Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Laminin-like protein lam-2

Gene

lam-2

Organism
Caenorhabditis elegans
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

During the formation of neuromuscular junctions at the larval stage, negatively regulates membrane protrusion from body wall muscles, probably downstream of the integrin complex formed by pat-2 and pat-3.1 Publication

GO - Biological processi

  • basement membrane assembly Source: InterPro
  • positive regulation of locomotion Source: WormBase
  • system development Source: InterPro
Complete GO annotation...

Enzyme and pathway databases

ReactomeiR-CEL-3000157. Laminin interactions.

Names & Taxonomyi

Protein namesi
Recommended name:
Laminin-like protein lam-2
Gene namesi
Name:lam-2
ORF Names:C54D1.5
OrganismiCaenorhabditis elegans
Taxonomic identifieri6239 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaNematodaChromadoreaRhabditidaRhabditoideaRhabditidaePeloderinaeCaenorhabditis
Proteomesi
  • UP000001940 Componenti: Chromosome X

Organism-specific databases

WormBaseiC54D1.5; CE45033; WBGene00016913; lam-2.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Pathology & Biotechi

Disruption phenotypei

RNAi-mediated knockdown in L4 larval stage, causes ectopic membrane extensions from body wall muscles.1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1919Sequence analysisAdd
BLAST
Chaini20 – 16331614Laminin-like protein lam-2PRO_0000017099Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi116 – 1161N-linked (GlcNAc...)1 Publication
Glycosylationi136 – 1361N-linked (GlcNAc...)Sequence analysis
Disulfide bondi287 ↔ 296PROSITE-ProRule annotation
Disulfide bondi289 ↔ 310PROSITE-ProRule annotation
Disulfide bondi312 ↔ 321PROSITE-ProRule annotation
Disulfide bondi324 ↔ 344PROSITE-ProRule annotation
Disulfide bondi347 ↔ 356PROSITE-ProRule annotation
Glycosylationi348 – 3481N-linked (GlcNAc...)1 Publication
Disulfide bondi349 ↔ 372PROSITE-ProRule annotation
Disulfide bondi375 ↔ 384PROSITE-ProRule annotation
Disulfide bondi387 ↔ 400PROSITE-ProRule annotation
Disulfide bondi403 ↔ 415PROSITE-ProRule annotation
Disulfide bondi405 ↔ 421PROSITE-ProRule annotation
Disulfide bondi423 ↔ 432PROSITE-ProRule annotation
Disulfide bondi435 ↔ 447PROSITE-ProRule annotation
Disulfide bondi450 ↔ 464PROSITE-ProRule annotation
Disulfide bondi452 ↔ 471PROSITE-ProRule annotation
Disulfide bondi473 ↔ 482PROSITE-ProRule annotation
Disulfide bondi485 ↔ 500PROSITE-ProRule annotation
Glycosylationi522 – 5221N-linked (GlcNAc...)Sequence analysis
Glycosylationi658 – 6581N-linked (GlcNAc...)2 Publications
Disulfide bondi736 ↔ 745PROSITE-ProRule annotation
Disulfide bondi738 ↔ 752PROSITE-ProRule annotation
Glycosylationi740 – 7401N-linked (GlcNAc...)1 Publication
Disulfide bondi754 ↔ 763PROSITE-ProRule annotation
Disulfide bondi766 ↔ 782PROSITE-ProRule annotation
Disulfide bondi785 ↔ 803PROSITE-ProRule annotation
Disulfide bondi806 ↔ 815PROSITE-ProRule annotation
Disulfide bondi818 ↔ 832PROSITE-ProRule annotation
Disulfide bondi835 ↔ 849PROSITE-ProRule annotation
Disulfide bondi837 ↔ 856PROSITE-ProRule annotation
Disulfide bondi859 ↔ 868PROSITE-ProRule annotation
Disulfide bondi871 ↔ 887PROSITE-ProRule annotation
Disulfide bondi890 ↔ 909PROSITE-ProRule annotation
Disulfide bondi892 ↔ 916PROSITE-ProRule annotation
Disulfide bondi918 ↔ 927PROSITE-ProRule annotation
Disulfide bondi930 ↔ 943PROSITE-ProRule annotation
Glycosylationi936 – 9361N-linked (GlcNAc...)Sequence analysis
Disulfide bondi946 ↔ 958PROSITE-ProRule annotation
Disulfide bondi948 ↔ 965PROSITE-ProRule annotation
Disulfide bondi967 ↔ 976PROSITE-ProRule annotation
Disulfide bondi979 ↔ 991PROSITE-ProRule annotation
Disulfide bondi994 ↔ 1006PROSITE-ProRule annotation
Disulfide bondi996 ↔ 1013PROSITE-ProRule annotation
Disulfide bondi1015 ↔ 1024PROSITE-ProRule annotation
Disulfide bondi1027 ↔ 1038PROSITE-ProRule annotation
Glycosylationi1077 – 10771N-linked (GlcNAc...)2 Publications
Glycosylationi1183 – 11831N-linked (GlcNAc...)1 Publication
Glycosylationi1226 – 12261N-linked (GlcNAc...)2 Publications
Glycosylationi1259 – 12591N-linked (GlcNAc...)2 Publications
Glycosylationi1336 – 13361N-linked (GlcNAc...)Sequence analysis
Glycosylationi1452 – 14521N-linked (GlcNAc...)2 Publications
Glycosylationi1528 – 15281N-linked (GlcNAc...)Sequence analysis

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

EPDiQ18823.
PaxDbiQ18823.

Interactioni

Protein-protein interaction databases

BioGridi45905. 10 interactions.
IntActiQ18823. 1 interaction.
MINTiMINT-118164.
STRINGi6239.C54D1.5.1.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini47 – 286240Laminin N-terminalPROSITE-ProRule annotationAdd
BLAST
Domaini287 – 34660Laminin EGF-like 1PROSITE-ProRule annotationAdd
BLAST
Domaini347 – 40256Laminin EGF-like 2PROSITE-ProRule annotationAdd
BLAST
Domaini403 – 44947Laminin EGF-like 3PROSITE-ProRule annotationAdd
BLAST
Domaini450 – 50253Laminin EGF-like 4PROSITE-ProRule annotationAdd
BLAST
Domaini503 – 51210Laminin EGF-like 5; first partPROSITE-ProRule annotation
Domaini529 – 701173Laminin IV type APROSITE-ProRule annotationAdd
BLAST
Domaini702 – 74746Laminin EGF-like 5; second partPROSITE-ProRule annotationAdd
BLAST
Domaini752 – 78433Laminin EGF-like 6; truncatedPROSITE-ProRule annotationAdd
BLAST
Domaini785 – 83450Laminin EGF-like 7PROSITE-ProRule annotationAdd
BLAST
Domaini835 – 88955Laminin EGF-like 8PROSITE-ProRule annotationAdd
BLAST
Domaini890 – 94556Laminin EGF-like 9PROSITE-ProRule annotationAdd
BLAST
Domaini946 – 99348Laminin EGF-like 10PROSITE-ProRule annotationAdd
BLAST
Domaini994 – 104047Laminin EGF-like 11PROSITE-ProRule annotationAdd
BLAST

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

Laminin EGF-like domain, Repeat, Signal

Phylogenomic databases

eggNOGiKOG1836. Eukaryota.
ENOG410XRDC. LUCA.
GeneTreeiENSGT00780000121851.
HOGENOMiHOG000019301.
InParanoidiQ18823.
OMAiSCDCNGN.

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. 3 hits.
PfamiPF00052. Laminin_B. 1 hit.
PF00053. Laminin_EGF. 10 hits.
PF00055. Laminin_N. 1 hit.
[Graphical view]
SMARTiSM00181. EGF. 8 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. 10 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.

Q18823-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTSILWLFSL AVLWHMGQPQ PAELYPSVDP NHFGADGNPC YDRATRQPQR
60 70 80 90 100
CVPDFVNAAF NLEVQVTNTC GTKRPTKFCV QSGHTGQRSV CETCDDRHEG
110 120 130 140 150
FSHPAKYLTD FNVGNNETWW QSDTMQEGQQ YPTTTNLTLV LGKSFDITYV
160 170 180 190 200
RLKFISPRPE SFTIYKKTHT DSEWEPWQFY SGSCRATYGL SDRAPILPGN
210 220 230 240 250
EATAQCTKEF SDISPITGGN IAFSTLEGRP SAHAFEESEV LQKWVTASAI
260 270 280 290 300
RISLNRMNTF GDEVFKDPQV LRSYYYAISD FAVGGRCKCN GHASECVGSS
310 320 330 340 350
SVDGENRLVC RCEHNTQGAD CNECLPFYND RPWRSGTSVE ANECIACNCS
360 370 380 390 400
QLSNRCYFDQ QLFEETGHGG HCIDCQGNTQ GVHCEQCIAN HWRRPGENYC
410 420 430 440 450
VACGCNEIGS LSTQCDNEGK CQCKPGVTGR FCDQCLDGFY DFSTNGCKNC
460 470 480 490 500
GCETSGSLNN QPRCDSSSGS CSCKLNVEGR QCDKCKPGYF DLSTENQFGC
510 520 530 540 550
TPCFCFGHSS ICNTADGYFA MNVSSVFDQD KQKWAGQNRI GLQDTQWAEL
560 570 580 590 600
DKAVAVSDTD NSPVYFVAPE QFLGDQRSSY NQDLVFTLKV AKHVTNQDVK
610 620 630 640 650
DIIIVGADRQ ELSTSITAQG NPFPTTEAQT YRFRVHADPY FGWYPRINEL
660 670 680 690 700
DFIGILSNIT AIKIRGTYSY KDIGYLSNVN LGTAGVAPSA ANPKQATWIE
710 720 730 740 750
HCECLPGFVG QFCESCESGF RRETKFGGPF NHCIKCDCHN HSNSCEAESG
760 770 780 790 800
SCICEHNTAG DTCERCARGY YGDALQGTEE DCQKCPCPND GPCILHADGD
810 820 830 840 850
VICTECPNGY TGRRCDECSD GYFGNPKDGT ECVECACSGN TDPNSIGNCD
860 870 880 890 900
KITGECKKCI FNTHGFNCEN CKPGYWGDAL IEPKGNCQSC GCFAAGTRRP
910 920 930 940 950
NNDYTLLECN QQDGQCDCLP NVIGIQCDQC AHGFYNITSG LGCQECNCDP
960 970 980 990 1000
LGSEGNTCDV NTGQCQCKPG VTGQRCDRCA DYHFGFSANG CQPCDCEYIG
1010 1020 1030 1040 1050
SENQQCDVNS GQCLCKENVE GRRCDQCAEN RYGITQGCLP CDDCYTLIQS
1060 1070 1080 1090 1100
RVNVFREKVK SLDNTLQEII ENPAPVNDTK FDEKVKETSR AASEVWEAVK
1110 1120 1130 1140 1150
QKTKEGGGTI KTKSKAIKDE IVAALEKLTS IDESVAQAKV GADAAENDMK
1160 1170 1180 1190 1200
RWEIIIENAR REIENVLHYL ETEGEERAQI AYNASQKYGE QSKRMSELAS
1210 1220 1230 1240 1250
GTREEAEKHL KQASEIEQLS EQAIANATQA NKEASDAIYG GEQISKQIAE
1260 1270 1280 1290 1300
LKEKQNQLNE SIHRTLDLAE EQKKSADEAN NLAAVSLTNV EAVKIPSVDP
1310 1320 1330 1340 1350
KELRNDVAGV LEESENLVDS SVKENSANDE LFDEVNRSVA DARNELQSSQ
1360 1370 1380 1390 1400
DQQRVSDQLM LELEKSRERI VDSVSTADKT LKDAEAALQV LEEFGAKIEK
1410 1420 1430 1440 1450
SRNDAVAEFA GVEGINQRLD DIIDAQDKRR NSLPIDKQFV IDYRKSADVL
1460 1470 1480 1490 1500
LNETHALADR YKDIIHSDVD TRDSTEAVQY DIEQLMEELT DSNENLQYYK
1510 1520 1530 1540 1550
KQAEDDKQMA TEAVRKATLA KNSAIEANAT ILAEEDEIKK IINSLDTMEE
1560 1570 1580 1590 1600
VNNAELDELE EEIDRLDQLL AQAQLAKEVP TYQQYRADED VKVAQLKNDI
1610 1620 1630
SELQKEVLNL EEIRDNLPTK CFNVINLEQE GQK
Length:1,633
Mass (Da):181,213
Last modified:September 21, 2011 - v3
Checksum:i9480A825AED27255
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
FO080795 Genomic DNA. Translation: CCD66855.1.
PIRiT28811.
RefSeqiNP_509204.3. NM_076803.5.
UniGeneiCel.20145.

Genome annotation databases

EnsemblMetazoaiC54D1.5.1; C54D1.5.1; WBGene00016913.
C54D1.5.2; C54D1.5.2; WBGene00016913.
GeneIDi180980.
KEGGicel:CELE_C54D1.5.
UCSCiC54D1.5. c. elegans.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
FO080795 Genomic DNA. Translation: CCD66855.1.
PIRiT28811.
RefSeqiNP_509204.3. NM_076803.5.
UniGeneiCel.20145.

3D structure databases

ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi45905. 10 interactions.
IntActiQ18823. 1 interaction.
MINTiMINT-118164.
STRINGi6239.C54D1.5.1.

Proteomic databases

EPDiQ18823.
PaxDbiQ18823.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaiC54D1.5.1; C54D1.5.1; WBGene00016913.
C54D1.5.2; C54D1.5.2; WBGene00016913.
GeneIDi180980.
KEGGicel:CELE_C54D1.5.
UCSCiC54D1.5. c. elegans.

Organism-specific databases

CTDi180980.
WormBaseiC54D1.5; CE45033; WBGene00016913; lam-2.

Phylogenomic databases

eggNOGiKOG1836. Eukaryota.
ENOG410XRDC. LUCA.
GeneTreeiENSGT00780000121851.
HOGENOMiHOG000019301.
InParanoidiQ18823.
OMAiSCDCNGN.

Enzyme and pathway databases

ReactomeiR-CEL-3000157. Laminin interactions.

Miscellaneous databases

PROiQ18823.

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. 3 hits.
PfamiPF00052. Laminin_B. 1 hit.
PF00053. Laminin_EGF. 10 hits.
PF00055. Laminin_N. 1 hit.
[Graphical view]
SMARTiSM00181. EGF. 8 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. 10 hits.
PS51115. LAMININ_IVA. 1 hit.
PS51117. LAMININ_NTER. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Genome sequence of the nematode C. elegans: a platform for investigating biology."
    The C. elegans sequencing consortium
    Science 282:2012-2018(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Bristol N2.
  2. "Lectin affinity capture, isotope-coded tagging and mass spectrometry to identify N-linked glycoproteins."
    Kaji H., Saito H., Yamauchi Y., Shinkawa T., Taoka M., Hirabayashi J., Kasai K., Takahashi N., Isobe T.
    Nat. Biotechnol. 21:667-672(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-116, IDENTIFICATION BY MASS SPECTROMETRY.
    Strain: Bristol N2.
  3. "Identification of the hydrophobic glycoproteins of Caenorhabditis elegans."
    Fan X., She Y.-M., Bagshaw R.D., Callahan J.W., Schachter H., Mahuran D.J.
    Glycobiology 15:952-964(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-658; ASN-1077; ASN-1226; ASN-1259 AND ASN-1452, IDENTIFICATION BY MASS SPECTROMETRY.
  4. "FGF negatively regulates muscle membrane extension in Caenorhabditis elegans."
    Dixon S.J., Alexander M., Fernandes R., Ricker N., Roy P.J.
    Development 133:1263-1275(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, DISRUPTION PHENOTYPE.
  5. "Proteomics reveals N-linked glycoprotein diversity in Caenorhabditis elegans and suggests an atypical translocation mechanism for integral membrane proteins."
    Kaji H., Kamiie J., Kawakami H., Kido K., Yamauchi Y., Shinkawa T., Taoka M., Takahashi N., Isobe T.
    Mol. Cell. Proteomics 6:2100-2109(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-348; ASN-658; ASN-740; ASN-1077; ASN-1183; ASN-1226; ASN-1259 AND ASN-1452, IDENTIFICATION BY MASS SPECTROMETRY.
    Strain: Bristol N2.

Entry informationi

Entry nameiLAM2_CAEEL
AccessioniPrimary (citable) accession number: Q18823
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: September 21, 2011
Last modified: June 8, 2016
This is version 131 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programCaenorhabditis annotation project

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Caenorhabditis elegans
    Caenorhabditis elegans: entries, gene names and cross-references to WormBase
  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.