SLAP2_CAEEL
ID SLAP2_CAEEL Reviewed; 927 AA.
AC Q02328; Q95PX2;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 11-JUL-2002, sequence version 3.
DT 03-AUG-2022, entry version 151.
DE RecName: Full=Huntington interacting protein related 1;
DE AltName: Full=Actin-binding protein SLA2 homolog;
GN Name=hipr-1; ORFNames=ZK370.3;
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 [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 [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]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=17928447; DOI=10.1523/jneurosci.1941-07.2007;
RA Parker J.A., Metzler M., Georgiou J., Mage M., Roder J.C., Rose A.M.,
RA Hayden M.R., Neri C.;
RT "Huntingtin-interacting protein 1 influences worm and mouse presynaptic
RT function and protects Caenorhabditis elegans neurons against mutant
RT polyglutamine toxicity.";
RL J. Neurosci. 27:11056-11064(2007).
CC -!- FUNCTION: Regulates pre-synaptic vesicle recycling at neuromuscular
CC junctions of mechanosensory neurons. Plays a role in maintaining a
CC normal defecation cycle. {ECO:0000269|PubMed:17928447}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=a;
CC IsoId=Q02328-1; Sequence=Displayed;
CC Name=b;
CC IsoId=Q02328-2; Sequence=VSP_000494, VSP_000495;
CC -!- DISRUPTION PHENOTYPE: RNAi-mediated knockdown causes a reduction in
CC progeny numbers and a lengthening of the defecation cycle. Touch
CC responses are normal. Expression of poly-Q 128Q (128Q consists of the
CC first 57 amino acids of human HTT with a 28 Gln residue expansion) in
CC RNAi-mediated knockdown animals causes a more severe reduction in touch
CC response compared to wild type expressing 128Q.
CC {ECO:0000269|PubMed:17928447}.
CC -!- SIMILARITY: Belongs to the SLA2 family. {ECO:0000305}.
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DR EMBL; FO080164; CCD61721.1; -; Genomic_DNA.
DR EMBL; FO080164; CCD61722.1; -; Genomic_DNA.
DR PIR; E88537; E88537.
DR RefSeq; NP_498925.1; NM_066524.3. [Q02328-2]
DR RefSeq; NP_741253.1; NM_171215.5. [Q02328-1]
DR AlphaFoldDB; Q02328; -.
DR SMR; Q02328; -.
DR BioGRID; 41427; 17.
DR ELM; Q02328; -.
DR IntAct; Q02328; 2.
DR STRING; 6239.ZK370.3a.1; -.
DR EPD; Q02328; -.
DR PaxDb; Q02328; -.
DR PeptideAtlas; Q02328; -.
DR EnsemblMetazoa; ZK370.3a.1; ZK370.3a.1; WBGene00022717. [Q02328-1]
DR EnsemblMetazoa; ZK370.3b.1; ZK370.3b.1; WBGene00022717. [Q02328-2]
DR EnsemblMetazoa; ZK370.3b.2; ZK370.3b.2; WBGene00022717. [Q02328-2]
DR GeneID; 176224; -.
DR KEGG; cel:CELE_ZK370.3; -.
DR CTD; 176224; -.
DR WormBase; ZK370.3a; CE00540; WBGene00022717; hipr-1. [Q02328-1]
DR WormBase; ZK370.3b; CE29640; WBGene00022717; hipr-1. [Q02328-2]
DR eggNOG; KOG0980; Eukaryota.
DR GeneTree; ENSGT00940000153594; -.
DR InParanoid; Q02328; -.
DR OMA; MQNRFTA; -.
DR OrthoDB; 104219at2759; -.
DR PhylomeDB; Q02328; -.
DR Reactome; R-CEL-432722; Golgi Associated Vesicle Biogenesis.
DR Reactome; R-CEL-8856828; Clathrin-mediated endocytosis.
DR PRO; PR:Q02328; -.
DR Proteomes; UP000001940; Chromosome III.
DR Bgee; WBGene00022717; Expressed in pharyngeal muscle cell (C elegans) and 4 other tissues.
DR GO; GO:0030136; C:clathrin-coated vesicle; IBA:GO_Central.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0098793; C:presynapse; IEA:GOC.
DR GO; GO:0051015; F:actin filament binding; IBA:GO_Central.
DR GO; GO:0035615; F:clathrin adaptor activity; IBA:GO_Central.
DR GO; GO:0032051; F:clathrin light chain binding; IBA:GO_Central.
DR GO; GO:0043325; F:phosphatidylinositol-3,4-bisphosphate binding; IBA:GO_Central.
DR GO; GO:0080025; F:phosphatidylinositol-3,5-bisphosphate binding; IBA:GO_Central.
DR GO; GO:0007015; P:actin filament organization; IBA:GO_Central.
DR GO; GO:0048268; P:clathrin coat assembly; IBA:GO_Central.
DR GO; GO:0030421; P:defecation; IMP:WormBase.
DR GO; GO:0032502; P:developmental process; IMP:WormBase.
DR GO; GO:0006897; P:endocytosis; IBA:GO_Central.
DR GO; GO:0007269; P:neurotransmitter secretion; IMP:WormBase.
DR GO; GO:0008104; P:protein localization; IMP:WormBase.
DR GO; GO:0007624; P:ultradian rhythm; IMP:WormBase.
DR Gene3D; 1.25.40.90; -; 1.
DR InterPro; IPR011417; ANTH_dom.
DR InterPro; IPR013809; ENTH.
DR InterPro; IPR008942; ENTH_VHS.
DR InterPro; IPR035964; I/LWEQ_dom_sf.
DR InterPro; IPR002558; ILWEQ_dom.
DR InterPro; IPR030224; Sla2_fam.
DR PANTHER; PTHR10407; PTHR10407; 2.
DR Pfam; PF07651; ANTH; 1.
DR Pfam; PF01608; I_LWEQ; 1.
DR SMART; SM00273; ENTH; 1.
DR SMART; SM00307; ILWEQ; 1.
DR SUPFAM; SSF109885; SSF109885; 1.
DR SUPFAM; SSF48464; SSF48464; 1.
DR PROSITE; PS50942; ENTH; 1.
DR PROSITE; PS50945; I_LWEQ; 1.
PE 3: Inferred from homology;
KW Actin-binding; Alternative splicing; Coiled coil; Cytoplasm; Cytoskeleton;
KW Endocytosis; Reference proteome.
FT CHAIN 1..927
FT /note="Huntington interacting protein related 1"
FT /id="PRO_0000071949"
FT DOMAIN 7..136
FT /note="ENTH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00243"
FT DOMAIN 673..914
FT /note="I/LWEQ"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00292"
FT COILED 336..524
FT /evidence="ECO:0000255"
FT VAR_SEQ 921
FT /note="E -> S (in isoform b)"
FT /evidence="ECO:0000305"
FT /id="VSP_000494"
FT VAR_SEQ 922..927
FT /note="Missing (in isoform b)"
FT /evidence="ECO:0000305"
FT /id="VSP_000495"
SQ SEQUENCE 927 AA; 104428 MW; F76A356EBBF1183D CRC64;
MDHRAQAREV FVRAQLEAVQ KAITKNEVPL KPKHARTIIV GTHKEKSSGI FWHTVGRIQL
EKHPVLTWKF CHLVHKLLRD GHRKVPEETY RYVNRFTQLS QFWKHLNTSG YGPCIESYCK
LLHDRVTFHN KYPVVPGKLD LNDSQLKTLE GDLDNMFEMT IDMLDQMDAL LVLQDRVYEM
MNSLRWNSLI PQGQCMLSPL IIAILDTSKF YDYLVKMIFK LHSQVPPDAL EGHRSRFRTI
FERTKKFYEE SSNLQYFKYL VSIPTLPSHA PNFLQQSDLE SYRTPHAYLH SEGSEDGTSL
NGHDGELLNL AEAEPQQASP SSQPDPREEQ IVMLSRAVED EKFAKERLIQ EARSRIEQYE
NRLLQMQGEF DHAKREADEN REEAQRLKNE LALRDASRTQ TDDARVKEAE LKATAAEERF
NKMKGVYEKF RSEHVLALTK LGDIQKQLEA SEKSKFDKDE EITALNRKVE EAQREAGRAL
TKAEGDAGAV DEMRTQLVKA DIEVEELKRT IDHLRESHAN QLVQSSAEET NKIRLAELEV
AKESGVGITQ MFDHCEDALQ NATSITYPPH LAQSAMNNLV NILSNERLDE PLATKDNVFA
GHLLSTTLSA AASAAYTASI ESYEGVNDQC KKVLAAAKVA FSDDSALSRA DKMKLLRQDI
QTLNSLMISL PLQTDIDKDV VGNELEQEMR RMDDAIRRAV QEIEAIQRRA RESSDGIRLE
VNESILANCQ ALMSVIMQLV IASRELQTEI VAAGKAGGSP AEFYKRNHQW TEGLLSAAKA
VGVAARVLVE SADGVVTGKG KFEHLIVAAQ EIAASTAQLF VSSRVKADKD SSKLDALSVA
AKAVNQNTAQ VVAAVKNGQT TLNDEGSLDF SYLSLHAAKK EEMESQVKML ELEQSLNQER
AKLAALRKQH YHMAQLVANK EGEEAQE
