Skip Header

Contribute Send feedback
Read comments (?) or add your own

P11046 (LAMB1_DROME) Reviewed, UniProtKB/Swiss-Prot

Last modified May 29, 2013. Version 135. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Laminin subunit beta-1
Alternative name(s):
Laminin B1 chain
Gene names
Name:LanB1
Synonyms:lamB1
ORF Names:CG7123
OrganismDrosophila melanogaster (Fruit fly) [Reference proteome]
Taxonomic identifier7227 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Ecdysozoa › Arthropoda › Hexapoda › Insecta › Pterygota › Neoptera › Endopterygota › Diptera › Brachycera › Muscomorpha › Ephydroidea › Drosophilidae › Drosophila › Sophophora ›

Protein attributes

Sequence length1788 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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.

Subunit structure

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.

Subcellular location

Secreted › extracellular space › extracellular matrix › basement membrane.

Tissue specificity

Found in the basement membranes (major component).

Domain

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 similarities

Contains 13 laminin EGF-like domains.

Contains 1 laminin IV type B domain.

Contains 1 laminin N-terminal domain.

Sequence caution

The sequence AAM11329.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

The sequence AAT94451.1 differs from that shown. Reason: Frameshift at position 458.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2424 Potential
Chain25 – 17881764Laminin subunit beta-1
PRO_0000017073

Regions

Domain50 – 287238Laminin N-terminal
Domain288 – 35467Laminin EGF-like 1
Domain355 – 41763Laminin EGF-like 2
Domain418 – 47760Laminin EGF-like 3
Domain478 – 52851Laminin EGF-like 4
Domain529 – 55931Laminin EGF-like 5; truncated
Domain567 – 783217Laminin IV type B
Domain789 – 83648Laminin EGF-like 6
Domain837 – 88246Laminin EGF-like 7
Domain883 – 93250Laminin EGF-like 8
Domain933 – 99058Laminin EGF-like 9
Domain991 – 104252Laminin EGF-like 10
Domain1043 – 109351Laminin EGF-like 11
Domain1094 – 114148Laminin EGF-like 12
Domain1142 – 118847Laminin EGF-like 13
Region1189 – 1405217Domain II
Region1406 – 143227Domain alpha
Region1433 – 1788356Domain I
Coiled coil1255 – 1405151 Potential
Coiled coil1453 – 150553 Potential
Coiled coil1540 – 156122 Potential
Coiled coil1608 – 1762155 Potential
Motif641 – 6433Cell attachment site Potential

Amino acid modifications

Glycosylation1381N-linked (GlcNAc...) Potential
Glycosylation2011N-linked (GlcNAc...) Potential
Glycosylation2321N-linked (GlcNAc...) Potential
Glycosylation4871N-linked (GlcNAc...) Potential
Glycosylation5911N-linked (GlcNAc...) Potential
Glycosylation10511N-linked (GlcNAc...) Potential
Glycosylation12461N-linked (GlcNAc...) Potential
Glycosylation13011N-linked (GlcNAc...) Potential
Glycosylation13301N-linked (GlcNAc...) Potential
Glycosylation13411N-linked (GlcNAc...) Potential
Glycosylation14731N-linked (GlcNAc...) Potential
Glycosylation14931N-linked (GlcNAc...) Ref.7
Glycosylation15151N-linked (GlcNAc...) Potential
Glycosylation15811N-linked (GlcNAc...) Potential
Glycosylation16441N-linked (GlcNAc...) Potential
Glycosylation17031N-linked (GlcNAc...) Potential
Disulfide bond288 ↔ 297 By similarity
Disulfide bond290 ↔ 318 By similarity
Disulfide bond320 ↔ 329 By similarity
Disulfide bond332 ↔ 352 By similarity
Disulfide bond355 ↔ 364 By similarity
Disulfide bond357 ↔ 382 By similarity
Disulfide bond385 ↔ 394 By similarity
Disulfide bond397 ↔ 415 By similarity
Disulfide bond418 ↔ 431 By similarity
Disulfide bond420 ↔ 446 By similarity
Disulfide bond448 ↔ 457 By similarity
Disulfide bond460 ↔ 475 By similarity
Disulfide bond478 ↔ 491 By similarity
Disulfide bond480 ↔ 498 By similarity
Disulfide bond500 ↔ 509 By similarity
Disulfide bond512 ↔ 526 By similarity
Disulfide bond529 ↔ 541 By similarity
Disulfide bond531 ↔ 548 By similarity
Disulfide bond550 ↔ 559 By similarity
Disulfide bond789 ↔ 801 By similarity
Disulfide bond791 ↔ 808 By similarity
Disulfide bond810 ↔ 819 By similarity
Disulfide bond822 ↔ 834 By similarity
Disulfide bond837 ↔ 849 By similarity
Disulfide bond839 ↔ 856 By similarity
Disulfide bond858 ↔ 867 By similarity
Disulfide bond870 ↔ 880 By similarity
Disulfide bond883 ↔ 892 By similarity
Disulfide bond885 ↔ 899 By similarity
Disulfide bond902 ↔ 911 By similarity
Disulfide bond914 ↔ 930 By similarity
Disulfide bond933 ↔ 949 By similarity
Disulfide bond935 ↔ 960 By similarity
Disulfide bond962 ↔ 971 By similarity
Disulfide bond974 ↔ 988 By similarity
Disulfide bond991 ↔ 1005 By similarity
Disulfide bond993 ↔ 1012 By similarity
Disulfide bond1015 ↔ 1024 By similarity
Disulfide bond1027 ↔ 1040 By similarity
Disulfide bond1043 ↔ 1057 By similarity
Disulfide bond1045 ↔ 1064 By similarity
Disulfide bond1066 ↔ 1075 By similarity
Disulfide bond1078 ↔ 1091 By similarity
Disulfide bond1094 ↔ 1106 By similarity
Disulfide bond1096 ↔ 1113 By similarity
Disulfide bond1115 ↔ 1124 By similarity
Disulfide bond1127 ↔ 1139 By similarity
Disulfide bond1142 ↔ 1154 By similarity
Disulfide bond1144 ↔ 1161 By similarity
Disulfide bond1163 ↔ 1172 By similarity
Disulfide bond1175 ↔ 1186 By similarity
Disulfide bond1189Interchain Probable
Disulfide bond1192Interchain Probable
Disulfide bond1786Interchain Probable

Experimental info

Sequence conflict121L → LAL in AAD19752. Ref.1
Sequence conflict121L → LAL in AAA28663. Ref.2
Sequence conflict6661L → H in AAD19752. Ref.1
Sequence conflict724 – 7252DS → VT in AAA28663. Ref.2
Sequence conflict766 – 7672KS → NA in AAD19752. Ref.1
Sequence conflict766 – 7672KS → NA in AAA28663. Ref.2
Sequence conflict9391V → I in AAT94451. Ref.5
Sequence conflict946 – 9472Missing in AAD19752. Ref.1
Sequence conflict946 – 9472Missing in AAA28663. Ref.2
Sequence conflict1356 – 137318TDRNC…KIQAE → SDRIAREWKICLIRFRPN in AAD19752. Ref.1
Sequence conflict1356 – 137318TDRNC…KIQAE → SDRIAREWKICLIRFRPN in AAA28663. Ref.2

Sequences

Sequence LengthMass (Da)Tools
P11046 [UniParc].

Last modified November 13, 2007. Version 4.
Checksum: 7CB99C9608452085

FASTA1,788198,333
        10         20         30         40         50         60 
MLELRLIVVI VLALLSWQWD PVDSQRPPQH GRRDRPKYPP NKFIKTHPCE RSSCYPATGN 

        70         80         90        100        110        120 
LLIGRENRLT ASSTCGLHSP ERFCILSHLQ DKKCFLCDTR EETKHDPYKN HRIGQIIYKT 

       130        140        150        160        170        180 
KPGTNIPTWW QSENGKENAT IQLDLEAEFH FTHLIITFTT FRPAAMYIER SFDFGQTWHI 

       190        200        210        220        230        240 
YRYFAYDCKE SFPGVPTVLE NITDVMCTSR YSNVEPSRNG EVIFRVLPPN INVTDPYAEH 

       250        260        270        280        290        300 
VQNQLKMTNL RIQMTKLHKL GDNLLDSRLE NEEKYYYGIS NMVVRGSCSC YGHASQCLPL 

       310        320        330        340        350        360 
DPAFSQADNE DGMVHGRCEC THNTKGMNCE ECEDFFNDLP WKPAFGKKTN ACKKCECNDH 

       370        380        390        400        410        420 
AVSCHFDEAV FTASGFVSGG VCDNCLHNTR GQHCEECMPY FYRDPEQDIT SERVCQPCDC 

       430        440        450        460        470        480 
DPQGSSDDGI CDSLNELEEG AVAGACHCKA FVTGRRCNQC KDGYWNLQSD NPEGCEPCTC 

       490        500        510        520        530        540 
NPLGTLNNSG CVMRTGECKC KKYVTGKDCN QCMPETYGLS ESPEGCSLCN CDAGGSYDNY 

       550        560        570        580        590        600 
CDVISGQCRC RPHMTGRSCS QPKQNYFIPL LPEVHEAEVV DECISYGANG NCSLVAETPD 

       610        620        630        640        650        660 
GSFTGIGFTR VPENSELVFT VGDIPRSMPY DAVIRYQSTS RGDWENAFIT LVRPDQVDPE 

       670        680        690        700        710        720 
GGCGELAAAT SSETRIPFSL PDRSRQVVAL NEVCLEAGKV YKFRIYFERK RHDVDSPTAT 

       730        740        750        760        770        780 
ILVDSLTLIP RIDVTPIFQG SVLADIRKKD YEKYNCKSSL YDMNYKSDPK CQNLDNILSV 

       790        800        810        820        830        840 
FVHDGASMCN CNPTGSLSKV CESNGGYCQC KPNVVGRQCD QCAPGTYGFG PEGCKACDCN 

       850        860        870        880        890        900 
SIGSKDKYCD LITGQCQCVP NTYGRECNQC QPGYWNFPEC RVCQCNGHAA TCDPIQGTCI 

       910        920        930        940        950        960 
DCQDSTTGYS CDSCLDGYYG NPLFGSEIGC RPCRCPETVA SGLAHADGCS LDTRNNNMLC 

       970        980        990       1000       1010       1020 
HCQEGYSGSR CEICADNFFG NPDNGGTCSK CECSNNVDLY DTGNCDRQTG ACLKCLYQTT 

      1030       1040       1050       1060       1070       1080 
GDHCELCKDG FFGDALQQNC QQCECDFLGT NNTIAHCDRF TGQCPCLPNV QGVRCDQCAE 

      1090       1100       1110       1120       1130       1140 
NHWKIASGEG CESCNCDPIG ALHEQCNSYT GQCQCKPGFG GRACNQCQAH YWGNPNEKCQ 

      1150       1160       1170       1180       1190       1200 
PCECDQFGAA DFQCDRETGN CVCHEGIGGY KCNECARGYI GQFPHCSPCG ECFNNWDLIL 

      1210       1220       1230       1240       1250       1260 
SALEDATTAT ILRAKEIKQV GATGAYTSEF SELDKKLQHI RNLLQNTSVS LVDIEKLDYE 

      1270       1280       1290       1300       1310       1320 
TQSLRDQLQA SHGRLSETEQ NLDDIYNSLS LSGVELESLQ NHSRLVQQLS KELKENGIQL 

      1330       1340       1350       1360       1370       1380 
QESNIEGALN LTRHAYERVS NLSTLKDEAN ELASNTDRNC KRVENLSNKI QAEADDLANN 

      1390       1400       1410       1420       1430       1440 
NKLIEDYRAE LTSLTSQIPE LNNQVCGKPG DPCDSLCGGA GCGHCGGFLS CEHGAKTHSE 

      1450       1460       1470       1480       1490       1500 
EALKVAKDAE TAITSKKDQA DQTIRALTQA KLNASEAYEK AKRGFEQSER YLNQTNANIK 

      1510       1520       1530       1540       1550       1560 
LAENLFIALN NFQENKTASP SESKELAQKT LDLDLKLEPE EIETLGDQIN RAVSSLKNVE 

      1570       1580       1590       1600       1610       1620 
AIIYRTKPDL DRVNNLQSIA NATKEKADKI LDSANSVVES LAAADESQGK AKDAIQQANS 

      1630       1640       1650       1660       1670       1680 
NIELAGQDLE KIDEETYSAE APANNTAQQV EKLAKKVQKL QNNIMKNDRD AKEITKEAGS 

      1690       1700       1710       1720       1730       1740 
VKLEAMRARG EANNLQSATS ATNQTLTDRA SRSENARERA KQLLQRASKL TVDTNAKLKD 

      1750       1760       1770       1780 
LNDLQTVYLN KNQQLLRLQA EIGPLNKELN EHLIHIKERG SHYRQCYT

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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]"Annotation of the Drosophila melanogaster euchromatic genome: a systematic review."
Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., Bettencourt B.R., Celniker S.E., de Grey A.D.N.J. expand/collapse author list , Drysdale R.A., Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.
Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002) [PubMed] [Europe PMC] [Abstract]
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]"A Drosophila full-length cDNA resource."
Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M., Celniker S.E.
Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002) [PubMed] [Europe PMC] [Abstract]
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, MASS SPECTROMETRY.
Strain: Oregon-R.
Tissue: Head.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		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.
PIRMMFFB1. A28783.
RefSeqNP_476618.1. NM_057270.4.
NP_723319.1. NM_164773.2.
UniGeneDm.4756.

3D structure databases

ProteinModelPortalP11046.
SMRP11046. Positions 49-567, 789-1174.
ModBaseSearch...

Protein-protein interaction databases

IntActP11046. 3 interactions.
MINTMINT-749338.

Proteomic databases

PaxDbP11046.
PRIDEP11046.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaFBtr0079490; FBpp0079113; FBgn0261800.
FBtr0079491; FBpp0079114; FBgn0261800.
GeneID34068.
KEGGdme:Dmel_CG7123.

Organism-specific databases

CTD34068.
FlyBaseFBgn0261800. LanB1.

Phylogenomic databases

eggNOGNOG241384.
GeneTreeENSGT00620000087753.
InParanoidP11046.
KOK05636.
OMADQCAENH.
OrthoDBEOG4ZPC92.
PhylomeDBP11046.

Gene expression databases

BgeeP11046.
GermOnlineCG7123. Drosophila melanogaster.

Family and domain databases

InterProIPR013032. EGF-like_CS.
IPR002049. EGF_laminin.
IPR013015. Laminin_IV.
IPR008211. Laminin_N.
[Graphical view]
PfamPF00053. Laminin_EGF. 13 hits.
PF00055. Laminin_N. 1 hit.
[Graphical view]
SMARTSM00180. EGF_Lam. 13 hits.
SM00136. LamNT. 1 hit.
[Graphical view]
PROSITEPS00022. 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]
ProtoNetSearch...

Other

ChiTaRSLanB1. drosophila.
GenomeRNAi34068.
NextBio786713.

Entry information

Entry nameLAMB1_DROME
AccessionPrimary (citable) accession number: P11046
Secondary accession number(s): A4V0D8 expand/collapse secondary AC list , Q26328, Q6AWM6, Q8SWY0, Q9VLW6, Q9XZT4
Entry history
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: November 13, 2007
Last modified: May 29, 2013
This is version 135 of the entry and version 4 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Relevant documents

Drosophila

Drosophila: entries, gene names and cross-references to FlyBase

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents