GO:0008021; C:synaptic vesicle; IEA:UniProtKB-SubCell.
DR GO; GO:0005102; F:signaling receptor binding; IEA:InterPro.
DR GO; GO:0009887; P:animal organ morphogenesis; IBA:GO_Central.
DR GO; GO:0007411; P:axon guidance; IMP:FlyBase.
DR GO; GO:0071711; P:basement membrane organization; IMP:UniProtKB.
DR GO; GO:0033627; P:cell adhesion mediated by integrin; IDA:FlyBase.
DR GO; GO:0035001; P:dorsal trunk growth, open tracheal system; IMP:FlyBase.
DR GO; GO:0007507; P:heart development; IMP:FlyBase.
DR GO; GO:0035011; P:melanotic encapsulation of foreign target; IMP:FlyBase.
DR GO; GO:0007498; P:mesoderm development; IEP:FlyBase.
DR GO; GO:0045886; P:negative regulation of synaptic assembly at neuromuscular junction; IMP:FlyBase.
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:0034446; P:substrate adhesion-dependent cell spreading; IDA:FlyBase.
DR GO; GO:0009888; P:tissue development; IBA:GO_Central.
DR CDD; cd00055; EGF_Lam; 22.
DR CDD; cd00110; LamG; 5.
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; IPR001791; Laminin_G.
DR InterPro; IPR000034; Laminin_IV.
DR InterPro; IPR008211; Laminin_N.
DR InterPro; IPR002049; LE_dom.
DR Pfam; PF00052; Laminin_B; 1.
DR Pfam; PF00053; Laminin_EGF; 20.
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; 14.
DR SMART; SM00180; EGF_Lam; 21.
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; 17.
DR PROSITE; PS01186; EGF_2; 5.
DR PROSITE; PS01248; EGF_LAM_1; 19.
DR PROSITE; PS50027; EGF_LAM_2; 22.
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 Basement membrane; Cell adhesion; Cell projection; Coiled coil;
KW Cytoplasmic vesicle; Disulfide bond; Extracellular matrix; Glycoprotein;
KW Laminin EGF-like domain; Reference proteome; Repeat; Secreted; Signal;
KW Synapse.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT CHAIN 23..3712
FT /note="Laminin subunit alpha"
FT /id="PRO_0000017064"
FT DOMAIN 23..272
FT /note="Laminin N-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00466"
FT DOMAIN 273..332
FT /note="Laminin EGF-like 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DOMAIN 333..402
FT /note="Laminin EGF-like 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DOMAIN 403..447
FT /note="Laminin EGF-like 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DOMAIN 448..494
FT /note="Laminin EGF-like 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DOMAIN 495..540
FT /note="Laminin EGF-like 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DOMAIN 541..586
FT /note="Laminin EGF-like 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DOMAIN 587..631
FT /note="Laminin EGF-like 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DOMAIN 632..676
FT /note="Laminin EGF-like 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DOMAIN 677..731
FT /note="Laminin EGF-like 9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DOMAIN 732..784
FT /note="Laminin EGF-like 10"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DOMAIN 785..815
FT /note="Laminin EGF-like 11; truncated"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DOMAIN 1375..1420
FT /note="Laminin EGF-like 12"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DOMAIN 1421..1465
FT /note="Laminin EGF-like 13"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DOMAIN 1466..1513
FT /note="Laminin EGF-like 14"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DOMAIN 1514..1564
FT /note="Laminin EGF-like 15"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DOMAIN 1565..1574
FT /note="Laminin EGF-like 16; first part"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DOMAIN 1585..1775
FT /note="Laminin IV type A"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00458"
FT DOMAIN 1776..1808
FT /note="Laminin EGF-like 16; second part"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DOMAIN 1809..1858
FT /note="Laminin EGF-like 17"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DOMAIN 1859..1916
FT /note="Laminin EGF-like 18"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DOMAIN 1917..1969
FT /note="Laminin EGF-like 19"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DOMAIN 1970..2016
FT /note="Laminin EGF-like 20"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DOMAIN 2017..2063
FT /note="Laminin EGF-like 21"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DOMAIN 2064..2111
FT /note="Laminin EGF-like 22"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DOMAIN 2672..2868
FT /note="Laminin G-like 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00122"
FT DOMAIN 2876..3048
FT /note="Laminin G-like 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00122"
FT DOMAIN 3055..3223
FT /note="Laminin G-like 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00122"
FT DOMAIN 3349..3528
FT /note="Laminin G-like 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00122"
FT DOMAIN 3534..3709
FT /note="Laminin G-like 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00122"
FT REGION 816..1374
FT /note="Domain IV''"
FT REGION 2112..2671
FT /note="Domain II and I"
FT REGION 3244..3297
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 2178..2249
FT /evidence="ECO:0000255"
FT COILED 2301..2321
FT /evidence="ECO:0000255"
FT COILED 2376..2450
FT /evidence="ECO:0000255"
FT COILED 2541..2676
FT /evidence="ECO:0000255"
FT COMPBIAS 3266..3297
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 116
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 219
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 395
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 453
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 508
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 588
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 722
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 897
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1352
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1484
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1583
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1617
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1847
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1943
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2024
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2196
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:17893096"
FT CARBOHYD 2215
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2267
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2301
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2323
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2482
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2524
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2538
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:17893096"
FT CARBOHYD 2569
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2699
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2720
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2890
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2938
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 3010
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 3070
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 3491
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 3612
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 273..282
FT /evidence="ECO:0000250"
FT DISULFID 275..296
FT /evidence="ECO:0000250"
FT DISULFID 298..307
FT /evidence="ECO:0000250"
FT DISULFID 310..330
FT /evidence="ECO:0000250"
FT DISULFID 333..342
FT /evidence="ECO:0000250"
FT DISULFID 335..367
FT /evidence="ECO:0000250"
FT DISULFID 370..379
FT /evidence="ECO:0000250"
FT DISULFID 382..400
FT /evidence="ECO:0000250"
FT DISULFID 403..414
FT /evidence="ECO:0000250"
FT DISULFID 405..421
FT /evidence="ECO:0000250"
FT DISULFID 423..432
FT /evidence="ECO:0000250"
FT DISULFID 435..445
FT /evidence="ECO:0000250"
FT DISULFID 448..460
FT /evidence="ECO:0000250"
FT DISULFID 450..468
FT /evidence="ECO:0000250"
FT DISULFID 470..479
FT /evidence="ECO:0000250"
FT DISULFID 482..492
FT /evidence="ECO:0000250"
FT DISULFID 495..507
FT /evidence="ECO:0000250"
FT DISULFID 497..514
FT /evidence="ECO:0000250"
FT DISULFID 516..525
FT /evidence="ECO:0000250"
FT DISULFID 528..538
FT /evidence="ECO:0000250"
FT DISULFID 541..553
FT /evidence="ECO:0000250"
FT DISULFID 543..560
FT /evidence="ECO:0000250"
FT DISULFID 562..571
FT /evidence="ECO:0000250"
FT DISULFID 574..584
FT /evidence="ECO:0000250"
FT DISULFID 587..599
FT /evidence="ECO:0000250"
FT DISULFID 589..605
FT /evidence="ECO:0000250"
FT DISULFID 607..616
FT /evidence="ECO:0000250"
FT DISULFID 619..629
FT /evidence="ECO:0000250"
FT DISULFID 632..644
FT /evidence="ECO:0000250"
FT DISULFID 634..650
FT /evidence="ECO:0000250"
FT DISULFID 652..661
FT /evidence="ECO:0000250"
FT DISULFID 664..674
FT /evidence="ECO:0000250"
FT DISULFID 677..691
FT /evidence="ECO:0000250"
FT DISULFID 679..700
FT /evidence="ECO:0000250"
FT DISULFID 702..711
FT /evidence="ECO:0000250"
FT DISULFID 714..729
FT /evidence="ECO:0000250"
FT DISULFID 732..746
FT /evidence="ECO:0000250"
FT DISULFID 734..753
FT /evidence="ECO:0000250"
FT DISULFID 755..764
FT /evidence="ECO:0000250"
FT DISULFID 767..782
FT /evidence="ECO:0000250"
FT DISULFID 785..797
FT /evidence="ECO:0000250"
FT DISULFID 787..804
FT /evidence="ECO:0000250"
FT DISULFID 806..815
FT /evidence="ECO:0000250"
FT DISULFID 1375..1387
FT /evidence="ECO:0000250"
FT DISULFID 1377..1394
FT /evidence="ECO:0000250"
FT DISULFID 1396..1405
FT /evidence="ECO:0000250"
FT DISULFID 1408..1418
FT /evidence="ECO:0000250"
FT DISULFID 1421..1429
FT /evidence="ECO:0000250"
FT DISULFID 1423..1436
FT /evidence="ECO:0000250"
FT DISULFID 1438..1447
FT /evidence="ECO:0000250"
FT DISULFID 1450..1463
FT /evidence="ECO:0000250"
FT DISULFID 1466..1480
FT /evidence="ECO:0000250"
FT DISULFID 1468..1487
FT /evidence="ECO:0000250"
FT DISULFID 1489..1498
FT /evidence="ECO:0000250"
FT DISULFID 1501..1511
FT /evidence="ECO:0000250"
FT DISULFID 1514..1526
FT /evidence="ECO:0000250"
FT DISULFID 1516..1533
FT /evidence="ECO:0000250"
FT DISULFID 1535..1544
FT /evidence="ECO:0000250"
FT DISULFID 1547..1562
FT /evidence="ECO:0000250"
FT DISULFID 1778..1787
FT /evidence="ECO:0000250"
FT DISULFID 1790..1806
FT /evidence="ECO:0000250"
FT DISULFID 1809..1818
FT /evidence="ECO:0000250"
FT DISULFID 1811..1825
FT /evidence="ECO:0000250"
FT DISULFID 1828..1837
FT /evidence="ECO:0000250"
FT DISULFID 1840..1856
FT /evidence="ECO:0000250"
FT DISULFID 1859..1874
FT /evidence="ECO:0000250"
FT DISULFID 1861..1885
FT /evidence="ECO:0000250"
FT DISULFID 1887..1896
FT /evidence="ECO:0000250"
FT DISULFID 1899..1914
FT /evidence="ECO:0000250"
FT DISULFID 1917..1931
FT /evidence="ECO:0000250"
FT DISULFID 1919..1938
FT /evidence="ECO:0000250"
FT DISULFID 1941..1950
FT /evidence="ECO:0000250"
FT DISULFID 1953..1967
FT /evidence="ECO:0000250"
FT DISULFID 1970..1980
FT /evidence="ECO:0000250"
FT DISULFID 1972..1987
FT /evidence="ECO:0000250"
FT DISULFID 1989..1998
FT /evidence="ECO:0000250"
FT DISULFID 2001..2014
FT /evidence="ECO:0000250"
FT DISULFID 2017..2028
FT /evidence="ECO:0000250"
FT DISULFID 2019..2035
FT /evidence="ECO:0000250"
FT DISULFID 2037..2046
FT /evidence="ECO:0000250"
FT DISULFID 2049..2061
FT /evidence="ECO:0000250"
FT DISULFID 2064..2076
FT /evidence="ECO:0000250"
FT DISULFID 2066..2083
FT /evidence="ECO:0000250"
FT DISULFID 2085..2094
FT /evidence="ECO:0000250"
FT DISULFID 2097..2109
FT /evidence="ECO:0000250"
FT DISULFID 2112
FT /note="Interchain"
FT /evidence="ECO:0000305"
FT DISULFID 2115
FT /note="Interchain"
FT /evidence="ECO:0000305"
FT DISULFID 3022..3048
FT /evidence="ECO:0000250"
FT DISULFID 3196..3223
FT /evidence="ECO:0000250"
FT DISULFID 3505..3528
FT /evidence="ECO:0000250"
FT DISULFID 3682..3709
FT /evidence="ECO:0000250"
FT CONFLICT 45
FT /note="Q -> P (in Ref. 1; AAA28662)"
FT /evidence="ECO:0000305"
FT CONFLICT 1032
FT /note="L -> R (in Ref. 2; AAC37178)"
FT /evidence="ECO:0000305"
FT CONFLICT 1407
FT /note="A -> R (in Ref. 1; AAA28662)"
FT /evidence="ECO:0000305"
FT CONFLICT 1559
FT /note="P -> Q (in Ref. 2; AAC37178)"
FT /evidence="ECO:0000305"
FT CONFLICT 1598
FT /note="H -> Q (in Ref. 2; AAC37178)"
FT /evidence="ECO:0000305"
FT CONFLICT 1912
FT /note="Q -> E (in Ref. 2; AAC37178)"
FT /evidence="ECO:0000305"
FT CONFLICT 2630
FT /note="N -> S (in Ref. 3; AAF50672)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 3712 AA; 411157 MW; F8DB4D0CC88BBEC1 CRC64;
MGHGVASIGA LLVILAISYC QAELTPPYFN LATGRKIYAT ATCGQDTDGP ELYCKLVGAN
TEHDHIDYSV IQGQVCDYCD PTVPERNHPP ENAIDGTEAW WQSPPLSRGM KFNEVNLTIN
FEQEFHVAYL FIRMGNSPRP GLWTLEKSTD YGKTWTPWQH FSDTPADCET YFGKDTYKPI
TRDDDVICTT EYSKIVPLEN GEIPVMLLNE RPSSTNYFNS TVLQEWTRAT NVRIRLLRTK
NLLGHLMSVA RQDPTVTRRY FYSIKDISIG GRCMCNGHAD TCDVKDPKSP VRILACRCQH
HTCGIQCNEC CPGFEQKKWR QNTNARPFNC EPCNCHGHSN ECKYDEEVNR KGLSLDIHGH
YDGGGVCQNC QHNTVGINCN KCKPKYYRPK GKHWNETDVC SPCQCDYFFS TGHCEEETGN
CECRAAFQPP SCDSCAYGYY GYPNCRECEC NLNGTNGYHC EAESGQQCPC KINFAGAYCK
QCAEGYYGFP ECKACECNKI GSITNDCNVT TGECKCLTNF GGDNCERCKH GYFNYPTCSY
CDCDNQGTES EICNKQSGQC ICREGFGGPR CDQCLPGFYN YPDCKPCNCS STGSSAITCD
NTGKCNCLNN FAGKQCTLCT AGYYSYPDCL PCHCDSHGSQ GVSCNSDGQC LCQPNFDGRQ
CDSCKEGFYN FPSCEDCNCD PAGVIDKFAG CGSVPVGELC KCKERVTGRI CNECKPLYWN
LNISNTEGCE ICDCWTDGTI SALDTCTSKS GQCPCKPHTQ GRRCQECRDG TFDLDSASLF
GCKDCSCDVG GSWQSVCDKI SGQCKCHPRI TGLACTQPLT THFFPTLHQF QYEYEDGSLP
SGTQVRYDYD EAAFPGFSSK GYVVFNAIQN DVRNEVNVFK SSLYRIVLRY VNPNAENVTA
TISVTSDNPL EVDQHVKVLL QPTSEPQFVT VAGPLGVKPS AIVLDPGRYV FTTKANKNVM
LDYFVLLPAA YYEAGILTRH ISNPCELGNM ELCRHYKYAS VEVFSPAATP FVIGENSKPT
NPVETYTDPE HLQIVSHVGD IPVLSGSQNE LHYIVDVPRS GRYIFVIDYI SDRNFPDSYY
INLKLKDNPD SETSVLLYPC LYSTICRTSV NEDGMEKSFY INKEDLQPVI ISADIEDGSR
FPIISVTAIP VDQWSIDYIN PSPVCVIHDQ QCATPKFRSV PDSKKIEFET DHEDRIATNK
PPYASLDERV KLVHLDSQNE ATIVIESKVD ATKPNLFVIL VKYYQPSHPK YQVYYTLTAG
KNQYDGKFDI QHCPSSSGCR GVIRPAGEGS FEIDDEFKFT ITTDRSQSVW LDYLVVVPLK
QYNDDLLVEE TFDQTKEFIQ NCGHDHFHIT HNASDFCKKS VFSLTADYNS GALPCNCDYA
GSTSFECHPF GGQCQCKPNV IERTCGACRS RYYGFPDCKP CKCPNSAMCE PTTGECMCPP
NVIGDLCEKC APNTYGFHQV IGCEECACNP MGIANGNSQC DLFNGTCECR QNIEGRACDV
CSNGYFNFPH CEQCSCHKPG TELEVCDKID GACFCKKNVV GRDCDQCVDG TYNLQESNPD
GCTTCFCFGK TSRCDSAYLR VYNVSLLKHV SITTPEFHEE SIKFDMWPVP ADEILLNETT
LKADFTLREV NDERPAYFGV LDYLLNQNNH ISAYGGDLAY TLHFTSGFDG KYIVAPDVIL
FSEHNALVHT SYEQPSRNEP FTNRVNIVES NFQTISGKPV SRADFMMVLR DLKVIFIRAN
YWEQTLVTHL SDVYLTLADE DADGTGEYQF LAVERCSCPP GYSGHSCEDC APGYYRDPSG
PYGGYCIPCE CNGHSETCDC ATGICSKCQH GTEGDHCERC VSGYYGNATN GTPGDCMICA
CPLPFDSNNF ATSCEISESG DQIHCECKPG YTGPRCESCA NGFYGEPESI GQVCKPCECS
GNINPEDQGS CDTRTGECLR CLNNTFGAAC NLCAPGFYGD AIKLKNCQSC DCDDLGTQTC
DPFVGVCTCH ENVIGDRCDR CKPDHYGFES GVGCRACDCG AASNSTQCDP HTGHCACKSG
VTGRQCDRCA VDHWKYEKDG CTPCNCNQGY SRGFGCNPNT GKCQCLPGVI GDRCDACPNR
WVLIKDEGCQ ECNNCHHALL DVTDRMRYQI DSVLEDFNSV TLAFFTSQKL NYYDQLADEL
EPKVKLLDPN SVDLSPSKKA NSELESDAKS YAKQVNQTLA NAFDIRERSS TTLGNITVAY
DEAVKSADQA KEAIASVEAL SKNLEAAAST KIDAALEQAQ HILGQINGTS IELTPNEQVL
EKARKLYEEV NTLVLPIKAQ NKSLNALKND IGEFSDHLED LFNWSEASQA KSADVERRNV
ANQKAFDNSK FDTVSEQKLQ AEKNIKDAGN FLINGDLTLN QINQKLDNLR DALNELNSFN
KNVDEELPVR EDQHKEADAL TDQAEQKAAE LAIKAQDLAA QYTDMTASAE PAIKAATAYS
GIVEAVEAAQ KLSQDAISAA GNATDKTDGI EERAHLADTG STDLLQRARQ SLQKVQDDLE
PRLNASAGKV QKISAVNNAT EHQLKDINKL IDQLPAESQR DMWKNSNANA SDALEILKNV
LEILEPVSVQ TPKELEKAHG INRDLDLTNK DVSQANKQLD DVEGSVSKLN ELAEDIEEQQ
HRVGSQSRQL GQEIENLKAQ VEAARQLANS IKVGVNFKPS TILELKTPEK TKLLATRTNL
STYFRTTEPS GFLLYLGNDN KTAQKNNDFV AVEIVNGYPI LTIDLGNGPE RITSDKYVAD
GRWYQAVVDR MGPNAKLTIR EELPNGDVVE HSKSGYLEGS QNILHVDKNS RLFVGGYPGI
SDFNAPPDLT TNSFSGDIED LKIGDESVGL WNFVYGDDND QGARERDVLL EKKKPVTGLR
FKGNGYVQLN ATSNLKSRSS IQFSFKADKD TSNGLLFFYG RDKHYMSIEM IDGAIFFNIS
LGEGGGVQSG SQDRYNDNQW HKVQAERENR NGLLKVDDIV ISRTNAPLEA DLELPKLRRL
YFGGHPRRLN TSISLQPNFD GCIDNVVINQ GVVDLTEYVT GGGVEEGCSA KFSTVVSYAP
HEYGFLRMNN VSSDNNLHVV LHFKTTQPNG VLFYAANHDQ SSTIGLSLQD GLLKLNSMGS
QLVIDDRILN DGEDHVVTVQ HTQGELRLTV DDVDNKRLGS PQPLILEGGD IFFAGLPDNY
RTPRNALASL AYFVGCISDV TVNEEIINFA NSAEKKNGNI NGCPPHVLAY EPSLVPSYYP
SGDNEVESPW SNADTLPPLK PDIESTLPPT TPTTTTTTTT TTTSTTTTST TTTTTTPSPI
VIDEEKEIEA KTPQKILTTR PPAKLNLPSD ERCKLPEQPN FDVDFTEAGY RFYGLREQRL
QINSLPVKVR RHHDIGISFR TERPNGLLIY AGSKQRDDFI AVYLLDGRVT YEIRVGAQLQ
AKITTEAELN DGTWHTVEVV RTQRKVSLLI DKLEQPGSVD LNAERSAPVL AVELPIYLGG
VNKFLESEVK NLTDFKTEVP YFNGCLKNIK FDAMDLETPP EEFGVVPCSE QVERGLFFNN
QKAFVKIFDH FDVGTEMKIS FDFRPRDPNG LLFSVHGKNS YAILELVDNT LYFTVKTDLK
NIVSTNYKLP NNESFCDGKT RNVQAIKSKF VINIAVDFIS SNPGVGNEGS VITRTNRPLF
LGGHVAFQRA PGIKTKKSFK GCISKVEVNQ RMINITPNMV VGDIWQGYCP LN
