PICAL_CAEEL
ID PICAL_CAEEL Reviewed; 586 AA.
AC Q9XZI6; Q95Q72; Q95Q73; Q95Q74; Q95Q75; Q9UA04; Q9UA05; Q9XZI7; Q9XZI8;
AC Q9XZI9;
DT 01-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 149.
DE RecName: Full=Phosphatidylinositol-binding clathrin assembly protein unc-11;
DE AltName: Full=AP180-like adaptor protein;
DE AltName: Full=Uncoordinated protein 11;
GN Name=unc-11; ORFNames=C32E8.10;
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239 {ECO:0000312|EMBL:AAD37365.1};
RN [1] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS A; B; C; D AND E), FUNCTION, AND
RP SUBCELLULAR LOCATION.
RC STRAIN=Bristol N2 {ECO:0000269|PubMed:10397769};
RX PubMed=10397769; DOI=10.1091/mbc.10.7.2343;
RA Nonet M.L., Holgado A.M., Brewer F., Serpe C.J., Norbeck B.A., Holleran J.,
RA Wei L., Hartwieg E., Jorgensen E.M., Alfonso A.;
RT "UNC-11, a Caenorhabditis elegans AP180 homologue, regulates the size and
RT protein composition of synaptic vesicles.";
RL Mol. Biol. Cell 10:2343-2360(1999).
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).
CC -!- FUNCTION: Assembly protein recruiting clathrin and adaptor protein
CC complex 2 (AP2) to cell membranes at sites of coated-pit formation and
CC clathrin-vesicle assembly. May be required to determine the amount of
CC membrane to be recycled, possibly by regulating the size of the
CC clathrin cage. Involved in AP2-dependent clathrin-mediated endocytosis
CC at the neuromuscular junction. Required for the efficient targeting of
CC the synaptic vesicle protein synaptobrevin.
CC {ECO:0000269|PubMed:10397769}.
CC -!- SUBUNIT: Binds clathrin and phosphatidylinositol 4,5-bisphosphate.
CC {ECO:0000250}.
CC -!- INTERACTION:
CC Q9XZI6; O17670: eya-1; NbExp=4; IntAct=EBI-311866, EBI-311862;
CC Q9XZI6; Q9U2T9: itsn-1; NbExp=3; IntAct=EBI-311866, EBI-2414252;
CC Q9XZI6; Q95XW5: magu-1; NbExp=3; IntAct=EBI-311866, EBI-2317194;
CC Q9XZI6; G5EC32: sorb-1; NbExp=3; IntAct=EBI-311866, EBI-325337;
CC -!- SUBCELLULAR LOCATION: Membrane, clathrin-coated pit
CC {ECO:0000269|PubMed:10397769}. Golgi apparatus
CC {ECO:0000269|PubMed:10397769}. Cytoplasmic vesicle, clathrin-coated
CC vesicle {ECO:0000269|PubMed:10397769}. Note=Colocalized with clathrin
CC in the Golgi area.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=9;
CC Name=A {ECO:0000269|PubMed:10397769}; Synonyms=a {ECO:0000305};
CC IsoId=Q9XZI6-1; Sequence=Displayed;
CC Name=B {ECO:0000269|PubMed:10397769}; Synonyms=h {ECO:0000305};
CC IsoId=Q9XZI6-2; Sequence=VSP_050682, VSP_050683;
CC Name=C {ECO:0000269|PubMed:10397769}; Synonyms=b {ECO:0000305};
CC IsoId=Q9XZI6-3; Sequence=VSP_050682;
CC Name=c;
CC IsoId=Q9XZI6-7; Sequence=VSP_020101;
CC Name=D {ECO:0000269|PubMed:10397769};
CC IsoId=Q9XZI6-4; Sequence=VSP_050681, VSP_050683;
CC Name=d;
CC IsoId=Q9XZI6-8; Sequence=VSP_020099, VSP_020100;
CC Name=E {ECO:0000269|PubMed:10397769};
CC IsoId=Q9XZI6-5; Sequence=VSP_050680;
CC Name=e;
CC IsoId=Q9XZI6-9; Sequence=VSP_020098, VSP_020102;
CC Name=f {ECO:0000305};
CC IsoId=Q9XZI6-6; Sequence=VSP_050679;
CC -!- TISSUE SPECIFICITY: High levels in the nervous system and at lower
CC levels in other tissues. In neurons, enriched at presynaptic terminals
CC and is also present in cell bodies. {ECO:0000269|PubMed:10397769}.
CC -!- SIMILARITY: Belongs to the PICALM/SNAP91 family. {ECO:0000305}.
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DR EMBL; AF144257; AAD37365.1; -; mRNA.
DR EMBL; AF144258; AAD37366.1; -; mRNA.
DR EMBL; AF144259; AAD37367.1; -; mRNA.
DR EMBL; AF144260; AAD37368.1; -; mRNA.
DR EMBL; AF144261; AAD37369.1; -; mRNA.
DR EMBL; AF144262; AAD37370.1; -; mRNA.
DR EMBL; FO080749; CCD66409.1; -; Genomic_DNA.
DR EMBL; FO080749; CCD66410.1; -; Genomic_DNA.
DR EMBL; FO080749; CCD66411.1; -; Genomic_DNA.
DR EMBL; FO080749; CCD66412.1; -; Genomic_DNA.
DR EMBL; FO080749; CCD66413.1; -; Genomic_DNA.
DR EMBL; FO080749; CCD66414.1; -; Genomic_DNA.
DR EMBL; FO080749; CCD66415.1; -; Genomic_DNA.
DR RefSeq; NP_001021014.1; NM_001025843.2. [Q9XZI6-3]
DR RefSeq; NP_001021015.1; NM_001025844.1.
DR RefSeq; NP_001021016.1; NM_001025845.2. [Q9XZI6-2]
DR RefSeq; NP_491227.1; NM_058826.1. [Q9XZI6-1]
DR RefSeq; NP_491228.1; NM_058827.3.
DR RefSeq; NP_491229.1; NM_058828.1.
DR RefSeq; NP_491230.1; NM_058829.3. [Q9XZI6-6]
DR AlphaFoldDB; Q9XZI6; -.
DR SMR; Q9XZI6; -.
DR BioGRID; 37426; 10.
DR DIP; DIP-25315N; -.
DR IntAct; Q9XZI6; 8.
DR iPTMnet; Q9XZI6; -.
DR EPD; Q9XZI6; -.
DR PeptideAtlas; Q9XZI6; -.
DR EnsemblMetazoa; C32E8.10a.1; C32E8.10a.1; WBGene00006751. [Q9XZI6-1]
DR EnsemblMetazoa; C32E8.10b.1; C32E8.10b.1; WBGene00006751. [Q9XZI6-3]
DR EnsemblMetazoa; C32E8.10c.1; C32E8.10c.1; WBGene00006751.
DR EnsemblMetazoa; C32E8.10d.1; C32E8.10d.1; WBGene00006751.
DR EnsemblMetazoa; C32E8.10e.1; C32E8.10e.1; WBGene00006751.
DR EnsemblMetazoa; C32E8.10f.1; C32E8.10f.1; WBGene00006751. [Q9XZI6-6]
DR EnsemblMetazoa; C32E8.10h.1; C32E8.10h.1; WBGene00006751. [Q9XZI6-2]
DR GeneID; 171952; -.
DR KEGG; cel:CELE_C32E8.10; -.
DR UCSC; C32E8.10f; c. elegans. [Q9XZI6-1]
DR CTD; 171952; -.
DR WormBase; C32E8.10a; CE23562; WBGene00006751; unc-11. [Q9XZI6-1]
DR WormBase; C32E8.10b; CE27812; WBGene00006751; unc-11. [Q9XZI6-3]
DR WormBase; C32E8.10c; CE24822; WBGene00006751; unc-11. [Q9XZI6-7]
DR WormBase; C32E8.10d; CE23564; WBGene00006751; unc-11. [Q9XZI6-8]
DR WormBase; C32E8.10e; CE23565; WBGene00006751; unc-11. [Q9XZI6-9]
DR WormBase; C32E8.10f; CE23566; WBGene00006751; unc-11. [Q9XZI6-6]
DR WormBase; C32E8.10h; CE27813; WBGene00006751; unc-11. [Q9XZI6-2]
DR GeneTree; ENSGT00950000183068; -.
DR InParanoid; Q9XZI6; -.
DR OMA; RDSAWTI; -.
DR OrthoDB; 755817at2759; -.
DR PhylomeDB; Q9XZI6; -.
DR Reactome; R-CEL-432722; Golgi Associated Vesicle Biogenesis.
DR Reactome; R-CEL-8856825; Cargo recognition for clathrin-mediated endocytosis.
DR Reactome; R-CEL-8856828; Clathrin-mediated endocytosis.
DR PRO; PR:Q9XZI6; -.
DR Proteomes; UP000001940; Chromosome I.
DR Bgee; WBGene00006751; Expressed in pharyngeal muscle cell (C elegans) and 4 other tissues.
DR GO; GO:0005905; C:clathrin-coated pit; IDA:UniProtKB.
DR GO; GO:0030136; C:clathrin-coated vesicle; IBA:GO_Central.
DR GO; GO:0098894; C:extrinsic component of presynaptic endocytic zone membrane; IBA:GO_Central.
DR GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-SubCell.
DR GO; GO:0042734; C:presynaptic membrane; IDA:WormBase.
DR GO; GO:0008021; C:synaptic vesicle; IBA:GO_Central.
DR GO; GO:0005545; F:1-phosphatidylinositol binding; ISS:UniProtKB.
DR GO; GO:0030276; F:clathrin binding; ISS:WormBase.
DR GO; GO:0032050; F:clathrin heavy chain binding; IBA:GO_Central.
DR GO; GO:0005546; F:phosphatidylinositol-4,5-bisphosphate binding; IBA:GO_Central.
DR GO; GO:0000149; F:SNARE binding; IBA:GO_Central.
DR GO; GO:0048268; P:clathrin coat assembly; IEA:InterPro.
DR GO; GO:0072583; P:clathrin-dependent endocytosis; IBA:GO_Central.
DR GO; GO:0040011; P:locomotion; IMP:WormBase.
DR GO; GO:0010940; P:positive regulation of necrotic cell death; IGI:WormBase.
DR GO; GO:0009791; P:post-embryonic development; IMP:WormBase.
DR GO; GO:1903539; P:protein localization to postsynaptic membrane; IMP:UniProtKB.
DR GO; GO:0006898; P:receptor-mediated endocytosis; IDA:UniProtKB.
DR GO; GO:1902683; P:regulation of receptor localization to synapse; IDA:UniProtKB.
DR GO; GO:0016185; P:synaptic vesicle budding from presynaptic endocytic zone membrane; IBA:GO_Central.
DR GO; GO:0048488; P:synaptic vesicle endocytosis; IMP:WormBase.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IMP:UniProtKB.
DR GO; GO:0006900; P:vesicle budding from membrane; IBA:GO_Central.
DR Gene3D; 1.20.58.150; -; 1.
DR Gene3D; 1.25.40.90; -; 1.
DR InterPro; IPR011417; ANTH_dom.
DR InterPro; IPR014712; ANTH_dom_sf.
DR InterPro; IPR045192; AP180-like.
DR InterPro; IPR013809; ENTH.
DR InterPro; IPR008942; ENTH_VHS.
DR PANTHER; PTHR22951; PTHR22951; 1.
DR Pfam; PF07651; ANTH; 1.
DR SMART; SM00273; ENTH; 1.
DR SUPFAM; SSF48464; SSF48464; 1.
DR PROSITE; PS50942; ENTH; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Coated pit; Cytoplasmic vesicle; Endocytosis;
KW Golgi apparatus; Membrane; Reference proteome.
FT CHAIN 1..586
FT /note="Phosphatidylinositol-binding clathrin assembly
FT protein unc-11"
FT /id="PRO_0000187065"
FT DOMAIN 29..161
FT /note="ENTH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00243,
FT ECO:0000305"
FT REGION 450..474
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 1..388
FT /note="Missing (in isoform f)"
FT /evidence="ECO:0000305"
FT /id="VSP_050679"
FT VAR_SEQ 383..512
FT /note="Missing (in isoform E)"
FT /evidence="ECO:0000303|PubMed:10397769"
FT /id="VSP_050680"
FT VAR_SEQ 383..467
FT /note="QPDLLDMFQSSAAPAPQTADVTNPFGNFAAPSAFPTNVPPPAAHSAPFGVQP
FT APQHSAAPFYANLHQAPPMQSQAPNGHQAAPFG -> HQCIRLQWECINNHLVLSQCGI
FT LRWQHTVNNMDTDNLFHHNSNTKFNWFMQRWLQRTLHKLNRPRPPQPIHLDYSLVVYFS
FT LSLS (in isoform e)"
FT /evidence="ECO:0000303|PubMed:10397769"
FT /id="VSP_020098"
FT VAR_SEQ 397..449
FT /note="Missing (in isoform D)"
FT /evidence="ECO:0000303|PubMed:10397769"
FT /id="VSP_050681"
FT VAR_SEQ 397..408
FT /note="APQTADVTNPFG -> LLQCNRKLQMVS (in isoform d)"
FT /evidence="ECO:0000303|PubMed:10397769"
FT /id="VSP_020099"
FT VAR_SEQ 409..460
FT /note="Missing (in isoform d)"
FT /evidence="ECO:0000303|PubMed:10397769"
FT /id="VSP_020100"
FT VAR_SEQ 419..458
FT /note="Missing (in isoform C and isoform B)"
FT /evidence="ECO:0000303|PubMed:10397769"
FT /id="VSP_050682"
FT VAR_SEQ 459
FT /note="N -> NEPENPFITAPAAPQMHNAPPVPPPPASQGAPAPINPFADPSATAAS
FT SAQPFGDPDDFKFEQKNVKIKILIP (in isoform c)"
FT /evidence="ECO:0000303|PubMed:10397769"
FT /id="VSP_020101"
FT VAR_SEQ 468..586
FT /note="Missing (in isoform e)"
FT /evidence="ECO:0000303|PubMed:10397769"
FT /id="VSP_020102"
FT VAR_SEQ 489
FT /note="G -> GYR (in isoform B and isoform D)"
FT /evidence="ECO:0000303|PubMed:10397769"
FT /id="VSP_050683"
SQ SEQUENCE 586 AA; 64064 MW; 6E337A81D302DD81 CRC64;
MQTIEKALHQ PMPFTTGGQT ISDRLTAAKH SLAGSQLGKT ICKATTEEVM APKKKHLDYL
LHCTNEPNVS IPSMANLLIE RTQNPNWTVV YKALITIHNI MCYGNERFSQ YLASCNTTFN
LTAFVDKVGG AGGYDMSTHV RRYAKYIGEK INTYRMCAFD FCKVKRGRED GLLRTMHTDK
LLKTIPILQN QIDALLEFSV TTSELNNGVI NCSFILLFRD LIRLFACYND GIINVLEKYF
DMNKKQCRDA LDTYKSFLTR LDKVAEFLRV AESVGIDRGE IPDLTRAPAS LLEALEAHLI
HLEGGKAPPP TQQHVAPHQF TTGFAFSQQP QPALGDAERQ RYIELEQERL RQFEDQKKSI
NSANPFANDV ASAAPAPATS AAQPDLLDMF QSSAAPAPQT ADVTNPFGNF AAPSAFPTNV
PPPAAHSAPF GVQPAPQHSA APFYANLHQA PPMQSQAPNG HQAAPFGYPN AHPDDLARMT
AQMSLNQQGA PAGWNTTTSA VSNNPFGATS APQPMYTAPM GMYQQPFGAQ PMWNPAMAAY
GQQYGYGQPV PPQQQHQIQL VHAAMAAKNA AQAQQAQAAS ADPFGL
