LEV9_CAEEL
ID LEV9_CAEEL Reviewed; 622 AA.
AC Q22328; C7C692;
DT 01-OCT-2014, integrated into UniProtKB/Swiss-Prot.
DT 06-FEB-2013, sequence version 3.
DT 03-AUG-2022, entry version 132.
DE RecName: Full=Protein lev-9;
DE Flags: Precursor;
GN Name=lev-9; ORFNames=T07H6.5;
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 [MRNA], FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=19794415; DOI=10.1038/nature08430;
RA Gendrel M., Rapti G., Richmond J.E., Bessereau J.L.;
RT "A secreted complement control-related protein ensures acetylcholine
RT receptor clustering.";
RL Nature 461:992-996(2009).
RN [2]
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 [3]
RP FUNCTION, AND PROTEOLYTIC PROCESSING.
RX PubMed=24619422; DOI=10.1074/jbc.c113.534677;
RA Briseno-Roa L., Bessereau J.L.;
RT "Proteolytic processing of the extracellular scaffolding protein LEV-9 is
RT required for clustering acetylcholine receptors.";
RL J. Biol. Chem. 289:10967-10974(2014).
CC -!- FUNCTION: Scaffolding protein that is necessary to cluster
CC acetylcholine receptors at neuromuscular junctions.
CC {ECO:0000269|PubMed:19794415, ECO:0000269|PubMed:24619422}.
CC -!- SUBCELLULAR LOCATION: Synapse {ECO:0000269|PubMed:19794415}. Secreted
CC {ECO:0000269|PubMed:19794415}. Note=Secreted by muscle cells and
CC localizes at cholinergic neuromuscular junctions.
CC -!- PTM: Proteolytic processing of the C-terminus is required for
CC clustering activity but not for secretion nor traffic.
CC {ECO:0000269|PubMed:24619422}.
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DR EMBL; FN433774; CBA12962.1; -; mRNA.
DR EMBL; FO081717; CCD74396.2; -; Genomic_DNA.
DR PIR; T16833; T16833.
DR RefSeq; NP_509053.3; NM_076652.6.
DR AlphaFoldDB; Q22328; -.
DR SMR; Q22328; -.
DR BioGRID; 45833; 1.
DR STRING; 6239.T07H6.5; -.
DR PaxDb; Q22328; -.
DR EnsemblMetazoa; T07H6.5a.1; T07H6.5a.1; WBGene00002976.
DR GeneID; 188252; -.
DR UCSC; T07H6.5; c. elegans.
DR CTD; 188252; -.
DR WormBase; T07H6.5a; CE47917; WBGene00002976; lev-9.
DR eggNOG; KOG4297; Eukaryota.
DR GeneTree; ENSGT00940000163310; -.
DR HOGENOM; CLU_502134_0_0_1; -.
DR InParanoid; Q22328; -.
DR OMA; HCTVDEN; -.
DR OrthoDB; 46968at2759; -.
DR Reactome; R-CEL-373080; Class B/2 (Secretin family receptors).
DR Reactome; R-CEL-6798695; Neutrophil degranulation.
DR Reactome; R-CEL-6807878; COPI-mediated anterograde transport.
DR Reactome; R-CEL-977606; Regulation of Complement cascade.
DR PRO; PR:Q22328; -.
DR Proteomes; UP000001940; Chromosome X.
DR Bgee; WBGene00002976; Expressed in larva and 2 other tissues.
DR ExpressionAtlas; Q22328; baseline and differential.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0005615; C:extracellular space; IDA:WormBase.
DR GO; GO:0045202; C:synapse; IEA:UniProtKB-SubCell.
DR GO; GO:0030414; F:peptidase inhibitor activity; IEA:InterPro.
DR CDD; cd00033; CCP; 6.
DR Gene3D; 4.10.75.10; -; 1.
DR InterPro; IPR036645; Elafin-like_sf.
DR InterPro; IPR035976; Sushi/SCR/CCP_sf.
DR InterPro; IPR000436; Sushi_SCR_CCP_dom.
DR InterPro; IPR008197; WAP_dom.
DR Pfam; PF00084; Sushi; 6.
DR Pfam; PF00095; WAP; 1.
DR SMART; SM00032; CCP; 8.
DR SMART; SM00217; WAP; 1.
DR SUPFAM; SSF57256; SSF57256; 1.
DR SUPFAM; SSF57535; SSF57535; 8.
DR PROSITE; PS50923; SUSHI; 8.
DR PROSITE; PS51390; WAP; 1.
PE 1: Evidence at protein level;
KW Disulfide bond; Glycoprotein; Reference proteome; Repeat; Secreted; Signal;
KW Sushi; Synapse.
FT SIGNAL 1..16
FT /evidence="ECO:0000255"
FT CHAIN 17..575
FT /note="Protein lev-9"
FT /id="PRO_0000430313"
FT PROPEP 576..622
FT /id="PRO_0000430314"
FT DOMAIN 17..61
FT /note="WAP; atypical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00722"
FT DOMAIN 62..120
FT /note="Sushi 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DOMAIN 122..190
FT /note="Sushi 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DOMAIN 191..248
FT /note="Sushi 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DOMAIN 249..306
FT /note="Sushi 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DOMAIN 307..364
FT /note="Sushi 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DOMAIN 365..422
FT /note="Sushi 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DOMAIN 423..483
FT /note="Sushi 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DOMAIN 484..558
FT /note="Sushi 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT SITE 575..576
FT /note="Cleavage"
FT CARBOHYD 411
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 19..49
FT /evidence="ECO:0000250"
FT DISULFID 35..47
FT /evidence="ECO:0000250"
FT DISULFID 41..57
FT /evidence="ECO:0000250"
FT DISULFID 64..105
FT /evidence="ECO:0000250"
FT DISULFID 91..118
FT /evidence="ECO:0000250"
FT DISULFID 124..171
FT /evidence="ECO:0000250"
FT DISULFID 154..188
FT /evidence="ECO:0000250"
FT DISULFID 193..233
FT /evidence="ECO:0000250"
FT DISULFID 219..246
FT /evidence="ECO:0000250"
FT DISULFID 251..291
FT /evidence="ECO:0000250"
FT DISULFID 277..304
FT /evidence="ECO:0000250"
FT DISULFID 309..349
FT /evidence="ECO:0000250"
FT DISULFID 335..362
FT /evidence="ECO:0000250"
FT DISULFID 366..409
FT /evidence="ECO:0000250"
FT DISULFID 395..420
FT /evidence="ECO:0000250"
FT DISULFID 425..467
FT /evidence="ECO:0000250"
FT DISULFID 452..481
FT /evidence="ECO:0000250"
FT DISULFID 486..543
FT /evidence="ECO:0000250"
FT DISULFID 529..556
FT /evidence="ECO:0000250"
SQ SEQUENCE 622 AA; 68692 MW; 60965F9799A0D5DC CRC64;
MRFLLLLAIS ITYASALSCP EVTLSQRPKH CKKECIADED CKRNKRCMCD GECGLSCVNP
IAMCHPLPNI ENGFIRTAGD LRFGSNAEYG CNKGYILVGA SQRRCQANKE WSSSQPVCRL
QLKCGPPPEI PFAVHDGSSF SGEYDLDAEV AYNCIPGYHK FNAKGLSISK CLLNRKNVAQ
WFGPDLRCKA RACPDPGDIE NGLREGDTFE YPHHVKYSCN PGFLLVGSTS RQCSSNGEWT
NEPANCKATE CSRPSSPLHG KVVGSSLTYQ SVVTYSCDHG YRLVGQVQRI CLAEGIWGGN
EPRCEEIRCS VLPTLPNGYI EGSETSFGAV AVFRCLETMT HEGASKAKCM EDGQWSAPIP
RCLASCRVPH IQNGKIRDKS EGQLIASGSK VIVECNKQHE ANIDERLICS NSTWSHVPVC
SPLSCHNWPP RVPHARILFS KSSHGSIAKY ECNNGYHPNR NNQIIKCLYG EWTKDGPPMK
CLPSWCEHPS KTYGTLPGGQ ILLEGILGAY EFQSYIQKVE EGRAISFQCG KGNYLIGPPK
ATCVNGEWMP KVSPKCVSQT HPMIEGKILW DRKKRSLPGR AVREYVDDEL STHRQHSGKC
GIVSGKLERM IMQHSDNGVS VC
