LAM2_CAEEL
ID LAM2_CAEEL Reviewed; 1633 AA.
AC Q18823;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 21-SEP-2011, sequence version 3.
DT 03-AUG-2022, entry version 165.
DE RecName: Full=Laminin-like protein lam-2;
DE Flags: Precursor;
GN Name=lam-2; ORFNames=C54D1.5;
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [2]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-116, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC STRAIN=Bristol N2;
RX PubMed=12754521; DOI=10.1038/nbt829;
RA Kaji H., Saito H., Yamauchi Y., Shinkawa T., Taoka M., Hirabayashi J.,
RA Kasai K., Takahashi N., Isobe T.;
RT "Lectin affinity capture, isotope-coded tagging and mass spectrometry to
RT identify N-linked glycoproteins.";
RL Nat. Biotechnol. 21:667-672(2003).
RN [3]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-658; ASN-1077; ASN-1226;
RP ASN-1259 AND ASN-1452, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=15888633; DOI=10.1093/glycob/cwi075;
RA Fan X., She Y.-M., Bagshaw R.D., Callahan J.W., Schachter H., Mahuran D.J.;
RT "Identification of the hydrophobic glycoproteins of Caenorhabditis
RT elegans.";
RL Glycobiology 15:952-964(2005).
RN [4]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=16495308; DOI=10.1242/dev.02300;
RA Dixon S.J., Alexander M., Fernandes R., Ricker N., Roy P.J.;
RT "FGF negatively regulates muscle membrane extension in Caenorhabditis
RT elegans.";
RL Development 133:1263-1275(2006).
RN [5]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-348; ASN-658; ASN-740;
RP ASN-1077; ASN-1183; ASN-1226; ASN-1259 AND ASN-1452, AND IDENTIFICATION BY
RP MASS SPECTROMETRY.
RC STRAIN=Bristol N2;
RX PubMed=17761667; DOI=10.1074/mcp.m600392-mcp200;
RA Kaji H., Kamiie J., Kawakami H., Kido K., Yamauchi Y., Shinkawa T.,
RA Taoka M., Takahashi N., Isobe T.;
RT "Proteomics reveals N-linked glycoprotein diversity in Caenorhabditis
RT elegans and suggests an atypical translocation mechanism for integral
RT membrane proteins.";
RL Mol. Cell. Proteomics 6:2100-2109(2007).
CC -!- FUNCTION: During the formation of neuromuscular junctions at the larval
CC stage, negatively regulates membrane protrusion from body wall muscles,
CC probably downstream of the integrin complex formed by pat-2 and pat-3.
CC {ECO:0000269|PubMed:16495308}.
CC -!- DISRUPTION PHENOTYPE: RNAi-mediated knockdown in L4 larval stage,
CC causes ectopic membrane extensions from body wall muscles.
CC {ECO:0000269|PubMed:16495308}.
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DR EMBL; FO080795; CCD66855.1; -; Genomic_DNA.
DR PIR; T28811; T28811.
DR RefSeq; NP_509204.3; NM_076803.5.
DR AlphaFoldDB; Q18823; -.
DR SMR; Q18823; -.
DR BioGRID; 45905; 13.
DR IntAct; Q18823; 1.
DR MINT; Q18823; -.
DR STRING; 6239.C54D1.5.1; -.
DR iPTMnet; Q18823; -.
DR EPD; Q18823; -.
DR PaxDb; Q18823; -.
DR PeptideAtlas; Q18823; -.
DR EnsemblMetazoa; C54D1.5.1; C54D1.5.1; WBGene00016913.
DR GeneID; 180980; -.
DR KEGG; cel:CELE_C54D1.5; -.
DR UCSC; C54D1.5; c. elegans.
DR CTD; 180980; -.
DR WormBase; C54D1.5; CE45033; WBGene00016913; lam-2.
DR eggNOG; KOG1836; Eukaryota.
DR GeneTree; ENSGT00940000169261; -.
DR HOGENOM; CLU_002471_1_0_1; -.
DR InParanoid; Q18823; -.
DR OMA; TCVQLAD; -.
DR OrthoDB; 156553at2759; -.
DR PhylomeDB; Q18823; -.
DR Reactome; R-CEL-1474228; Degradation of the extracellular matrix.
DR Reactome; R-CEL-3000157; Laminin interactions.
DR Reactome; R-CEL-381426; Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs).
DR Reactome; R-CEL-446107; Type I hemidesmosome assembly.
DR Reactome; R-CEL-8957275; Post-translational protein phosphorylation.
DR PRO; PR:Q18823; -.
DR Proteomes; UP000001940; Chromosome X.
DR Bgee; WBGene00016913; Expressed in pharyngeal muscle cell (C elegans) and 3 other tissues.
DR GO; GO:0005604; C:basement membrane; IBA:GO_Central.
DR GO; GO:0009887; P:animal organ morphogenesis; IBA:GO_Central.
DR GO; GO:0016477; P:cell migration; IBA:GO_Central.
DR GO; GO:0040017; P:positive regulation of locomotion; IMP:WormBase.
DR GO; GO:0034446; P:substrate adhesion-dependent cell spreading; IBA:GO_Central.
DR GO; GO:0009888; P:tissue development; IBA:GO_Central.
DR CDD; cd00055; EGF_Lam; 9.
DR InterPro; IPR000742; EGF-like_dom.
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; 11.
DR Pfam; PF00055; Laminin_N; 1.
DR SMART; SM00181; EGF; 8.
DR SMART; SM00180; EGF_Lam; 11.
DR SMART; SM00281; LamB; 1.
DR SMART; SM00136; LamNT; 1.
DR PROSITE; PS00022; EGF_1; 8.
DR PROSITE; PS01186; EGF_2; 1.
DR PROSITE; PS01248; EGF_LAM_1; 11.
DR PROSITE; PS50027; EGF_LAM_2; 10.
DR PROSITE; PS51115; LAMININ_IVA; 1.
DR PROSITE; PS51117; LAMININ_NTER; 1.
PE 1: Evidence at protein level;
KW Disulfide bond; Glycoprotein; Laminin EGF-like domain; Reference proteome;
KW Repeat; Signal.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT CHAIN 20..1633
FT /note="Laminin-like protein lam-2"
FT /id="PRO_0000017099"
FT DOMAIN 47..286
FT /note="Laminin N-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00466"
FT DOMAIN 287..346
FT /note="Laminin EGF-like 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DOMAIN 347..402
FT /note="Laminin EGF-like 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DOMAIN 403..449
FT /note="Laminin EGF-like 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DOMAIN 450..502
FT /note="Laminin EGF-like 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DOMAIN 503..512
FT /note="Laminin EGF-like 5; first part"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DOMAIN 529..701
FT /note="Laminin IV type A"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00458"
FT DOMAIN 702..747
FT /note="Laminin EGF-like 5; second part"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DOMAIN 752..784
FT /note="Laminin EGF-like 6; truncated"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DOMAIN 785..834
FT /note="Laminin EGF-like 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DOMAIN 835..889
FT /note="Laminin EGF-like 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DOMAIN 890..945
FT /note="Laminin EGF-like 9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DOMAIN 946..993
FT /note="Laminin EGF-like 10"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DOMAIN 994..1040
FT /note="Laminin EGF-like 11"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT CARBOHYD 116
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:12754521"
FT CARBOHYD 136
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 348
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:17761667"
FT CARBOHYD 522
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 658
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:15888633,
FT ECO:0000269|PubMed:17761667"
FT CARBOHYD 740
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:17761667"
FT CARBOHYD 936
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1077
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:15888633,
FT ECO:0000269|PubMed:17761667"
FT CARBOHYD 1183
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:17761667"
FT CARBOHYD 1226
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:15888633,
FT ECO:0000269|PubMed:17761667"
FT CARBOHYD 1259
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:15888633,
FT ECO:0000269|PubMed:17761667"
FT CARBOHYD 1336
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1452
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:15888633,
FT ECO:0000269|PubMed:17761667"
FT CARBOHYD 1528
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 287..296
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 289..310
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 312..321
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 324..344
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 347..356
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 349..372
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 375..384
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 387..400
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 403..415
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 405..421
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 423..432
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 435..447
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 450..464
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 452..471
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 473..482
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 485..500
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 736..745
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 738..752
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 754..763
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 766..782
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 785..803
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 806..815
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 818..832
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 835..849
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 837..856
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 859..868
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 871..887
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 890..909
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 892..916
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 918..927
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 930..943
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 946..958
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 948..965
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 967..976
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 979..991
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 994..1006
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 996..1013
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 1015..1024
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 1027..1038
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
SQ SEQUENCE 1633 AA; 181213 MW; 9480A825AED27255 CRC64;
MTSILWLFSL AVLWHMGQPQ PAELYPSVDP NHFGADGNPC YDRATRQPQR CVPDFVNAAF
NLEVQVTNTC GTKRPTKFCV QSGHTGQRSV CETCDDRHEG FSHPAKYLTD FNVGNNETWW
QSDTMQEGQQ YPTTTNLTLV LGKSFDITYV RLKFISPRPE SFTIYKKTHT DSEWEPWQFY
SGSCRATYGL SDRAPILPGN EATAQCTKEF SDISPITGGN IAFSTLEGRP SAHAFEESEV
LQKWVTASAI RISLNRMNTF GDEVFKDPQV LRSYYYAISD FAVGGRCKCN GHASECVGSS
SVDGENRLVC RCEHNTQGAD CNECLPFYND RPWRSGTSVE ANECIACNCS QLSNRCYFDQ
QLFEETGHGG HCIDCQGNTQ GVHCEQCIAN HWRRPGENYC VACGCNEIGS LSTQCDNEGK
CQCKPGVTGR FCDQCLDGFY DFSTNGCKNC GCETSGSLNN QPRCDSSSGS CSCKLNVEGR
QCDKCKPGYF DLSTENQFGC TPCFCFGHSS ICNTADGYFA MNVSSVFDQD KQKWAGQNRI
GLQDTQWAEL DKAVAVSDTD NSPVYFVAPE QFLGDQRSSY NQDLVFTLKV AKHVTNQDVK
DIIIVGADRQ ELSTSITAQG NPFPTTEAQT YRFRVHADPY FGWYPRINEL DFIGILSNIT
AIKIRGTYSY KDIGYLSNVN LGTAGVAPSA ANPKQATWIE HCECLPGFVG QFCESCESGF
RRETKFGGPF NHCIKCDCHN HSNSCEAESG SCICEHNTAG DTCERCARGY YGDALQGTEE
DCQKCPCPND GPCILHADGD VICTECPNGY TGRRCDECSD GYFGNPKDGT ECVECACSGN
TDPNSIGNCD KITGECKKCI FNTHGFNCEN CKPGYWGDAL IEPKGNCQSC GCFAAGTRRP
NNDYTLLECN QQDGQCDCLP NVIGIQCDQC AHGFYNITSG LGCQECNCDP LGSEGNTCDV
NTGQCQCKPG VTGQRCDRCA DYHFGFSANG CQPCDCEYIG SENQQCDVNS GQCLCKENVE
GRRCDQCAEN RYGITQGCLP CDDCYTLIQS RVNVFREKVK SLDNTLQEII ENPAPVNDTK
FDEKVKETSR AASEVWEAVK QKTKEGGGTI KTKSKAIKDE IVAALEKLTS IDESVAQAKV
GADAAENDMK RWEIIIENAR REIENVLHYL ETEGEERAQI AYNASQKYGE QSKRMSELAS
GTREEAEKHL KQASEIEQLS EQAIANATQA NKEASDAIYG GEQISKQIAE LKEKQNQLNE
SIHRTLDLAE EQKKSADEAN NLAAVSLTNV EAVKIPSVDP KELRNDVAGV LEESENLVDS
SVKENSANDE LFDEVNRSVA DARNELQSSQ DQQRVSDQLM LELEKSRERI VDSVSTADKT
LKDAEAALQV LEEFGAKIEK SRNDAVAEFA GVEGINQRLD DIIDAQDKRR NSLPIDKQFV
IDYRKSADVL LNETHALADR YKDIIHSDVD TRDSTEAVQY DIEQLMEELT DSNENLQYYK
KQAEDDKQMA TEAVRKATLA KNSAIEANAT ILAEEDEIKK IINSLDTMEE VNNAELDELE
EEIDRLDQLL AQAQLAKEVP TYQQYRADED VKVAQLKNDI SELQKEVLNL EEIRDNLPTK
CFNVINLEQE GQK
