LAP1_CAEEL
ID LAP1_CAEEL Reviewed; 699 AA.
AC O61967; Q6A580; Q9NFN7;
DT 16-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT 27-SEP-2005, sequence version 3.
DT 03-AUG-2022, entry version 170.
DE RecName: Full=Protein lap1;
DE AltName: Full=Lethal protein 413;
GN Name=let-413 {ECO:0000312|WormBase:F26D11.11b};
GN ORFNames=F26D11.11 {ECO:0000312|WormBase:F26D11.11b};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A), FUNCTION, SUBCELLULAR LOCATION,
RP DEVELOPMENTAL STAGE, MUTAGENESIS OF PRO-305, AND DISRUPTION PHENOTYPE.
RC STRAIN=Bristol N2 {ECO:0000269|PubMed:10878806};
RX PubMed=10878806; DOI=10.1038/35017046;
RA Legouis R., Gansmuller A., Sookhareea S., Bosher J.M., Baillie D.L.,
RA Labouesse M.;
RT "LET-413 is a basolateral protein required for the assembly of adherens
RT junctions in Caenorhabditis elegans.";
RL Nat. Cell Biol. 2:415-422(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND ALTERNATIVE SPLICING.
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 [3] {ECO:0000305, ECO:0000312|EMBL:CAB91651.1}
RP SUBCELLULAR LOCATION, AND MUTAGENESIS OF PRO-305.
RX PubMed=14578922; DOI=10.1038/sj.embor.embor7400006;
RA Legouis R., Jaulin-Bastard F., Schott S., Navarro C., Borg J.-P.,
RA Labouesse M.;
RT "Basolateral targeting by leucine-rich repeat domains in epithelial
RT cells.";
RL EMBO Rep. 4:1096-1102(2003).
RN [4]
RP FUNCTION.
RX PubMed=11715019; DOI=10.1038/ncb1101-983;
RA Koeppen M., Simske J.S., Sims P.A., Firestein B.L., Hall D.H., Radice A.D.,
RA Rongo C., Hardin J.D.;
RT "Cooperative regulation of AJM-1 controls junctional integrity in
RT Caenorhabditis elegans epithelia.";
RL Nat. Cell Biol. 3:983-991(2001).
RN [5] {ECO:0000305}
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=15063180; DOI=10.1016/j.ydbio.2004.01.003;
RA Bossinger O., Fukushige T., Claeys M., Borgonie G., McGhee J.D.;
RT "The apical disposition of the Caenorhabditis elegans intestinal terminal
RT web is maintained by LET-413.";
RL Dev. Biol. 268:448-456(2004).
RN [6]
RP FUNCTION.
RX PubMed=18411252; DOI=10.1242/jcs.017137;
RA Lockwood C.A., Lynch A.M., Hardin J.;
RT "Dynamic analysis identifies novel roles for DLG-1 subdomains in AJM-1
RT recruitment and LET-413-dependent apical focusing.";
RL J. Cell Sci. 121:1477-1487(2008).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY, SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RX PubMed=27506200; DOI=10.1186/s12915-016-0286-x;
RA Waaijers S., Munoz J., Berends C., Ramalho J.J., Goerdayal S.S., Low T.Y.,
RA Zoumaro-Djayoon A.D., Hoffmann M., Koorman T., Tas R.P., Harterink M.,
RA Seelk S., Kerver J., Hoogenraad C.C., Bossinger O., Tursun B.,
RA van den Heuvel S., Heck A.J., Boxem M.;
RT "A tissue-specific protein purification approach in Caenorhabditis elegans
RT identifies novel interaction partners of DLG-1/Discs large.";
RL BMC Biol. 14:66-66(2016).
CC -!- FUNCTION: Critical role in assembling adherens junctions; adapter
CC protein involved in polarizing protein trafficking in epithelial cells.
CC Necessary to maintain, not establish, the entire terminal web
CC (organelle-depleted, intermediate filament-rich layer of cytoplasm that
CC underlies the apical microvilli of polarized epithelial cells) or brush
CC border assembly at the apical surface gut cells. Required for correct
CC localization of ifb-2 intermediate filaments in the terminal web.
CC Required for dlg-1 lateral localization (PubMed:18411252). With dlg-1,
CC cooperatively regulates ajm-1 localization to apical junctions
CC (PubMed:11715019). {ECO:0000269|PubMed:10878806,
CC ECO:0000269|PubMed:11715019, ECO:0000269|PubMed:15063180,
CC ECO:0000269|PubMed:18411252}.
CC -!- SUBCELLULAR LOCATION: Basolateral cell membrane
CC {ECO:0000269|PubMed:10878806, ECO:0000269|PubMed:14578922,
CC ECO:0000269|PubMed:27506200}; Peripheral membrane protein
CC {ECO:0000269|PubMed:10878806, ECO:0000269|PubMed:14578922}.
CC Note=Basolateral membrane of epithelial cells.
CC {ECO:0000269|PubMed:10878806, ECO:0000269|PubMed:14578922}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=b;
CC IsoId=O61967-1; Sequence=Displayed;
CC Name=a;
CC IsoId=O61967-2; Sequence=VSP_015673, VSP_015674;
CC -!- TISSUE SPECIFICITY: Expressed in the terminal web of the intestine
CC (PubMed:15063180, PubMed:27506200). Expressed in seam cells
CC (PubMed:27506200). {ECO:0000269|PubMed:15063180,
CC ECO:0000269|PubMed:27506200}.
CC -!- DEVELOPMENTAL STAGE: Expressed in all embryonic epithelial cells.
CC {ECO:0000269|PubMed:10878806}.
CC -!- DISRUPTION PHENOTYPE: Worms display a severely affected epithelial
CC integrity, leading to abnormal morphogenesis of the pharynx, intestine
CC and embryo. {ECO:0000269|PubMed:10878806}.
CC -!- SIMILARITY: Belongs to the LAP (LRR and PDZ) protein family.
CC {ECO:0000305}.
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DR EMBL; AJ276590; CAB91651.1; -; mRNA.
DR EMBL; FO081227; CCD70053.1; -; Genomic_DNA.
DR EMBL; FO081227; CCD70054.1; -; Genomic_DNA.
DR PIR; T33295; T33295.
DR RefSeq; NP_001023850.1; NM_001028679.3.
DR RefSeq; NP_001023851.1; NM_001028680.3. [O61967-1]
DR AlphaFoldDB; O61967; -.
DR SMR; O61967; -.
DR BioGRID; 44213; 20.
DR DIP; DIP-25349N; -.
DR IntAct; O61967; 7.
DR STRING; 6239.F26D11.11b; -.
DR iPTMnet; O61967; -.
DR EPD; O61967; -.
DR PaxDb; O61967; -.
DR PeptideAtlas; O61967; -.
DR EnsemblMetazoa; F26D11.11a.1; F26D11.11a.1; WBGene00002632.
DR EnsemblMetazoa; F26D11.11b.1; F26D11.11b.1; WBGene00002632. [O61967-1]
DR GeneID; 179171; -.
DR UCSC; F26D11.11a; c. elegans. [O61967-1]
DR CTD; 179171; -.
DR WormBase; F26D11.11a; CE29778; WBGene00002632; let-413. [O61967-2]
DR WormBase; F26D11.11b; CE37008; WBGene00002632; let-413. [O61967-1]
DR eggNOG; KOG0619; Eukaryota.
DR eggNOG; KOG3528; Eukaryota.
DR GeneTree; ENSGT00940000164066; -.
DR HOGENOM; CLU_000288_18_23_1; -.
DR InParanoid; O61967; -.
DR OMA; DIFRFRK; -.
DR OrthoDB; 442171at2759; -.
DR PhylomeDB; O61967; -.
DR PRO; PR:O61967; -.
DR Proteomes; UP000001940; Chromosome V.
DR Bgee; WBGene00002632; Expressed in pharyngeal muscle cell (C elegans) and 4 other tissues.
DR ExpressionAtlas; O61967; baseline and differential.
DR GO; GO:0005912; C:adherens junction; IBA:GO_Central.
DR GO; GO:0016323; C:basolateral plasma membrane; IDA:WormBase.
DR GO; GO:0030054; C:cell junction; IBA:GO_Central.
DR GO; GO:0014069; C:postsynaptic density; IBA:GO_Central.
DR GO; GO:0030029; P:actin filament-based process; IMP:WormBase.
DR GO; GO:0034333; P:adherens junction assembly; IDA:ARUK-UCL.
DR GO; GO:0098609; P:cell-cell adhesion; IBA:GO_Central.
DR GO; GO:0007043; P:cell-cell junction assembly; IMP:WormBase.
DR GO; GO:0009792; P:embryo development ending in birth or egg hatching; IMP:WormBase.
DR GO; GO:0048557; P:embryonic digestive tract morphogenesis; IMP:WormBase.
DR GO; GO:0007163; P:establishment or maintenance of cell polarity; IEP:UniProtKB.
DR GO; GO:0045197; P:establishment or maintenance of epithelial cell apical/basal polarity; IBA:GO_Central.
DR GO; GO:0045199; P:maintenance of epithelial cell apical/basal polarity; IMP:WormBase.
DR GO; GO:0098968; P:neurotransmitter receptor transport postsynaptic membrane to endosome; IBA:GO_Central.
DR GO; GO:0098887; P:neurotransmitter receptor transport, endosome to postsynaptic membrane; IBA:GO_Central.
DR GO; GO:0015031; P:protein transport; IEP:UniProtKB.
DR GO; GO:0043113; P:receptor clustering; IBA:GO_Central.
DR GO; GO:0097120; P:receptor localization to synapse; IBA:GO_Central.
DR GO; GO:0045108; P:regulation of intermediate filament polymerization or depolymerization; IMP:UniProtKB.
DR Gene3D; 2.30.42.10; -; 1.
DR Gene3D; 3.80.10.10; -; 2.
DR InterPro; IPR001611; Leu-rich_rpt.
DR InterPro; IPR003591; Leu-rich_rpt_typical-subtyp.
DR InterPro; IPR032675; LRR_dom_sf.
DR InterPro; IPR001478; PDZ.
DR InterPro; IPR036034; PDZ_sf.
DR Pfam; PF13855; LRR_8; 3.
DR Pfam; PF00595; PDZ; 1.
DR SMART; SM00369; LRR_TYP; 12.
DR SMART; SM00228; PDZ; 1.
DR SUPFAM; SSF50156; SSF50156; 1.
DR PROSITE; PS51450; LRR; 14.
DR PROSITE; PS50106; PDZ; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell adhesion; Cell membrane; Leucine-rich repeat;
KW Membrane; Reference proteome; Repeat.
FT CHAIN 1..699
FT /note="Protein lap1"
FT /id="PRO_0000188305"
FT REPEAT 37..59
FT /note="LRR 1"
FT REPEAT 60..81
FT /note="LRR 2"
FT REPEAT 83..104
FT /note="LRR 3"
FT REPEAT 106..127
FT /note="LRR 4"
FT REPEAT 129..150
FT /note="LRR 5"
FT REPEAT 152..174
FT /note="LRR 6"
FT REPEAT 175..196
FT /note="LRR 7"
FT REPEAT 198..219
FT /note="LRR 8"
FT REPEAT 221..242
FT /note="LRR 9"
FT REPEAT 244..265
FT /note="LRR 10"
FT REPEAT 267..288
FT /note="LRR 11"
FT REPEAT 290..311
FT /note="LRR 12"
FT REPEAT 313..334
FT /note="LRR 13"
FT REPEAT 336..357
FT /note="LRR 14"
FT REPEAT 359..380
FT /note="LRR 15"
FT REPEAT 382..403
FT /note="LRR 16"
FT DOMAIN 584..665
FT /note="PDZ"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT REGION 656..699
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 658..699
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 531
FT /note="R -> RFIDAPAS (in isoform a)"
FT /evidence="ECO:0000303|PubMed:10878806"
FT /id="VSP_015673"
FT VAR_SEQ 666..699
FT /note="EPSLNGSSHQLNHFDAGSPDSTMFVTSSTPVYAS -> VSRPCEY (in
FT isoform a)"
FT /evidence="ECO:0000303|PubMed:10878806"
FT /id="VSP_015674"
FT MUTAGEN 305
FT /note="P->L: Abolishes membrane localization."
FT /evidence="ECO:0000269|PubMed:10878806,
FT ECO:0000269|PubMed:14578922"
SQ SEQUENCE 699 AA; 77350 MW; 2CE6478B5039F2DE CRC64;
MPAFFCLPMA CQRQVDSIDR SQSNLQAIPS DIFRFRKLED LNLTMNNIKE LDHRLFSLRH
LRILDVSDNE LAVLPAEIGN LTQLIELNLN RNSIAKLPDT MQNCKLLTTL NLSSNPFTRL
PETICECSSI TILSLNETSL TLLPSNIGSL TNLRVLEARD NLLRTIPLSI VELRKLEELD
LGQNELEALP AEIGKLTSLR EFYVDINSLT SLPDSISGCR MLDQLDVSEN QIIRLPENLG
RMPNLTDLNI SINEIIELPS SFGELKRLQM LKADRNSLHN LTSEIGKCQS LTELYLGQNF
LTDLPDTIGD LRQLTTLNVD CNNLSDIPDT IGNCKSLTVL SLRQNILTEL PMTIGKCENL
TVLDVASNKL PHLPFTVKVL YKLQALWLSE NQTQSILKLS ETRDDRKGIK VVTCYLLPQV
DAIDGEGRSG SAQHNTDRGA FLGGPKVHFH DQADTTFEEN KEAEIHLGNF ERHNTPHPKT
PKHKKGSIDG HMLPHEIDQP RQLSLVSNHR TSTSSFGESS NSINRDLADI RAQNGVREAT
LSPEREERMA TSLSSLSNLA AGTQNMHTIR IQKDDTGKLG LSFAGGTSND PAPNSNGDSG
LFVTKVTPGS AAYRCGLREG DKLIRANDVN MINASQDNAM EAIKKRETVE LVVLRRSPSP
VSRTSEPSLN GSSHQLNHFD AGSPDSTMFV TSSTPVYAS
