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Protein

Laminin subunit gamma-1

Gene

LanB2

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

  • basement membrane assembly Source: FlyBase
  • cell adhesion mediated by integrin Source: FlyBase
  • endodermal digestive tract morphogenesis Source: FlyBase
  • extracellular matrix assembly Source: FlyBase
  • midgut development Source: FlyBase
  • salivary gland morphogenesis Source: FlyBase
  • substrate adhesion-dependent cell spreading Source: FlyBase
Complete GO annotation...

Keywords - Biological processi

Cell adhesion

Enzyme and pathway databases

ReactomeiR-DME-446107. Type I hemidesmosome assembly.

Names & Taxonomyi

Protein namesi
Recommended name:
Laminin subunit gamma-1
Alternative name(s):
Laminin B2 chain
Gene namesi
Name:LanB2
Synonyms:LAMC1, LAMG1
ORF Names:CG3322
OrganismiDrosophila melanogaster (Fruit fly)
Taxonomic identifieri7227 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
Proteomesi
  • UP000000803 Componenti: Chromosome 3L

Organism-specific databases

FlyBaseiFBgn0267348. LanB2.

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)DescriptionActionsGraphical viewLength
Signal peptidei1 – 33Sequence analysisAdd BLAST33
ChainiPRO_000001708134 – 1639Laminin subunit gamma-1Add BLAST1606

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi147N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi299 ↔ 308PROSITE-ProRule annotation
Disulfide bondi301 ↔ 322PROSITE-ProRule annotation
Disulfide bondi324 ↔ 333PROSITE-ProRule annotation
Disulfide bondi336 ↔ 356PROSITE-ProRule annotation
Disulfide bondi359 ↔ 368PROSITE-ProRule annotation
Disulfide bondi361 ↔ 384PROSITE-ProRule annotation
Glycosylationi376N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi387 ↔ 396PROSITE-ProRule annotation
Disulfide bondi399 ↔ 411PROSITE-ProRule annotation
Disulfide bondi414 ↔ 426PROSITE-ProRule annotation
Disulfide bondi416 ↔ 432PROSITE-ProRule annotation
Disulfide bondi434 ↔ 443PROSITE-ProRule annotation
Disulfide bondi446 ↔ 458PROSITE-ProRule annotation
Disulfide bondi461 ↔ 475PROSITE-ProRule annotation
Disulfide bondi463 ↔ 482PROSITE-ProRule annotation
Disulfide bondi484 ↔ 493PROSITE-ProRule annotation
Disulfide bondi496 ↔ 511PROSITE-ProRule annotation
Glycosylationi669N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi712 ↔ 721PROSITE-ProRule annotation
Disulfide bondi724 ↔ 741PROSITE-ProRule annotation
Disulfide bondi744 ↔ 753PROSITE-ProRule annotation
Disulfide bondi746 ↔ 760PROSITE-ProRule annotation
Disulfide bondi762 ↔ 771PROSITE-ProRule annotation
Disulfide bondi774 ↔ 790PROSITE-ProRule annotation
Disulfide bondi793 ↔ 801PROSITE-ProRule annotation
Disulfide bondi795 ↔ 811PROSITE-ProRule annotation
Disulfide bondi814 ↔ 823PROSITE-ProRule annotation
Disulfide bondi826 ↔ 844PROSITE-ProRule annotation
Disulfide bondi847 ↔ 861PROSITE-ProRule annotation
Disulfide bondi849 ↔ 868PROSITE-ProRule annotation
Glycosylationi862N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi871 ↔ 880PROSITE-ProRule annotation
Disulfide bondi883 ↔ 899PROSITE-ProRule annotation
Disulfide bondi902 ↔ 919PROSITE-ProRule annotation
Disulfide bondi904 ↔ 926PROSITE-ProRule annotation
Disulfide bondi928 ↔ 937PROSITE-ProRule annotation
Disulfide bondi940 ↔ 953PROSITE-ProRule annotation
Disulfide bondi956 ↔ 968PROSITE-ProRule annotation
Disulfide bondi958 ↔ 975PROSITE-ProRule annotation
Glycosylationi965N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi977 ↔ 986PROSITE-ProRule annotation
Disulfide bondi989 ↔ 1001PROSITE-ProRule annotation
Disulfide bondi1004 ↔ 1016PROSITE-ProRule annotation
Disulfide bondi1006 ↔ 1022PROSITE-ProRule annotation
Disulfide bondi1024 ↔ 1033PROSITE-ProRule annotation
Disulfide bondi1036 ↔ 1047PROSITE-ProRule annotation
Disulfide bondi1050InterchainCurated
Disulfide bondi1053InterchainCurated
Glycosylationi1070N-linked (GlcNAc...)Sequence analysis1
Glycosylationi1156N-linked (GlcNAc...)Sequence analysis1
Glycosylationi1394N-linked (GlcNAc...)Sequence analysis1
Glycosylationi1479N-linked (GlcNAc...)Sequence analysis1
Glycosylationi1584N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi1631InterchainCurated

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

PaxDbiP15215.
PRIDEiP15215.

Expressioni

Gene expression databases

BgeeiFBgn0002528.
ExpressionAtlasiP15215. baseline.
GenevisibleiP15215. 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

BioGridi64509. 8 interactors.
DIPiDIP-21994N.
IntActiP15215. 12 interactors.
MINTiMINT-810240.
STRINGi7227.FBpp0076111.

Structurei

3D structure databases

ProteinModelPortaliP15215.
SMRiP15215.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini63 – 298Laminin N-terminalPROSITE-ProRule annotationAdd BLAST236
Domaini299 – 358Laminin EGF-like 1PROSITE-ProRule annotationAdd BLAST60
Domaini359 – 413Laminin EGF-like 2PROSITE-ProRule annotationAdd BLAST55
Domaini414 – 460Laminin EGF-like 3PROSITE-ProRule annotationAdd BLAST47
Domaini461 – 513Laminin EGF-like 4PROSITE-ProRule annotationAdd BLAST53
Domaini514 – 523Laminin EGF-like 5; first partPROSITE-ProRule annotation10
Domaini533 – 709Laminin IV type APROSITE-ProRule annotationAdd BLAST177
Domaini710 – 743Laminin EGF-like 5; second partPROSITE-ProRule annotationAdd BLAST34
Domaini744 – 792Laminin EGF-like 6PROSITE-ProRule annotationAdd BLAST49
Domaini793 – 846Laminin EGF-like 7PROSITE-ProRule annotationAdd BLAST54
Domaini847 – 901Laminin EGF-like 8PROSITE-ProRule annotationAdd BLAST55
Domaini902 – 955Laminin EGF-like 9PROSITE-ProRule annotationAdd BLAST54
Domaini956 – 1003Laminin EGF-like 10PROSITE-ProRule annotationAdd BLAST48
Domaini1004 – 1049Laminin EGF-like 11PROSITE-ProRule annotationAdd BLAST46

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni1050 – 1609Domain II and IAdd BLAST560

Coiled coil

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Coiled coili1087 – 1109Sequence analysisAdd BLAST23
Coiled coili1144 – 1247Sequence analysisAdd BLAST104
Coiled coili1306 – 1627Sequence analysisAdd BLAST322

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 11 laminin EGF-like domains.PROSITE-ProRule annotation
Contains 1 laminin IV type A 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

eggNOGiKOG1836. Eukaryota.
ENOG410XRDC. LUCA.
HOGENOMiHOG000264193.
InParanoidiP15215.
KOiK05635.
OMAiSCDCNGN.
OrthoDBiEOG091G005L.
PhylomeDBiP15215.

Family and domain databases

Gene3Di2.60.120.260. 1 hit.
InterProiIPR000742. EGF-like_dom.
IPR008979. Galactose-bd-like.
IPR002049. Laminin_EGF.
IPR031082. Laminin_gamma.
IPR000034. Laminin_IV.
IPR008211. Laminin_N.
[Graphical view]
PANTHERiPTHR10574:SF79. PTHR10574:SF79. 2 hits.
PfamiPF00052. Laminin_B. 1 hit.
PF00053. Laminin_EGF. 11 hits.
PF00055. Laminin_N. 1 hit.
[Graphical view]
SMARTiSM00181. EGF. 6 hits.
SM00180. EGF_Lam. 11 hits.
SM00281. LamB. 1 hit.
SM00136. LamNT. 1 hit.
[Graphical view]
PROSITEiPS00022. EGF_1. 8 hits.
PS01186. EGF_2. 1 hit.
PS01248. EGF_LAM_1. 11 hits.
PS50027. EGF_LAM_2. 11 hits.
PS51115. LAMININ_IVA. 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.

P15215-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKRSRWSHSG SSTARLLLIG VLFASCSTAI LGAQRPPINS AGGHELRGTT
60 70 80 90 100
FMPALECYDP YGRPQKCLPE FINAAYQLQI ESTNTCGEQN DNHFCIQTMN
110 120 130 140 150
QNHKNCEFCK YNDHNPSFLT DLHDPQSPTW WQSETMFEGI QHPNYVNLTL
160 170 180 190 200
HLGKSYDITY VRILFRSPRP ESFTIYKRTS ESGPWIPYQF YSATCRDTYS
210 220 230 240 250
LPDSRAIRKG EGEAHALCTS EYSDISPLRD GEIAFSTLEG RPSGINFERS
260 270 280 290 300
GELQEWVTAT DIRITLDRLN TFGDELFGDS QVLKSYFYAI SDIAVGARCK
310 320 330 340 350
CNGHASKCVP STGMHGERTL VCECRHNTDG PDCDRCLPLY NDLKWKRSTS
360 370 380 390 400
TEVNECKACN CNGLADKCFF DANLFNRTGH GGHCLDCREN RDGPNCERCK
410 420 430 440 450
ENFYMRDDGY CVNCACDPVG SRSLQCNSHG KCQCKPGVTG DKCDRCDNNY
460 470 480 490 500
YQFGPHGCQQ CGCDSGGSHQ NTPACDTETG ICFCKENVEG RRCNECKPGF
510 520 530 540 550
FNLDKNNRFG CTPCFCYGHT SECMTAPGYS IVSVTSNFNK FKERWTAADL
560 570 580 590 600
NQREVDIKYN QYSRSIGTTA QGNEHVYFQA PDRFLGDQRA SYNRDLKFKL
610 620 630 640 650
QLVGQVANTG VSDVILEGAG SRISLPIFAQ GNGIPDQGVK EYTFRLHEHH
660 670 680 690 700
DYQWQPSQSA RGFLSILSNL TAIKIRATYS VQGEAILDDV ELQTAHRGAA
710 720 730 740 750
GHPATWIEQC TCPEGYLGQF CESCAPGYRH SPARGGPFMP CIPCDCHGHA
760 770 780 790 800
DICDSETGRC ICQHNTHGDN CDQCAKGFYG NALGGTPNDC KRCPCPNDGA
810 820 830 840 850
CLQINEDTVI CTECPKGYFG SRCEQCSDGF FGDPTGLLGE VQTCKSCDCN
860 870 880 890 900
GNVDPNAVGN CNRTTGECLK CIHNTAGEHC DQCLSGHFGD PLALPHGRCD
910 920 930 940 950
RCSCYEAGTE QDEQSITRCD QVTGQCQCKP NVIGRDCGEC QPGYFNIRSG
960 970 980 990 1000
NGCENCLCDP VGSYNSTCDR YSGQCHCRPG VMGQRCDQCE NYFYGFSSEG
1010 1020 1030 1040 1050
CKPCECDESG SKGFQCDQNG QCPCNDNVEG RRCDRCKENK YDRHRGCIDC
1060 1070 1080 1090 1100
PDCYNLVQDA ADLHRAKLFN LSQTLDEIAR TPVTNDDEFE AKLKAVQEKV
1110 1120 1130 1140 1150
AVLAQDARDN SGDGGQTYAE VIDDLHKHLD SVREHLVSAD KFQADANGEI
1160 1170 1180 1190 1200
DRARQNYTIL DQITENAKKE LQQALDLLND EGAQALARAK EKSVEFGQQS
1210 1220 1230 1240 1250
EQISDISREA RALADKLESE AQFDLKNAKD AKDAVEKAHQ LAKSAIDLQL
1260 1270 1280 1290 1300
KIGTELRSEV GLELSHVKQS LGTVVQTSKE ALRKANEVYD TALTLLNDVN
1310 1320 1330 1340 1350
RQTQPEIDIS QLKKDAVAAN ERADELLKQI TELSNSNGEL FADFETEQEL
1360 1370 1380 1390 1400
TEALLKRAEQ QQLEDIELLE RAKAAHDKAT KAVEQGDNTL KEANNTYEKL
1410 1420 1430 1440 1450
AGFQSDVQRS SESAEKALQT VPNIEKEIQN AESLISQAEE ALDGANKNAN
1460 1470 1480 1490 1500
EAKKNAQEAQ LKYAEQASKD AELIRRKANE TKVAARNLRE EADQLNHRVK
1510 1520 1530 1540 1550
LTEMDIFKLE ESSTKDDNLV DDAKRKVGQA KADTQEAQKQ IEKANADLTA
1560 1570 1580 1590 1600
IKDELENLKD INTGDLDRLE NRLATVEGEI NRVNLTGRIE KYREQRTIQK
1610 1620 1630
NLIDKYDAEL RELKDEVQNI GLISKALPDS CFSRNRLEP
Length:1,639
Mass (Da):182,339
Last modified:November 1, 1997 - v2
Checksum:i8F510AC6933A52BC
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti1026 – 1027DN → EY (PubMed:2912972).Curated2

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural varianti831F → Y.1
Natural varianti892L → P in strain: Oregon-R. 1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M58417 Genomic DNA. Translation: AAA28665.1.
M25063 mRNA. Translation: AAA28664.1.
AE014296 Genomic DNA. Translation: AAF50238.1.
BT021394 mRNA. Translation: AAX33542.1.
PIRiA31483. MMFFB2.
RefSeqiNP_001287009.1. NM_001300080.1.
NP_524006.1. NM_079282.2.
UniGeneiDm.2551.

Genome annotation databases

EnsemblMetazoaiFBtr0076382; FBpp0076111; FBgn0267348.
FBtr0345031; FBpp0311281; FBgn0267348.
GeneIDi39118.
KEGGidme:Dmel_CG3322.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M58417 Genomic DNA. Translation: AAA28665.1.
M25063 mRNA. Translation: AAA28664.1.
AE014296 Genomic DNA. Translation: AAF50238.1.
BT021394 mRNA. Translation: AAX33542.1.
PIRiA31483. MMFFB2.
RefSeqiNP_001287009.1. NM_001300080.1.
NP_524006.1. NM_079282.2.
UniGeneiDm.2551.

3D structure databases

ProteinModelPortaliP15215.
SMRiP15215.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi64509. 8 interactors.
DIPiDIP-21994N.
IntActiP15215. 12 interactors.
MINTiMINT-810240.
STRINGi7227.FBpp0076111.

Proteomic databases

PaxDbiP15215.
PRIDEiP15215.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaiFBtr0076382; FBpp0076111; FBgn0267348.
FBtr0345031; FBpp0311281; FBgn0267348.
GeneIDi39118.
KEGGidme:Dmel_CG3322.

Organism-specific databases

CTDi39118.
FlyBaseiFBgn0267348. LanB2.

Phylogenomic databases

eggNOGiKOG1836. Eukaryota.
ENOG410XRDC. LUCA.
HOGENOMiHOG000264193.
InParanoidiP15215.
KOiK05635.
OMAiSCDCNGN.
OrthoDBiEOG091G005L.
PhylomeDBiP15215.

Enzyme and pathway databases

ReactomeiR-DME-446107. Type I hemidesmosome assembly.

Miscellaneous databases

GenomeRNAii39118.
PROiP15215.

Gene expression databases

BgeeiFBgn0002528.
ExpressionAtlasiP15215. baseline.
GenevisibleiP15215. DM.

Family and domain databases

Gene3Di2.60.120.260. 1 hit.
InterProiIPR000742. EGF-like_dom.
IPR008979. Galactose-bd-like.
IPR002049. Laminin_EGF.
IPR031082. Laminin_gamma.
IPR000034. Laminin_IV.
IPR008211. Laminin_N.
[Graphical view]
PANTHERiPTHR10574:SF79. PTHR10574:SF79. 2 hits.
PfamiPF00052. Laminin_B. 1 hit.
PF00053. Laminin_EGF. 11 hits.
PF00055. Laminin_N. 1 hit.
[Graphical view]
SMARTiSM00181. EGF. 6 hits.
SM00180. EGF_Lam. 11 hits.
SM00281. LamB. 1 hit.
SM00136. LamNT. 1 hit.
[Graphical view]
PROSITEiPS00022. EGF_1. 8 hits.
PS01186. EGF_2. 1 hit.
PS01248. EGF_LAM_1. 11 hits.
PS50027. EGF_LAM_2. 11 hits.
PS51115. LAMININ_IVA. 1 hit.
PS51117. LAMININ_NTER. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiLAMC1_DROME
AccessioniPrimary (citable) accession number: P15215
Secondary accession number(s): Q24373, Q5BI30, Q9VT18
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1990
Last sequence update: November 1, 1997
Last modified: November 30, 2016
This is version 162 of the entry and version 2 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.