ADD1_CAEEL
ID ADD1_CAEEL Reviewed; 732 AA.
AC Q9U9K0; O44581; Q95X64; Q9U9J9;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 02-AUG-2002, sequence version 2.
DT 03-AUG-2022, entry version 149.
DE RecName: Full=Adducin-related protein 1;
GN Name=add-1; ORFNames=F39C12.2;
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] (ISOFORMS A AND B).
RA Moorthy S., Bennett V.;
RT "Molecular and functional analysis of the spectrin based membrane skeleton
RT in Caenorhabditis elegans.";
RL Submitted (JUL-1999) to the EMBL/GenBank/DDBJ databases.
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: Membrane-cytoskeleton-associated protein that promotes the
CC assembly of the spectrin-actin network. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000250}. Cell
CC membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250};
CC Cytoplasmic side {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Comment=Experimental confirmation may be lacking for some isoforms.;
CC Name=b;
CC IsoId=Q9U9K0-1; Sequence=Displayed;
CC Name=a;
CC IsoId=Q9U9K0-2; Sequence=VSP_000194, VSP_000196;
CC Name=c;
CC IsoId=Q9U9K0-3; Sequence=VSP_000195;
CC Name=d;
CC IsoId=Q9U9K0-4; Sequence=VSP_000193;
CC -!- SIMILARITY: Belongs to the aldolase class II family. Adducin subfamily.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AF166167; AAD49856.1; -; mRNA.
DR EMBL; AF166168; AAD49857.1; -; mRNA.
DR EMBL; FO081331; CCD70842.1; -; Genomic_DNA.
DR EMBL; FO081331; CCD70843.1; -; Genomic_DNA.
DR EMBL; FO081331; CCD70844.1; -; Genomic_DNA.
DR EMBL; FO081331; CCD70845.1; -; Genomic_DNA.
DR RefSeq; NP_001024639.1; NM_001029468.2. [Q9U9K0-2]
DR RefSeq; NP_001024640.1; NM_001029469.2. [Q9U9K0-1]
DR RefSeq; NP_001024641.1; NM_001029470.2. [Q9U9K0-3]
DR RefSeq; NP_001024642.1; NM_001029471.1. [Q9U9K0-4]
DR AlphaFoldDB; Q9U9K0; -.
DR SMR; Q9U9K0; -.
DR BioGRID; 45695; 8.
DR IntAct; Q9U9K0; 3.
DR MINT; Q9U9K0; -.
DR STRING; 6239.F39C12.2b; -.
DR iPTMnet; Q9U9K0; -.
DR EPD; Q9U9K0; -.
DR PaxDb; Q9U9K0; -.
DR EnsemblMetazoa; F39C12.2a.1; F39C12.2a.1; WBGene00000072. [Q9U9K0-2]
DR EnsemblMetazoa; F39C12.2b.1; F39C12.2b.1; WBGene00000072. [Q9U9K0-1]
DR EnsemblMetazoa; F39C12.2c.1; F39C12.2c.1; WBGene00000072. [Q9U9K0-3]
DR EnsemblMetazoa; F39C12.2d.1; F39C12.2d.1; WBGene00000072. [Q9U9K0-4]
DR GeneID; 180760; -.
DR KEGG; cel:CELE_F39C12.2; -.
DR UCSC; F39C12.2b; c. elegans. [Q9U9K0-1]
DR CTD; 180760; -.
DR WormBase; F39C12.2a; CE28308; WBGene00000072; add-1. [Q9U9K0-2]
DR WormBase; F39C12.2b; CE28309; WBGene00000072; add-1. [Q9U9K0-1]
DR WormBase; F39C12.2c; CE29794; WBGene00000072; add-1. [Q9U9K0-3]
DR WormBase; F39C12.2d; CE30979; WBGene00000072; add-1. [Q9U9K0-4]
DR eggNOG; KOG3699; Eukaryota.
DR InParanoid; Q9U9K0; -.
DR OMA; KITKWVQ; -.
DR OrthoDB; 400524at2759; -.
DR PhylomeDB; Q9U9K0; -.
DR Reactome; R-CEL-264870; Caspase-mediated cleavage of cytoskeletal proteins.
DR Reactome; R-CEL-5223345; Miscellaneous transport and binding events.
DR Reactome; R-CEL-9013405; RHOD GTPase cycle.
DR Reactome; R-CEL-9035034; RHOF GTPase cycle.
DR PRO; PR:Q9U9K0; -.
DR Proteomes; UP000001940; Chromosome X.
DR Bgee; WBGene00000072; Expressed in larva and 3 other tissues.
DR ExpressionAtlas; Q9U9K0; baseline and differential.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0005856; C:cytoskeleton; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0014069; C:postsynaptic density; IDA:WormBase.
DR GO; GO:0051015; F:actin filament binding; ISS:WormBase.
DR GO; GO:0051016; P:barbed-end actin filament capping; ISS:WormBase.
DR GO; GO:0007616; P:long-term memory; IMP:WormBase.
DR GO; GO:0007613; P:memory; IMP:WormBase.
DR GO; GO:0097120; P:receptor localization to synapse; IMP:WormBase.
DR GO; GO:2000249; P:regulation of actin cytoskeleton reorganization; IMP:WormBase.
DR GO; GO:0007614; P:short-term memory; IMP:WormBase.
DR Gene3D; 3.40.225.10; -; 1.
DR InterPro; IPR001303; Aldolase_II/adducin_N.
DR InterPro; IPR036409; Aldolase_II/adducin_N_sf.
DR Pfam; PF00596; Aldolase_II; 1.
DR SMART; SM01007; Aldolase_II; 1.
DR SUPFAM; SSF53639; SSF53639; 1.
PE 2: Evidence at transcript level;
KW Actin-binding; Alternative splicing; Cell membrane; Cytoplasm;
KW Cytoskeleton; Membrane; Reference proteome.
FT CHAIN 1..732
FT /note="Adducin-related protein 1"
FT /id="PRO_0000218540"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 684..732
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 684..705
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 706..732
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 645..694
FT /note="Missing (in isoform d)"
FT /evidence="ECO:0000305"
FT /id="VSP_000193"
FT VAR_SEQ 665..679
FT /note="CDHPSPMSISTEYPE -> YPDILRPIYRQETYV (in isoform a)"
FT /evidence="ECO:0000303|Ref.1"
FT /id="VSP_000194"
FT VAR_SEQ 666..695
FT /note="Missing (in isoform c)"
FT /evidence="ECO:0000305"
FT /id="VSP_000195"
FT VAR_SEQ 680..732
FT /note="Missing (in isoform a)"
FT /evidence="ECO:0000303|Ref.1"
FT /id="VSP_000196"
FT CONFLICT 377
FT /note="P -> S (in Ref. 1; AAD49856/AAD49857)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 732 AA; 82170 MW; CBEA2AAD053C6322 CRC64;
MIGRKEKERE RPYYRDPDDP EYIKDLQRPA VIKEDLSEME RRKRVQQILE SKSFCHELEE
VIRQECDTAR TDPDHLQVLQ KLSDLTVPQG NMSFGNLHTY GGNTIAIADL RGNEKYSKAE
RIQRNKLACL FRLADLFQWS QGIHNEISYR TNDEDNTFLM NPFGLLYHEI TAATIVKIDE
NGKILDCGTL KAGVNQPAFL LHSAIYKAHP MVRCILHMHT AIVAAVASMK CGLLPLCKEA
MVLGPVGYHD YQDIGDDDIQ FDEIIANLGD KNVLFLRNQG FLVVGDTIEH ATFLANNTVI
ACETQVRAAR AGLDNLIIPE EKAIQRAFRN SRNTNSLKRN GTVDWRVGEL EWESWMRVLD
HANFQTGHVY RQPQLRPKSA MSTSMVNNND VAVPPTTSAY GQIDETNLES VSAHRLALLR
KEQERVRWMN SPNAYQKVEF LEYGADNPKK ITKWVHDVNV PSASGTPVKI SSVHQFSPAS
SNPKEFKEKQ KAIKENNRLG TLSAGPQSQI LDSVTYEDIA LLIKPDNDGT VGQSSTADRA
ILIGTASKGI IDRQFQHHAQ VYHQIYAPNP FSVETDADIK KYVDMVKAKN SQSAPVSARS
GYSQYDEVEA DTVSLMQGVR EHKLSQAALS ASDDGLNAGI SPNNVRTSEE SVNTSYMSQS
VVFDCDHPSP MSISTEYPEK VKMTRFSSTQ GTSEGNTTSR SCTTASEEEK PTKDEKKKKK
KGFLSFMRKK DK