JIP_CAEEL
ID JIP_CAEEL Reviewed; 1190 AA.
AC P34609; A7LPE3; A7LPE4; C0P271; C7FZT6; Q95V72; S6EZN6; S6EZP3; S6F548;
AC S6F556; S6FD02; S6FN04; S6FN08; S6FWP4; S6FWP6; U4MKU8;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 13-NOV-2019, sequence version 4.
DT 03-AUG-2022, entry version 158.
DE RecName: Full=JNK-interacting protein;
DE Short=JIP;
DE AltName: Full=JNK MAP kinase scaffold protein;
DE AltName: Full=Uncoordinated protein 16;
GN Name=unc-16 {ECO:0000312|WormBase:ZK1098.10e};
GN Synonyms=egl-39 {ECO:0000312|WormBase:ZK1098.10e};
GN ORFNames=ZK1098.10 {ECO:0000312|WormBase:ZK1098.10e};
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] (ISOFORM A), FUNCTION, INTERACTION WITH JNK-1;
RP JKK-1 AND SEK-1, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=10393177; DOI=10.1093/emboj/18.13.3604;
RA Kawasaki M., Hisamoto N., Iino Y., Yamamoto M., Ninomiya-Tsuji J.,
RA Matsumoto K.;
RT "A Caenorhabditis elegans JNK signal transduction pathway regulates
RT coordinated movement via type-D GABAergic motor neurons.";
RL EMBO J. 18:3604-3615(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=7906398; DOI=10.1038/368032a0;
RA Wilson R., Ainscough R., Anderson K., Baynes C., Berks M., Bonfield J.,
RA Burton J., Connell M., Copsey T., Cooper J., Coulson A., Craxton M.,
RA Dear S., Du Z., Durbin R., Favello A., Fraser A., Fulton L., Gardner A.,
RA Green P., Hawkins T., Hillier L., Jier M., Johnston L., Jones M.,
RA Kershaw J., Kirsten J., Laisster N., Latreille P., Lightning J., Lloyd C.,
RA Mortimore B., O'Callaghan M., Parsons J., Percy C., Rifken L., Roopra A.,
RA Saunders D., Shownkeen R., Sims M., Smaldon N., Smith A., Smith M.,
RA Sonnhammer E., Staden R., Sulston J., Thierry-Mieg J., Thomas K.,
RA Vaudin M., Vaughan K., Waterston R., Watson A., Weinstock L.,
RA Wilkinson-Sproat J., Wohldman P.;
RT "2.2 Mb of contiguous nucleotide sequence from chromosome III of C.
RT elegans.";
RL Nature 368:32-38(1994).
RN [3]
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 [4]
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND INTERACTION WITH
RP JNK-1; JKK-1 AND SEK-1.
RX PubMed=11738026; DOI=10.1016/s0896-6273(01)00532-3;
RA Byrd D.T., Kawasaki M., Walcoff M., Hisamoto N., Matsumoto K., Jin Y.;
RT "UNC-16, a JNK-signaling scaffold protein, regulates vesicle transport in
RT C. elegans.";
RL Neuron 32:787-800(2001).
RN [5]
RP FUNCTION, AND MUTAGENESIS OF LEU-75 AND 765-TRP--LYS-1157.
RX PubMed=30880001; DOI=10.1016/j.devcel.2019.02.013;
RA Hill S.E., Kauffman K.J., Krout M., Richmond J.E., Melia T.J.,
RA Colon-Ramos D.A.;
RT "Maturation and Clearance of Autophagosomes in Neurons Depends on a
RT Specific Cysteine Protease Isoform, ATG-4.2.";
RL Dev. Cell 49:251-266(2019).
CC -!- FUNCTION: The JNK-interacting protein (JIP) group of scaffold proteins
CC selectively mediates JNK signaling by aggregating specific components
CC of the MAPK cascade to form a functional JNK signaling module. May
CC function as a regulator of synaptic vesicle transport, through
CC interactions with the JNK-signaling components and motor proteins.
CC Binds specific components of the JNK signaling pathway namely jnk-1,
CC jkk-1 and sek-1. Associates with components of the motor protein,
CC kinesin-1. Pre-assembled unc-16 scaffolding complexes are then
CC transported as a cargo of kinesin, to the required subcellular
CC location. Regulates the retrograde transport of autophagosomes from the
CC neurites to the cell body of AIY interneurons (PubMed:30880001).
CC {ECO:0000269|PubMed:10393177, ECO:0000269|PubMed:11738026,
CC ECO:0000269|PubMed:30880001}.
CC -!- INTERACTION:
CC P34609; P46822: klc-2; NbExp=4; IntAct=EBI-315684, EBI-315578;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, perinuclear region
CC {ECO:0000269|PubMed:10393177, ECO:0000269|PubMed:11738026}.
CC Note=Diffusely localized throughout cell body but intensely localized
CC in regions adjacent to nucleus and at presumptive tips of neural
CC processes.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=16;
CC Name=e {ECO:0000312|WormBase:ZK1098.10e};
CC IsoId=P34609-1; Sequence=Displayed;
CC Name=a {ECO:0000312|WormBase:ZK1098.10a};
CC IsoId=P34609-3; Sequence=VSP_060417, VSP_060421;
CC Name=b {ECO:0000312|WormBase:ZK1098.10b};
CC IsoId=P34609-5; Sequence=VSP_060422;
CC Name=c {ECO:0000312|WormBase:ZK1098.10c};
CC IsoId=P34609-6; Sequence=VSP_060414;
CC Name=d {ECO:0000312|WormBase:ZK1098.10d};
CC IsoId=P34609-7; Sequence=VSP_060422, VSP_060428;
CC Name=f {ECO:0000312|WormBase:ZK1098.10f};
CC IsoId=P34609-8; Sequence=VSP_060416, VSP_060422;
CC Name=g {ECO:0000312|WormBase:ZK1098.10g};
CC IsoId=P34609-9; Sequence=VSP_060415;
CC Name=h {ECO:0000312|WormBase:ZK1098.10h};
CC IsoId=P34609-10; Sequence=VSP_060419, VSP_060426, VSP_060427;
CC Name=i {ECO:0000312|WormBase:ZK1098.10i};
CC IsoId=P34609-11; Sequence=VSP_060425;
CC Name=j {ECO:0000312|WormBase:ZK1098.10j};
CC IsoId=P34609-12; Sequence=VSP_060417, VSP_060420, VSP_060424,
CC VSP_060426, VSP_060427;
CC Name=k {ECO:0000312|WormBase:ZK1098.10k};
CC IsoId=P34609-13; Sequence=VSP_060416, VSP_060420, VSP_060424,
CC VSP_060426, VSP_060427;
CC Name=l {ECO:0000312|WormBase:ZK1098.10l};
CC IsoId=P34609-14; Sequence=VSP_060423, VSP_060426, VSP_060427;
CC Name=m {ECO:0000312|WormBase:ZK1098.10m};
CC IsoId=P34609-15; Sequence=VSP_060418, VSP_060420, VSP_060424,
CC VSP_060426, VSP_060427;
CC Name=n {ECO:0000312|WormBase:ZK1098.10n};
CC IsoId=P34609-16; Sequence=VSP_060421, VSP_060426, VSP_060427;
CC Name=o {ECO:0000312|WormBase:ZK1098.10o};
CC IsoId=P34609-17; Sequence=VSP_060415, VSP_060424;
CC Name=p {ECO:0000312|WormBase:ZK1098.10p};
CC IsoId=P34609-18; Sequence=VSP_060414, VSP_060428;
CC -!- TISSUE SPECIFICITY: Expressed in neurons of the ventral cord,
CC retrovesicular and preanal ganglia and nerve ring, intestinal cells,
CC seam and hypodermal cells, body wall, head muscle and pharynx.
CC {ECO:0000269|PubMed:10393177, ECO:0000269|PubMed:11738026}.
CC -!- SIMILARITY: Belongs to the JIP scaffold family. {ECO:0000305}.
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DR EMBL; AF424978; AAL23934.1; -; mRNA.
DR EMBL; BX284603; CAA80140.1; -; Genomic_DNA.
DR EMBL; BX284603; CAD45611.1; -; Genomic_DNA.
DR EMBL; BX284603; CAO82057.1; -; Genomic_DNA.
DR EMBL; BX284603; CAO82058.1; -; Genomic_DNA.
DR EMBL; BX284603; CAX51690.1; -; Genomic_DNA.
DR EMBL; BX284603; CBA11621.1; -; Genomic_DNA.
DR EMBL; BX284603; CDG24108.1; -; Genomic_DNA.
DR EMBL; BX284603; CDG24109.1; -; Genomic_DNA.
DR EMBL; BX284603; CDG24110.1; -; Genomic_DNA.
DR EMBL; BX284603; CDG24111.2; -; Genomic_DNA.
DR EMBL; BX284603; CDG24112.1; -; Genomic_DNA.
DR EMBL; BX284603; CDG24113.1; -; Genomic_DNA.
DR EMBL; BX284603; CDG24114.1; -; Genomic_DNA.
DR EMBL; BX284603; CDG24115.1; -; Genomic_DNA.
DR EMBL; BX284603; CDG24116.1; -; Genomic_DNA.
DR EMBL; BX284603; CDG24117.1; -; Genomic_DNA.
DR PIR; S40932; S40932.
DR RefSeq; NP_001022981.1; NM_001027810.3. [P34609-5]
DR RefSeq; NP_001122747.1; NM_001129275.2. [P34609-6]
DR RefSeq; NP_001122748.1; NM_001129276.1. [P34609-7]
DR RefSeq; NP_001255008.1; NM_001268079.1. [P34609-1]
DR RefSeq; NP_001255009.1; NM_001268080.1. [P34609-8]
DR RefSeq; NP_001293608.1; NM_001306679.1. [P34609-9]
DR RefSeq; NP_001293609.1; NM_001306680.1. [P34609-10]
DR RefSeq; NP_001293610.1; NM_001306681.1.
DR RefSeq; NP_001293611.1; NM_001306682.1. [P34609-12]
DR RefSeq; NP_001293612.1; NM_001306683.1. [P34609-13]
DR RefSeq; NP_001293613.1; NM_001306684.1. [P34609-14]
DR RefSeq; NP_001293614.1; NM_001306685.1. [P34609-15]
DR RefSeq; NP_001293615.1; NM_001306686.1. [P34609-16]
DR RefSeq; NP_001293616.1; NM_001306687.1. [P34609-17]
DR RefSeq; NP_001293617.1; NM_001306688.1. [P34609-18]
DR RefSeq; NP_741263.3; NM_171221.4. [P34609-3]
DR AlphaFoldDB; P34609; -.
DR BioGRID; 41544; 14.
DR DIP; DIP-25590N; -.
DR IntAct; P34609; 6.
DR STRING; 6239.ZK1098.10e; -.
DR iPTMnet; P34609; -.
DR EPD; P34609; -.
DR PaxDb; P34609; -.
DR PeptideAtlas; P34609; -.
DR EnsemblMetazoa; ZK1098.10a.1; ZK1098.10a.1; WBGene00006755. [P34609-3]
DR EnsemblMetazoa; ZK1098.10a.2; ZK1098.10a.2; WBGene00006755. [P34609-3]
DR EnsemblMetazoa; ZK1098.10b.1; ZK1098.10b.1; WBGene00006755. [P34609-5]
DR EnsemblMetazoa; ZK1098.10c.1; ZK1098.10c.1; WBGene00006755. [P34609-6]
DR EnsemblMetazoa; ZK1098.10d.1; ZK1098.10d.1; WBGene00006755. [P34609-7]
DR EnsemblMetazoa; ZK1098.10e.1; ZK1098.10e.1; WBGene00006755. [P34609-1]
DR EnsemblMetazoa; ZK1098.10f.1; ZK1098.10f.1; WBGene00006755. [P34609-8]
DR EnsemblMetazoa; ZK1098.10g.1; ZK1098.10g.1; WBGene00006755. [P34609-9]
DR EnsemblMetazoa; ZK1098.10h.1; ZK1098.10h.1; WBGene00006755. [P34609-10]
DR EnsemblMetazoa; ZK1098.10i.1; ZK1098.10i.1; WBGene00006755. [P34609-11]
DR EnsemblMetazoa; ZK1098.10j.1; ZK1098.10j.1; WBGene00006755. [P34609-12]
DR EnsemblMetazoa; ZK1098.10k.1; ZK1098.10k.1; WBGene00006755. [P34609-13]
DR EnsemblMetazoa; ZK1098.10l.1; ZK1098.10l.1; WBGene00006755. [P34609-14]
DR EnsemblMetazoa; ZK1098.10m.1; ZK1098.10m.1; WBGene00006755. [P34609-15]
DR EnsemblMetazoa; ZK1098.10n.1; ZK1098.10n.1; WBGene00006755. [P34609-16]
DR EnsemblMetazoa; ZK1098.10o.1; ZK1098.10o.1; WBGene00006755. [P34609-17]
DR EnsemblMetazoa; ZK1098.10p.1; ZK1098.10p.1; WBGene00006755. [P34609-18]
DR GeneID; 176349; -.
DR KEGG; cel:CELE_ZK1098.10; -.
DR UCSC; ZK1098.10b.1; c. elegans.
DR CTD; 176349; -.
DR WormBase; ZK1098.10a; CE00363; WBGene00006755; unc-16. [P34609-3]
DR WormBase; ZK1098.10b; CE31846; WBGene00006755; unc-16. [P34609-5]
DR WormBase; ZK1098.10c; CE41490; WBGene00006755; unc-16. [P34609-6]
DR WormBase; ZK1098.10d; CE41491; WBGene00006755; unc-16. [P34609-7]
DR WormBase; ZK1098.10e; CE43483; WBGene00006755; unc-16. [P34609-1]
DR WormBase; ZK1098.10f; CE44092; WBGene00006755; unc-16. [P34609-8]
DR WormBase; ZK1098.10g; CE48500; WBGene00006755; unc-16. [P34609-9]
DR WormBase; ZK1098.10h; CE48468; WBGene00006755; unc-16. [P34609-10]
DR WormBase; ZK1098.10i; CE48413; WBGene00006755; unc-16. [P34609-11]
DR WormBase; ZK1098.10j; CE48699; WBGene00006755; unc-16. [P34609-12]
DR WormBase; ZK1098.10k; CE48497; WBGene00006755; unc-16. [P34609-13]
DR WormBase; ZK1098.10l; CE48433; WBGene00006755; unc-16. [P34609-14]
DR WormBase; ZK1098.10m; CE48429; WBGene00006755; unc-16. [P34609-15]
DR WormBase; ZK1098.10n; CE48454; WBGene00006755; unc-16. [P34609-16]
DR WormBase; ZK1098.10o; CE48464; WBGene00006755; unc-16. [P34609-17]
DR WormBase; ZK1098.10p; CE48473; WBGene00006755; unc-16. [P34609-18]
DR eggNOG; KOG2077; Eukaryota.
DR GeneTree; ENSGT00940000153496; -.
DR HOGENOM; CLU_003841_0_0_1; -.
DR InParanoid; P34609; -.
DR OMA; YVTKMLG; -.
DR OrthoDB; 324912at2759; -.
DR Reactome; R-CEL-525793; Myogenesis.
DR SignaLink; P34609; -.
DR PRO; PR:P34609; -.
DR Proteomes; UP000001940; Chromosome III.
DR Bgee; WBGene00006755; Expressed in pharyngeal muscle cell (C elegans) and 4 other tissues.
DR GO; GO:0030424; C:axon; IDA:WormBase.
DR GO; GO:0043194; C:axon initial segment; IDA:WormBase.
DR GO; GO:0043679; C:axon terminus; IDA:WormBase.
DR GO; GO:0044297; C:cell body; IDA:WormBase.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0008432; F:JUN kinase binding; IBA:GO_Central.
DR GO; GO:0019900; F:kinase binding; IDA:WormBase.
DR GO; GO:0019894; F:kinesin binding; IMP:UniProtKB.
DR GO; GO:0005078; F:MAP-kinase scaffold activity; IDA:UniProtKB.
DR GO; GO:0030159; F:signaling receptor complex adaptor activity; IDA:WormBase.
DR GO; GO:0030421; P:defecation; IMP:WormBase.
DR GO; GO:0040011; P:locomotion; IMP:WormBase.
DR GO; GO:0018991; P:oviposition; IMP:WormBase.
DR GO; GO:0046328; P:regulation of JNK cascade; IDA:UniProtKB.
DR GO; GO:0030431; P:sleep; IMP:UniProtKB.
DR GO; GO:0048489; P:synaptic vesicle transport; IMP:WormBase.
DR GO; GO:0016192; P:vesicle-mediated transport; IMP:UniProtKB.
DR Gene3D; 2.130.10.10; -; 1.
DR InterPro; IPR039911; JIP3/JIP4.
DR InterPro; IPR032486; JIP_LZII.
DR InterPro; IPR019143; JNK/Rab-associated_protein-1_N.
DR InterPro; IPR011047; Quinoprotein_ADH-like_supfam.
DR InterPro; IPR034743; RH1.
DR InterPro; IPR034744; RH2.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR PANTHER; PTHR13886; PTHR13886; 1.
DR Pfam; PF16471; JIP_LZII; 1.
DR Pfam; PF09744; Jnk-SapK_ap_N; 1.
DR SUPFAM; SSF50998; SSF50998; 1.
DR PROSITE; PS51776; RH1; 1.
DR PROSITE; PS51777; RH2; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Coiled coil; Cytoplasm; Reference proteome.
FT CHAIN 1..1190
FT /note="JNK-interacting protein"
FT /id="PRO_0000220637"
FT DOMAIN 24..112
FT /note="RH1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01112"
FT DOMAIN 456..542
FT /note="RH2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01113"
FT REGION 1..35
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 263..364
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 775..829
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 78..165
FT /evidence="ECO:0000255"
FT COILED 383..491
FT /evidence="ECO:0000255"
FT COMPBIAS 1..24
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 272..292
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 810..824
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 1..644
FT /note="Missing (in isoform c and isoform p)"
FT /evidence="ECO:0000305"
FT /id="VSP_060414"
FT VAR_SEQ 1..350
FT /note="Missing (in isoform g and isoform o)"
FT /evidence="ECO:0000305"
FT /id="VSP_060415"
FT VAR_SEQ 1..259
FT /note="MACNLSPVNEMADSITSSTPSEIVYGGPGSPDEHRTMSDKVQTMASAIYREL
FT ETMIKVHGEDGVKTLMPLVVNVLEALDLAYLERDEQTAELEMLKEDNEQLQTQYEREKA
FT LRKQTEQKYIEIEDTLIGQNKELDKKIESLESIMRMLELKAKNATDHASRLEEREVEQK
FT LEFDRLHERYNTLLRTHVDHMERTKYLMGSEKFELMQNMPLPNMQLRNKMGMAASVDAS
FT SIRGVSDLISAHMTQSTTMDVNLANHITNE -> MNSNPQLTFI (in isoform f
FT and isoform k)"
FT /evidence="ECO:0000305"
FT /id="VSP_060416"
FT VAR_SEQ 1..36
FT /note="Missing (in isoform a and isoform j)"
FT /evidence="ECO:0000305"
FT /id="VSP_060417"
FT VAR_SEQ 219
FT /note="K -> NWFPISHRLHKSGDQSNLSL (in isoform m)"
FT /evidence="ECO:0000305"
FT /id="VSP_060418"
FT VAR_SEQ 330..363
FT /note="TDDESDWNGLGLIPRRHRPNEMLDDDDTSDDGSL -> TVNDTFI (in
FT isoform h)"
FT /evidence="ECO:0000305"
FT /id="VSP_060419"
FT VAR_SEQ 330
FT /note="T -> TGNLVDPAEFASA (in isoform j, isoform k and
FT isoform m)"
FT /evidence="ECO:0000305"
FT /id="VSP_060420"
FT VAR_SEQ 331..363
FT /note="DDESDWNGLGLIPRRHRPNEMLDDDDTSDDGSL -> GNLVDPAEFASAVND
FT TFI (in isoform a and isoform n)"
FT /evidence="ECO:0000305"
FT /id="VSP_060421"
FT VAR_SEQ 331..363
FT /note="Missing (in isoform b, isoform d and isoform f)"
FT /evidence="ECO:0000305"
FT /id="VSP_060422"
FT VAR_SEQ 331..363
FT /note="DDESDWNGLGLIPRRHRPNEMLDDDDTSDDGSL -> GNLVDPAEFASA
FT (in isoform l)"
FT /evidence="ECO:0000305"
FT /id="VSP_060423"
FT VAR_SEQ 363
FT /note="L -> LVNDTFI (in isoform j, isoform k, isoform m and
FT isoform o)"
FT /evidence="ECO:0000305"
FT /id="VSP_060424"
FT VAR_SEQ 554..1190
FT /note="SERRAAERREQYKLVREHVKKEDGRIEAYGWSLPNVEAEVSSVPIPVCCRPL
FT LDNEPSLKIWCATGVVLRGGRDERGQWIVGDPIYFAPASMKKTKTSNHRPELEDEIKRA
FT RNLDARESELDEWQSSSLVWVVSSNQGKSLIAVLDANNPNNIIETFPACDSHLLCIQAV
FT SGVMEGEPEMNEEQSKKYLSGGGKIKDLPEGLDGTDLGACEWVELRKMEDSEDGVPTYC
FT SNDMKPSPKRTRDFSISEVAPVDSSAPVKEDPLPPPANRPGGRAALPPHIRDAMSKYDG
FT VSGQMSGALPTVWMGGQNQYIYIHSAVTAWKQCLRRIKMPDAVLSIVHYKSRIFAALAN
FT GTIAIFHRNKHGEWSDEGYHSLRVGSATSSVRSLCLVSTNIWATYKNCVVVLDAESLQI
FT VKVFAAHPRKDSQVRNMQWVGAGVWLSIRLDSTLRLYHAHTYEHLQDVDIEPYVTKMLG
FT TSKLDFSYMRTTALLVSNRRLWIGTGTGVIISVPFSGQLEKKIETKDSKRPAGPGGLVR
FT VYGATSENATNDEKTNDDFIPYCNLAHAQLSFHGHKDSVKFFLGVPGASKNGEDESAEV
FT TLRRMLIMSGGDGYIDFRIGEENEPELTGQSIRPRDMSHLIIWEVDAELPILSK -> H
FT LSR (in isoform i)"
FT /evidence="ECO:0000305"
FT /id="VSP_060425"
FT VAR_SEQ 554..557
FT /note="SERR -> HLSR (in isoform h, isoform j, isoform k,
FT isoform l, isoform m and isoform n)"
FT /evidence="ECO:0000305"
FT /id="VSP_060426"
FT VAR_SEQ 558..1190
FT /note="Missing (in isoform h, isoform j, isoform k, isoform
FT l, isoform m and isoform n)"
FT /evidence="ECO:0000305"
FT /id="VSP_060427"
FT VAR_SEQ 810
FT /note="V -> VKAKTKLSRVSENVVPDETPKLIPLEKLK (in isoform d and
FT isoform p)"
FT /evidence="ECO:0000305"
FT /id="VSP_060428"
FT MUTAGEN 75
FT /note="L->P: In ju146; increases the number of lgg-1-
FT containing protein aggregates in the neurites of AIY
FT interneurons. This is further increased in either an atg-
FT 4.2 ola316 or atg-4.2 gk628327 mutant background. Reduces
FT the retrograde trafficking of autophagosomes in AIY
FT neurites, but increases anterograde autophagosome
FT trafficking and increases the number of autophagosomes
FT which are not trafficked. This results in an abnormal
FT accumulation of autophagic vacuoles in neurites."
FT /evidence="ECO:0000269|PubMed:30880001"
FT MUTAGEN 765..1157
FT /note="Missing: In n730; increases the number of lgg-1-
FT containing protein aggregates in the neurites of AIY
FT interneurons."
FT /evidence="ECO:0000269|PubMed:30880001"
SQ SEQUENCE 1190 AA; 134219 MW; 0AC346C0372882A2 CRC64;
MACNLSPVNE MADSITSSTP SEIVYGGPGS PDEHRTMSDK VQTMASAIYR ELETMIKVHG
EDGVKTLMPL VVNVLEALDL AYLERDEQTA ELEMLKEDNE QLQTQYEREK ALRKQTEQKY
IEIEDTLIGQ NKELDKKIES LESIMRMLEL KAKNATDHAS RLEEREVEQK LEFDRLHERY
NTLLRTHVDH MERTKYLMGS EKFELMQNMP LPNMQLRNKM GMAASVDASS IRGVSDLISA
HMTQSTTMDV NLANHITNED WQDEFSSDIE PSPRDIPQSS ADALTSPITT KEPTPKREAA
SPKQSEEEEA DETTSVDPKE NNDLLGADLT DDESDWNGLG LIPRRHRPNE MLDDDDTSDD
GSLGMGREVE NLIKENSELL DMKNALNIVK NDLINQVDEL NSENMILRDE NLSRQMVSEK
MQEQITKHEE EIKTLKQKLM EKENEQEEDD VPMAMRKRFT RSEMQRVLMD RNAYKEKLME
LEESIKWTEM QRAKKMQQQQ QNVNQKKSGG IWEFFSSLLG DSVTPPASSR GNRASSSRGK
MTRSVEYIDP DMISERRAAE RREQYKLVRE HVKKEDGRIE AYGWSLPNVE AEVSSVPIPV
CCRPLLDNEP SLKIWCATGV VLRGGRDERG QWIVGDPIYF APASMKKTKT SNHRPELEDE
IKRARNLDAR ESELDEWQSS SLVWVVSSNQ GKSLIAVLDA NNPNNIIETF PACDSHLLCI
QAVSGVMEGE PEMNEEQSKK YLSGGGKIKD LPEGLDGTDL GACEWVELRK MEDSEDGVPT
YCSNDMKPSP KRTRDFSISE VAPVDSSAPV KEDPLPPPAN RPGGRAALPP HIRDAMSKYD
GVSGQMSGAL PTVWMGGQNQ YIYIHSAVTA WKQCLRRIKM PDAVLSIVHY KSRIFAALAN
GTIAIFHRNK HGEWSDEGYH SLRVGSATSS VRSLCLVSTN IWATYKNCVV VLDAESLQIV
KVFAAHPRKD SQVRNMQWVG AGVWLSIRLD STLRLYHAHT YEHLQDVDIE PYVTKMLGTS
KLDFSYMRTT ALLVSNRRLW IGTGTGVIIS VPFSGQLEKK IETKDSKRPA GPGGLVRVYG
ATSENATNDE KTNDDFIPYC NLAHAQLSFH GHKDSVKFFL GVPGASKNGE DESAEVTLRR
MLIMSGGDGY IDFRIGEENE PELTGQSIRP RDMSHLIIWE VDAELPILSK
