PICAL_DROME
ID PICAL_DROME Reviewed; 468 AA.
AC Q9VI75; O96528; Q8MQM1;
DT 01-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT 23-OCT-2007, sequence version 3.
DT 03-AUG-2022, entry version 159.
DE RecName: Full=Phosphatidylinositol-binding clathrin assembly protein LAP;
DE AltName: Full=Like-AP180;
GN Name=lap; ORFNames=CG2520;
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227 {ECO:0000312|EMBL:AAM75091.1};
RN [1] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RC TISSUE=Head {ECO:0000269|PubMed:9883738};
RX PubMed=9883738; DOI=10.1016/s0896-6273(00)80664-9;
RA Zhang B., Koh Y.H., Beckstead R.B., Budnik V., Ganetzky B., Bellen H.J.;
RT "Synaptic vesicle size and number are regulated by a clathrin adaptor
RT protein required for endocytosis.";
RL Neuron 21:1465-1475(1998).
RN [2] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley {ECO:0000269|PubMed:10731132};
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=Berkeley;
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [4] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley {ECO:0000269|PubMed:12537569};
RC TISSUE=Head {ECO:0000269|PubMed:12537569};
RX PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A.,
RA Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA Celniker S.E.;
RT "A Drosophila full-length cDNA resource.";
RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
RN [5] {ECO:0000305}
RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 4-301.
RX PubMed=11239400; DOI=10.1016/s0092-8674(01)00230-6;
RA Mao Y., Chen J., Maynard J.A., Zhang B., Quiocho F.A.;
RT "A novel all helix fold of the AP180 amino-terminal domain for
RT phosphoinositide binding and clathrin assembly in synaptic vesicle
RT endocytosis.";
RL Cell 104:433-440(2001).
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. {ECO:0000269|PubMed:9883738}.
CC -!- SUBUNIT: Binds clathrin and phosphatidylinositol 4,5-bisphosphate.
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Membrane, clathrin-coated pit
CC {ECO:0000269|PubMed:9883738}. Golgi apparatus
CC {ECO:0000269|PubMed:9883738}. Cytoplasmic vesicle, clathrin-coated
CC vesicle {ECO:0000269|PubMed:9883738}. Note=Colocalized with clathrin in
CC the Golgi area.
CC -!- TISSUE SPECIFICITY: In embryos, expression is seen in central and
CC peripheral nervous systems (brain and ventral nerve cord) and Garland
CC cells. Coexpressed with clathrin at presynaptic boutons of
CC neuromuscular junctions. {ECO:0000269|PubMed:9883738}.
CC -!- SIMILARITY: Belongs to the PICALM/SNAP91 family. {ECO:0000305}.
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DR EMBL; AF075247; AAD08669.1; -; mRNA.
DR EMBL; AE014297; AAF54050.1; -; Genomic_DNA.
DR EMBL; AY128498; AAM75091.1; -; mRNA.
DR RefSeq; NP_524252.2; NM_079528.3.
DR PDB; 1HX8; X-ray; 2.20 A; A/B=1-299.
DR PDBsum; 1HX8; -.
DR AlphaFoldDB; Q9VI75; -.
DR SMR; Q9VI75; -.
DR BioGRID; 66058; 20.
DR ELM; Q9VI75; -.
DR IntAct; Q9VI75; 1.
DR STRING; 7227.FBpp0291394; -.
DR PaxDb; Q9VI75; -.
DR PRIDE; Q9VI75; -.
DR EnsemblMetazoa; FBtr0081572; FBpp0081091; FBgn0086372.
DR GeneID; 40863; -.
DR KEGG; dme:Dmel_CG2520; -.
DR CTD; 7939; -.
DR FlyBase; FBgn0086372; lap.
DR VEuPathDB; VectorBase:FBgn0086372; -.
DR eggNOG; KOG0251; Eukaryota.
DR GeneTree; ENSGT00950000183068; -.
DR HOGENOM; CLU_014080_1_1_1; -.
DR InParanoid; Q9VI75; -.
DR PhylomeDB; Q9VI75; -.
DR Reactome; R-DME-432722; Golgi Associated Vesicle Biogenesis.
DR Reactome; R-DME-8856825; Cargo recognition for clathrin-mediated endocytosis.
DR Reactome; R-DME-8856828; Clathrin-mediated endocytosis.
DR BioGRID-ORCS; 40863; 0 hits in 3 CRISPR screens.
DR EvolutionaryTrace; Q9VI75; -.
DR GenomeRNAi; 40863; -.
DR PRO; PR:Q9VI75; -.
DR Proteomes; UP000000803; Chromosome 3R.
DR Bgee; FBgn0086372; Expressed in brain and 27 other tissues.
DR ExpressionAtlas; Q9VI75; baseline and differential.
DR Genevisible; Q9VI75; DM.
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: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:UniProtKB.
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:0007268; P:chemical synaptic transmission; IMP:FlyBase.
DR GO; GO:0048268; P:clathrin coat assembly; IEA:InterPro.
DR GO; GO:0072583; P:clathrin-dependent endocytosis; IBA:GO_Central.
DR GO; GO:0150007; P:clathrin-dependent synaptic vesicle endocytosis; IMP:FlyBase.
DR GO; GO:0007270; P:neuron-neuron synaptic transmission; IMP:FlyBase.
DR GO; GO:0042331; P:phototaxis; IMP:FlyBase.
DR GO; GO:2000370; P:positive regulation of clathrin-dependent endocytosis; IMP:FlyBase.
DR GO; GO:0006898; P:receptor-mediated endocytosis; IDA:UniProtKB.
DR GO; GO:0016185; P:synaptic vesicle budding from presynaptic endocytic zone membrane; IBA:GO_Central.
DR GO; GO:0048489; P:synaptic vesicle transport; IMP:FlyBase.
DR GO; GO:0006900; P:vesicle budding from membrane; IBA:GO_Central.
DR DisProt; DP02763; -.
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 3D-structure; Coated pit; Cytoplasmic vesicle; Endocytosis;
KW Golgi apparatus; Membrane; Reference proteome.
FT CHAIN 1..468
FT /note="Phosphatidylinositol-binding clathrin assembly
FT protein LAP"
FT /id="PRO_0000187066"
FT DOMAIN 16..158
FT /note="ENTH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00243,
FT ECO:0000305"
FT REGION 438..468
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 51
FT /note="T -> A (in Ref. 1; AAD08669)"
FT /evidence="ECO:0000305"
FT CONFLICT 209
FT /note="M -> I (in Ref. 4; AAM75091)"
FT /evidence="ECO:0000305"
FT CONFLICT 372
FT /note="T -> A (in Ref. 1; AAD08669 and 4; AAM75091)"
FT /evidence="ECO:0000305"
FT HELIX 24..31
FT /evidence="ECO:0007829|PDB:1HX8"
FT STRAND 34..37
FT /evidence="ECO:0007829|PDB:1HX8"
FT HELIX 41..52
FT /evidence="ECO:0007829|PDB:1HX8"
FT HELIX 58..69
FT /evidence="ECO:0007829|PDB:1HX8"
FT HELIX 74..90
FT /evidence="ECO:0007829|PDB:1HX8"
FT HELIX 93..101
FT /evidence="ECO:0007829|PDB:1HX8"
FT HELIX 129..154
FT /evidence="ECO:0007829|PDB:1HX8"
FT HELIX 158..160
FT /evidence="ECO:0007829|PDB:1HX8"
FT TURN 170..172
FT /evidence="ECO:0007829|PDB:1HX8"
FT HELIX 175..193
FT /evidence="ECO:0007829|PDB:1HX8"
FT HELIX 199..201
FT /evidence="ECO:0007829|PDB:1HX8"
FT HELIX 205..236
FT /evidence="ECO:0007829|PDB:1HX8"
FT HELIX 242..270
FT /evidence="ECO:0007829|PDB:1HX8"
FT HELIX 275..277
FT /evidence="ECO:0007829|PDB:1HX8"
FT HELIX 286..297
FT /evidence="ECO:0007829|PDB:1HX8"
SQ SEQUENCE 468 AA; 49867 MW; 4B3011615AF007A0 CRC64;
MTMAGQTIND RLLAARHSLA GQGLAKSVCK ATTEECIGPK KKHLDYLVHC TNEPNVSIPH
LANLLIERSQ NANWVVVYKS LITTHHLMAY GNERFMQYLA SSNSTFNLSS FLDKGTVQDG
GMGVPGGRMG YDMSPFIRRY AKYLNEKSLS YRAMAFDFCK VKRGKEEGSL RSMNAEKLLK
TLPVLQAQLD ALLEFDCQSN DLSNGVINMS FMLLFRDLIR LFACYNDGII NLLEKYFDMN
KKHARDALDL YKKFLVRMDR VGEFLKVAEN VGIDKGDIPD LTKAPSSLLD ALEQHLATLE
GRKVSAANTP TQSSSSAFGT AAASSKFDTT NGIDEQLKAQ VLAEEEAAMN QYKSKVSSPT
SSGAAGASAA LTNPFLSSPP AAQAGQPIVD LFGAASAQPA AAAAATKASD DLLQLGNPFA
DMFDASGGGA AAVGATGNAG DGTAKYDGGA GSSPFDWGAT DDDGGAAQ
