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Protein

Laminin subunit beta-1

Gene

LanB1

Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Binding to cells via a high affinity receptor, laminin is thought to mediate the attachment, migration and organization of cells into tissues during embryonic development by interacting with other extracellular matrix components.

GO - Biological processi

  • animal organ development Source: FlyBase
  • basement membrane assembly Source: FlyBase
  • cardiac muscle cell development Source: FlyBase
  • cell adhesion mediated by integrin Source: FlyBase
  • cell migration Source: FlyBase
  • defense response to Gram-negative bacterium Source: FlyBase
  • embryonic heart tube morphogenesis Source: FlyBase
  • embryonic morphogenesis Source: FlyBase
  • extracellular matrix organization Source: FlyBase
  • gonad development Source: FlyBase
  • organ morphogenesis Source: FlyBase
  • positive regulation of innate immune response Source: FlyBase
  • substrate adhesion-dependent cell spreading Source: FlyBase
  • tissue development Source: FlyBase
Complete GO annotation...

Keywords - Biological processi

Cell adhesion

Names & Taxonomyi

Protein namesi
Recommended name:
Laminin subunit beta-1
Alternative name(s):
Laminin B1 chain
Gene namesi
Name:LanB1
Synonyms:lamB1
ORF Names:CG7123
OrganismiDrosophila melanogaster (Fruit fly)
Taxonomic identifieri7227 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
Proteomesi
  • UP000000803 Componenti: Chromosome 2L

Organism-specific databases

FlyBaseiFBgn0261800. LanB1.

Subcellular locationi

GO - Cellular componenti

  • basal lamina Source: FlyBase
  • basement membrane Source: FlyBase
  • endomembrane system Source: FlyBase
  • extracellular matrix Source: FlyBase
Complete GO annotation...

Keywords - Cellular componenti

Basement membrane, Extracellular matrix, Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2424Sequence analysisAdd
BLAST
Chaini25 – 17881764Laminin subunit beta-1PRO_0000017073Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi138 – 1381N-linked (GlcNAc...)Sequence analysis
Glycosylationi201 – 2011N-linked (GlcNAc...)Sequence analysis
Glycosylationi232 – 2321N-linked (GlcNAc...)Sequence analysis
Disulfide bondi288 ↔ 297PROSITE-ProRule annotation
Disulfide bondi290 ↔ 318PROSITE-ProRule annotation
Disulfide bondi320 ↔ 329PROSITE-ProRule annotation
Disulfide bondi332 ↔ 352PROSITE-ProRule annotation
Disulfide bondi355 ↔ 364PROSITE-ProRule annotation
Disulfide bondi357 ↔ 382PROSITE-ProRule annotation
Disulfide bondi385 ↔ 394PROSITE-ProRule annotation
Disulfide bondi397 ↔ 415PROSITE-ProRule annotation
Disulfide bondi418 ↔ 431PROSITE-ProRule annotation
Disulfide bondi420 ↔ 446PROSITE-ProRule annotation
Disulfide bondi448 ↔ 457PROSITE-ProRule annotation
Disulfide bondi460 ↔ 475PROSITE-ProRule annotation
Disulfide bondi478 ↔ 491PROSITE-ProRule annotation
Disulfide bondi480 ↔ 498PROSITE-ProRule annotation
Glycosylationi487 – 4871N-linked (GlcNAc...)Sequence analysis
Disulfide bondi500 ↔ 509PROSITE-ProRule annotation
Disulfide bondi512 ↔ 526PROSITE-ProRule annotation
Disulfide bondi529 ↔ 541PROSITE-ProRule annotation
Disulfide bondi531 ↔ 548PROSITE-ProRule annotation
Disulfide bondi550 ↔ 559PROSITE-ProRule annotation
Glycosylationi591 – 5911N-linked (GlcNAc...)Sequence analysis
Disulfide bondi789 ↔ 801PROSITE-ProRule annotation
Disulfide bondi791 ↔ 808PROSITE-ProRule annotation
Disulfide bondi810 ↔ 819PROSITE-ProRule annotation
Disulfide bondi822 ↔ 834PROSITE-ProRule annotation
Disulfide bondi837 ↔ 849PROSITE-ProRule annotation
Disulfide bondi839 ↔ 856PROSITE-ProRule annotation
Disulfide bondi858 ↔ 867PROSITE-ProRule annotation
Disulfide bondi870 ↔ 880PROSITE-ProRule annotation
Disulfide bondi883 ↔ 892PROSITE-ProRule annotation
Disulfide bondi885 ↔ 899PROSITE-ProRule annotation
Disulfide bondi902 ↔ 911PROSITE-ProRule annotation
Disulfide bondi914 ↔ 930PROSITE-ProRule annotation
Disulfide bondi933 ↔ 949PROSITE-ProRule annotation
Disulfide bondi935 ↔ 960PROSITE-ProRule annotation
Disulfide bondi962 ↔ 971PROSITE-ProRule annotation
Disulfide bondi974 ↔ 988PROSITE-ProRule annotation
Disulfide bondi991 ↔ 1005PROSITE-ProRule annotation
Disulfide bondi993 ↔ 1012PROSITE-ProRule annotation
Disulfide bondi1015 ↔ 1024PROSITE-ProRule annotation
Disulfide bondi1027 ↔ 1040PROSITE-ProRule annotation
Disulfide bondi1043 ↔ 1057PROSITE-ProRule annotation
Disulfide bondi1045 ↔ 1064PROSITE-ProRule annotation
Glycosylationi1051 – 10511N-linked (GlcNAc...)Sequence analysis
Disulfide bondi1066 ↔ 1075PROSITE-ProRule annotation
Disulfide bondi1078 ↔ 1091PROSITE-ProRule annotation
Disulfide bondi1094 ↔ 1106PROSITE-ProRule annotation
Disulfide bondi1096 ↔ 1113PROSITE-ProRule annotation
Disulfide bondi1115 ↔ 1124PROSITE-ProRule annotation
Disulfide bondi1127 ↔ 1139PROSITE-ProRule annotation
Disulfide bondi1142 ↔ 1154PROSITE-ProRule annotation
Disulfide bondi1144 ↔ 1161PROSITE-ProRule annotation
Disulfide bondi1163 ↔ 1172PROSITE-ProRule annotation
Disulfide bondi1175 ↔ 1186PROSITE-ProRule annotation
Disulfide bondi1189 – 1189InterchainCurated
Disulfide bondi1192 – 1192InterchainCurated
Glycosylationi1246 – 12461N-linked (GlcNAc...)Sequence analysis
Glycosylationi1301 – 13011N-linked (GlcNAc...)Sequence analysis
Glycosylationi1330 – 13301N-linked (GlcNAc...)Sequence analysis
Glycosylationi1341 – 13411N-linked (GlcNAc...)Sequence analysis
Glycosylationi1473 – 14731N-linked (GlcNAc...)Sequence analysis
Glycosylationi1493 – 14931N-linked (GlcNAc...)1 Publication
Glycosylationi1515 – 15151N-linked (GlcNAc...)Sequence analysis
Glycosylationi1581 – 15811N-linked (GlcNAc...)Sequence analysis
Glycosylationi1644 – 16441N-linked (GlcNAc...)Sequence analysis
Glycosylationi1703 – 17031N-linked (GlcNAc...)Sequence analysis
Disulfide bondi1786 – 1786InterchainCurated

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

PaxDbiP11046.
PRIDEiP11046.

Expressioni

Tissue specificityi

Found in the basement membranes (major component).

Gene expression databases

BgeeiP11046.
GenevisibleiP11046. DM.

Interactioni

Subunit structurei

Laminin is a complex glycoprotein, consisting of three different polypeptide chains (alpha, beta, gamma), which are bound to each other by disulfide bonds into a cross-shaped molecule comprising one long and three short arms with globules at each end.

Protein-protein interaction databases

BioGridi60207. 17 interactions.
IntActiP11046. 9 interactions.
MINTiMINT-749338.
STRINGi7227.FBpp0079113.

Structurei

3D structure databases

ProteinModelPortaliP11046.
SMRiP11046. Positions 49-567, 800-1190.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini50 – 287238Laminin N-terminalPROSITE-ProRule annotationAdd
BLAST
Domaini288 – 35467Laminin EGF-like 1PROSITE-ProRule annotationAdd
BLAST
Domaini355 – 41763Laminin EGF-like 2PROSITE-ProRule annotationAdd
BLAST
Domaini418 – 47760Laminin EGF-like 3PROSITE-ProRule annotationAdd
BLAST
Domaini478 – 52851Laminin EGF-like 4PROSITE-ProRule annotationAdd
BLAST
Domaini529 – 55931Laminin EGF-like 5; truncatedPROSITE-ProRule annotationAdd
BLAST
Domaini567 – 783217Laminin IV type BPROSITE-ProRule annotationAdd
BLAST
Domaini789 – 83648Laminin EGF-like 6PROSITE-ProRule annotationAdd
BLAST
Domaini837 – 88246Laminin EGF-like 7PROSITE-ProRule annotationAdd
BLAST
Domaini883 – 93250Laminin EGF-like 8PROSITE-ProRule annotationAdd
BLAST
Domaini933 – 99058Laminin EGF-like 9PROSITE-ProRule annotationAdd
BLAST
Domaini991 – 104252Laminin EGF-like 10PROSITE-ProRule annotationAdd
BLAST
Domaini1043 – 109351Laminin EGF-like 11PROSITE-ProRule annotationAdd
BLAST
Domaini1094 – 114148Laminin EGF-like 12PROSITE-ProRule annotationAdd
BLAST
Domaini1142 – 118847Laminin EGF-like 13PROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1189 – 1405217Domain IIAdd
BLAST
Regioni1406 – 143227Domain alphaAdd
BLAST
Regioni1433 – 1788356Domain IAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili1255 – 1405151Sequence analysisAdd
BLAST
Coiled coili1453 – 150553Sequence analysisAdd
BLAST
Coiled coili1540 – 156122Sequence analysisAdd
BLAST
Coiled coili1608 – 1762155Sequence analysisAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi641 – 6433Cell attachment siteSequence analysis

Domaini

The alpha-helical domains I and II are thought to interact with other laminin chains to form a coiled coil structure.
Domains VI and IV are globular.

Sequence similaritiesi

Contains 13 laminin EGF-like domains.PROSITE-ProRule annotation
Contains 1 laminin IV type B domain.PROSITE-ProRule annotation
Contains 1 laminin N-terminal domain.PROSITE-ProRule annotation

Keywords - Domaini

Coiled coil, Laminin EGF-like domain, Repeat, Signal

Phylogenomic databases

eggNOGiKOG0994. Eukaryota.
ENOG410XPEG. LUCA.
GeneTreeiENSGT00780000121851.
InParanoidiP11046.
KOiK05636.
OMAiNCRTDEG.
OrthoDBiEOG75XGK0.
PhylomeDBiP11046.

Family and domain databases

InterProiIPR013032. EGF-like_CS.
IPR000742. EGF-like_dom.
IPR002049. Laminin_EGF.
IPR013015. Laminin_IV_B.
IPR008211. Laminin_N.
[Graphical view]
PfamiPF00053. Laminin_EGF. 13 hits.
PF00055. Laminin_N. 1 hit.
[Graphical view]
SMARTiSM00181. EGF. 8 hits.
SM00180. EGF_Lam. 13 hits.
SM00136. LamNT. 1 hit.
[Graphical view]
PROSITEiPS00022. EGF_1. 10 hits.
PS01186. EGF_2. 2 hits.
PS01248. EGF_LAM_1. 12 hits.
PS50027. EGF_LAM_2. 13 hits.
PS51116. LAMININ_IVB. 1 hit.
PS51117. LAMININ_NTER. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P11046-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLELRLIVVI VLALLSWQWD PVDSQRPPQH GRRDRPKYPP NKFIKTHPCE
60 70 80 90 100
RSSCYPATGN LLIGRENRLT ASSTCGLHSP ERFCILSHLQ DKKCFLCDTR
110 120 130 140 150
EETKHDPYKN HRIGQIIYKT KPGTNIPTWW QSENGKENAT IQLDLEAEFH
160 170 180 190 200
FTHLIITFTT FRPAAMYIER SFDFGQTWHI YRYFAYDCKE SFPGVPTVLE
210 220 230 240 250
NITDVMCTSR YSNVEPSRNG EVIFRVLPPN INVTDPYAEH VQNQLKMTNL
260 270 280 290 300
RIQMTKLHKL GDNLLDSRLE NEEKYYYGIS NMVVRGSCSC YGHASQCLPL
310 320 330 340 350
DPAFSQADNE DGMVHGRCEC THNTKGMNCE ECEDFFNDLP WKPAFGKKTN
360 370 380 390 400
ACKKCECNDH AVSCHFDEAV FTASGFVSGG VCDNCLHNTR GQHCEECMPY
410 420 430 440 450
FYRDPEQDIT SERVCQPCDC DPQGSSDDGI CDSLNELEEG AVAGACHCKA
460 470 480 490 500
FVTGRRCNQC KDGYWNLQSD NPEGCEPCTC NPLGTLNNSG CVMRTGECKC
510 520 530 540 550
KKYVTGKDCN QCMPETYGLS ESPEGCSLCN CDAGGSYDNY CDVISGQCRC
560 570 580 590 600
RPHMTGRSCS QPKQNYFIPL LPEVHEAEVV DECISYGANG NCSLVAETPD
610 620 630 640 650
GSFTGIGFTR VPENSELVFT VGDIPRSMPY DAVIRYQSTS RGDWENAFIT
660 670 680 690 700
LVRPDQVDPE GGCGELAAAT SSETRIPFSL PDRSRQVVAL NEVCLEAGKV
710 720 730 740 750
YKFRIYFERK RHDVDSPTAT ILVDSLTLIP RIDVTPIFQG SVLADIRKKD
760 770 780 790 800
YEKYNCKSSL YDMNYKSDPK CQNLDNILSV FVHDGASMCN CNPTGSLSKV
810 820 830 840 850
CESNGGYCQC KPNVVGRQCD QCAPGTYGFG PEGCKACDCN SIGSKDKYCD
860 870 880 890 900
LITGQCQCVP NTYGRECNQC QPGYWNFPEC RVCQCNGHAA TCDPIQGTCI
910 920 930 940 950
DCQDSTTGYS CDSCLDGYYG NPLFGSEIGC RPCRCPETVA SGLAHADGCS
960 970 980 990 1000
LDTRNNNMLC HCQEGYSGSR CEICADNFFG NPDNGGTCSK CECSNNVDLY
1010 1020 1030 1040 1050
DTGNCDRQTG ACLKCLYQTT GDHCELCKDG FFGDALQQNC QQCECDFLGT
1060 1070 1080 1090 1100
NNTIAHCDRF TGQCPCLPNV QGVRCDQCAE NHWKIASGEG CESCNCDPIG
1110 1120 1130 1140 1150
ALHEQCNSYT GQCQCKPGFG GRACNQCQAH YWGNPNEKCQ PCECDQFGAA
1160 1170 1180 1190 1200
DFQCDRETGN CVCHEGIGGY KCNECARGYI GQFPHCSPCG ECFNNWDLIL
1210 1220 1230 1240 1250
SALEDATTAT ILRAKEIKQV GATGAYTSEF SELDKKLQHI RNLLQNTSVS
1260 1270 1280 1290 1300
LVDIEKLDYE TQSLRDQLQA SHGRLSETEQ NLDDIYNSLS LSGVELESLQ
1310 1320 1330 1340 1350
NHSRLVQQLS KELKENGIQL QESNIEGALN LTRHAYERVS NLSTLKDEAN
1360 1370 1380 1390 1400
ELASNTDRNC KRVENLSNKI QAEADDLANN NKLIEDYRAE LTSLTSQIPE
1410 1420 1430 1440 1450
LNNQVCGKPG DPCDSLCGGA GCGHCGGFLS CEHGAKTHSE EALKVAKDAE
1460 1470 1480 1490 1500
TAITSKKDQA DQTIRALTQA KLNASEAYEK AKRGFEQSER YLNQTNANIK
1510 1520 1530 1540 1550
LAENLFIALN NFQENKTASP SESKELAQKT LDLDLKLEPE EIETLGDQIN
1560 1570 1580 1590 1600
RAVSSLKNVE AIIYRTKPDL DRVNNLQSIA NATKEKADKI LDSANSVVES
1610 1620 1630 1640 1650
LAAADESQGK AKDAIQQANS NIELAGQDLE KIDEETYSAE APANNTAQQV
1660 1670 1680 1690 1700
EKLAKKVQKL QNNIMKNDRD AKEITKEAGS VKLEAMRARG EANNLQSATS
1710 1720 1730 1740 1750
ATNQTLTDRA SRSENARERA KQLLQRASKL TVDTNAKLKD LNDLQTVYLN
1760 1770 1780
KNQQLLRLQA EIGPLNKELN EHLIHIKERG SHYRQCYT
Length:1,788
Mass (Da):198,333
Last modified:November 13, 2007 - v4
Checksum:i7CB99C9608452085
GO

Sequence cautioni

The sequence AAM11329.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
The sequence AAT94451.1 differs from that shown. Reason: Frameshift at position 458. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti12 – 121L → LAL in AAD19752 (PubMed:8397815).Curated
Sequence conflicti12 – 121L → LAL in AAA28663 (PubMed:3365769).Curated
Sequence conflicti666 – 6661L → H in AAD19752 (PubMed:8397815).Curated
Sequence conflicti724 – 7252DS → VT in AAA28663 (PubMed:3365769).Curated
Sequence conflicti766 – 7672KS → NA in AAD19752 (PubMed:8397815).Curated
Sequence conflicti766 – 7672KS → NA in AAA28663 (PubMed:3365769).Curated
Sequence conflicti939 – 9391V → I in AAT94451 (Ref. 5) Curated
Sequence conflicti946 – 9472Missing in AAD19752 (PubMed:8397815).Curated
Sequence conflicti946 – 9472Missing in AAA28663 (PubMed:3365769).Curated
Sequence conflicti1356 – 137318TDRNC…KIQAE → SDRIAREWKICLIRFRPN in AAD19752 (PubMed:8397815).CuratedAdd
BLAST
Sequence conflicti1356 – 137318TDRNC…KIQAE → SDRIAREWKICLIRFRPN in AAA28663 (PubMed:3365769).CuratedAdd
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M95811 Genomic DNA. Translation: AAD19752.1.
M19525 mRNA. Translation: AAA28663.1.
AE014134 Genomic DNA. Translation: AAF52563.1.
AE014134 Genomic DNA. Translation: AAN10647.1.
BT015222 mRNA. Translation: AAT94451.1. Frameshift.
AY095001 mRNA. Translation: AAM11329.1. Different initiation.
PIRiA28783. MMFFB1.
RefSeqiNP_476618.1. NM_057270.5.
NP_723319.1. NM_164773.3.

Genome annotation databases

EnsemblMetazoaiFBtr0079490; FBpp0079113; FBgn0261800.
FBtr0079491; FBpp0079114; FBgn0261800.
GeneIDi34068.
KEGGidme:Dmel_CG7123.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M95811 Genomic DNA. Translation: AAD19752.1.
M19525 mRNA. Translation: AAA28663.1.
AE014134 Genomic DNA. Translation: AAF52563.1.
AE014134 Genomic DNA. Translation: AAN10647.1.
BT015222 mRNA. Translation: AAT94451.1. Frameshift.
AY095001 mRNA. Translation: AAM11329.1. Different initiation.
PIRiA28783. MMFFB1.
RefSeqiNP_476618.1. NM_057270.5.
NP_723319.1. NM_164773.3.

3D structure databases

ProteinModelPortaliP11046.
SMRiP11046. Positions 49-567, 800-1190.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi60207. 17 interactions.
IntActiP11046. 9 interactions.
MINTiMINT-749338.
STRINGi7227.FBpp0079113.

Proteomic databases

PaxDbiP11046.
PRIDEiP11046.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaiFBtr0079490; FBpp0079113; FBgn0261800.
FBtr0079491; FBpp0079114; FBgn0261800.
GeneIDi34068.
KEGGidme:Dmel_CG7123.

Organism-specific databases

CTDi34068.
FlyBaseiFBgn0261800. LanB1.

Phylogenomic databases

eggNOGiKOG0994. Eukaryota.
ENOG410XPEG. LUCA.
GeneTreeiENSGT00780000121851.
InParanoidiP11046.
KOiK05636.
OMAiNCRTDEG.
OrthoDBiEOG75XGK0.
PhylomeDBiP11046.

Miscellaneous databases

ChiTaRSiLanB1. fly.
GenomeRNAii34068.
PROiP11046.

Gene expression databases

BgeeiP11046.
GenevisibleiP11046. DM.

Family and domain databases

InterProiIPR013032. EGF-like_CS.
IPR000742. EGF-like_dom.
IPR002049. Laminin_EGF.
IPR013015. Laminin_IV_B.
IPR008211. Laminin_N.
[Graphical view]
PfamiPF00053. Laminin_EGF. 13 hits.
PF00055. Laminin_N. 1 hit.
[Graphical view]
SMARTiSM00181. EGF. 8 hits.
SM00180. EGF_Lam. 13 hits.
SM00136. LamNT. 1 hit.
[Graphical view]
PROSITEiPS00022. EGF_1. 10 hits.
PS01186. EGF_2. 2 hits.
PS01248. EGF_LAM_1. 12 hits.
PS50027. EGF_LAM_2. 13 hits.
PS51116. LAMININ_IVB. 1 hit.
PS51117. LAMININ_NTER. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Analysis of the Drosophila gene for the laminin B1 chain."
    Gow C.-H., Chang H.-Y., Lih C.-J., Chang T.-W., Hui C.-F.
    DNA Cell Biol. 12:573-587(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: Canton-S.
  2. "Drosophila substrate adhesion molecule: sequence of laminin B1 chain reveals domains of homology with mouse."
    Montell D.J., Goodman C.S.
    Cell 53:463-473(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  3. "The genome sequence of Drosophila melanogaster."
    Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., Sutton G.G., Wortman J.R., Yandell M.D.
    , Zhang Q., Chen L.X., Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J., Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.
    Science 287:2185-2195(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Berkeley.
  4. Cited for: GENOME REANNOTATION.
    Strain: Berkeley.
  5. Stapleton M., Carlson J.W., Chavez C., Frise E., George R.A., Pacleb J.M., Park S., Wan K.H., Yu C., Rubin G.M., Celniker S.E.
    Submitted (AUG-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: Berkeley.
    Tissue: Embryo.
  6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 715-1788.
    Strain: Berkeley.
    Tissue: Head.
  7. "Identification of N-glycosylated proteins from the central nervous system of Drosophila melanogaster."
    Koles K., Lim J.-M., Aoki K., Porterfield M., Tiemeyer M., Wells L., Panin V.
    Glycobiology 17:1388-1403(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-1493, IDENTIFICATION BY MASS SPECTROMETRY.
    Strain: Oregon-R.
    Tissue: Head.

Entry informationi

Entry nameiLAMB1_DROME
AccessioniPrimary (citable) accession number: P11046
Secondary accession number(s): A4V0D8
, Q26328, Q6AWM6, Q8SWY0, Q9VLW6, Q9XZT4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: November 13, 2007
Last modified: July 6, 2016
This is version 164 of the entry and version 4 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Drosophila
    Drosophila: entries, gene names and cross-references to FlyBase
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.