PICAL_MOUSE
ID PICAL_MOUSE Reviewed; 660 AA.
AC Q7M6Y3; Q3TS04; Q811P1; Q8BUF6; Q8CIH8; Q8R0A9; Q8R3E1; Q8VDN5; Q921L0;
DT 01-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-2003, sequence version 1.
DT 03-AUG-2022, entry version 155.
DE RecName: Full=Phosphatidylinositol-binding clathrin assembly protein;
DE AltName: Full=Clathrin assembly lymphoid myeloid leukemia;
DE Short=CALM;
GN Name=Picalm; Synonyms=Calm, Fit1;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090 {ECO:0000312|EMBL:AAO17153.1};
RN [1] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, TISSUE SPECIFICITY, AND
RP DISRUPTION PHENOTYPE.
RC STRAIN=BALB/cRl {ECO:0000312|EMBL:AAO17153.1};
RC TISSUE=Liver {ECO:0000312|EMBL:AAO17153.1};
RX PubMed=12832620; DOI=10.1073/pnas.1432634100;
RA Klebig M.L., Wall M.D., Potter M.D., Rowe E.L., Carpenter D.A.,
RA Rinchik E.M.;
RT "Mutations in the clathrin-assembly gene Picalm are responsible for the
RT hematopoietic and iron metabolism abnormalities in fit1 mice.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:8360-8365(2003).
RN [2] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2; 3; 4; 5 AND 6).
RC STRAIN=Czech II, and FVB/N {ECO:0000312|EMBL:AAH57683.1};
RC TISSUE=Mammary tumor, and Retina;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 5), AND NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 143-660 (ISOFORM 2).
RC STRAIN=C57BL/6J; TISSUE=Epididymis, and Kidney;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [4] {ECO:0000305}
RP FUNCTION.
RX PubMed=9292517;
RA Potter M.D., Shinpock S.G., Popp R.A., Godfrey V., Carpenter D.A.,
RA Bernstein A., Johnson D.K., Rinchik E.M.;
RT "Mutations in the murine fitness 1 gene result in defective
RT hematopoiesis.";
RL Blood 90:1850-1857(1997).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [7]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=22363754; DOI=10.1371/journal.pone.0031854;
RA Suzuki M., Tanaka H., Tanimura A., Tanabe K., Oe N., Rai S., Kon S.,
RA Fukumoto M., Takei K., Abe T., Matsumura I., Kanakura Y., Watanabe T.;
RT "The clathrin assembly protein PICALM is required for erythroid maturation
RT and transferrin internalization in mice.";
RL PLoS ONE 7:E31854-E31854(2012).
CC -!- FUNCTION: Cytoplasmic adapter protein that plays a critical role in
CC clathrin-mediated endocytosis which is important in processes such as
CC internalization of cell receptors, synaptic transmission or removal of
CC apoptotic cells. Recruits AP-2 and attaches clathrin triskelions to the
CC cytoplasmic side of plasma membrane leading to clathrin-coated vesicles
CC (CCVs) assembly. Furthermore, regulates clathrin-coated vesicle size
CC and maturation by directly sensing and driving membrane curvature. In
CC addition to binding to clathrin, mediates the endocytosis of small R-
CC SNARES (Soluble NSF Attachment Protein REceptors) between plasma
CC membranes and endosomes including VAMP2, VAMP3, VAMP4, VAMP7 or VAMP8.
CC In turn, PICALM-dependent SNARE endocytosis is required for the
CC formation and maturation of autophagic precursors. Modulates thereby
CC autophagy and the turnover of autophagy substrates such as MAPT/TAU or
CC amyloid precursor protein cleaved C-terminal fragment (APP-CTF).
CC {ECO:0000250|UniProtKB:Q13492, ECO:0000269|PubMed:12832620,
CC ECO:0000269|PubMed:22363754}.
CC -!- SUBUNIT: Binds to clathrin; involves primarily the C-terminal
CC sequences, but the full-length protein is required for full binding
CC capacity. Binds phosphatidylinositol 4,5- bisphosphate. Interacts with
CC PIMREG; this interaction may change the subcellular location into the
CC nucleus. Interacts with AP2A1 (via its alpha-appendage domain).
CC Interacts (via N-terminus) with VAMP2; VAMP3; VAMP7 and VAMP8 (Via N-
CC terminus). Interacts with LC3/MAP1LC3A. {ECO:0000250|UniProtKB:Q13492}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q13492}.
CC Membrane, clathrin-coated pit {ECO:0000250|UniProtKB:Q13492}. Golgi
CC apparatus {ECO:0000250|UniProtKB:Q13492}. Cytoplasmic vesicle,
CC clathrin-coated vesicle {ECO:0000250|UniProtKB:Q13492}. Nucleus
CC {ECO:0000250|UniProtKB:Q13492}. Note=Colocalized with clathrin in the
CC Golgi area. Interaction with PIMREG may target PICALM to the nucleus in
CC some cells. {ECO:0000250|UniProtKB:Q13492}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=6;
CC Name=1 {ECO:0000305};
CC IsoId=Q7M6Y3-1; Sequence=Displayed;
CC Name=2 {ECO:0000305};
CC IsoId=Q7M6Y3-2; Sequence=VSP_050684, VSP_050685, VSP_050686;
CC Name=3 {ECO:0000305};
CC IsoId=Q7M6Y3-3; Sequence=VSP_050684, VSP_050685;
CC Name=4 {ECO:0000305};
CC IsoId=Q7M6Y3-4; Sequence=VSP_050684;
CC Name=5 {ECO:0000305};
CC IsoId=Q7M6Y3-5; Sequence=VSP_050685;
CC Name=6 {ECO:0000305};
CC IsoId=Q7M6Y3-6; Sequence=VSP_050686;
CC -!- TISSUE SPECIFICITY: Skins and livers of 1-week-old mice.
CC {ECO:0000269|PubMed:12832620}.
CC -!- DISRUPTION PHENOTYPE: PICALM-deficient mice suffer from severe anemia
CC due to ineffective erythropoiesis in the bone marrow. In addition, they
CC exhibit impaired clathrin-mediated internalization of transferrin
CC leading to iron metabolism abnormalities. {ECO:0000269|PubMed:12832620,
CC ECO:0000269|PubMed:22363754}.
CC -!- SIMILARITY: Belongs to the PICALM/SNAP91 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC39454.2; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AY206701; AAO17153.1; -; mRNA.
DR EMBL; BK001028; DAA01470.1; -; mRNA.
DR EMBL; BC011470; AAH11470.1; -; mRNA.
DR EMBL; BC021491; AAH21491.1; -; mRNA.
DR EMBL; BC023843; AAH23843.1; -; mRNA.
DR EMBL; BC025566; AAH25566.1; -; mRNA.
DR EMBL; BC027116; AAH27116.1; -; mRNA.
DR EMBL; BC057683; AAH57683.1; -; mRNA.
DR EMBL; AK085472; BAC39454.2; ALT_INIT; mRNA.
DR EMBL; AK162360; BAE36872.1; -; mRNA.
DR CCDS; CCDS52307.1; -. [Q7M6Y3-1]
DR CCDS; CCDS85334.1; -. [Q7M6Y3-6]
DR CCDS; CCDS85335.1; -. [Q7M6Y3-5]
DR CCDS; CCDS85336.1; -. [Q7M6Y3-4]
DR CCDS; CCDS85337.1; -. [Q7M6Y3-3]
DR CCDS; CCDS85338.1; -. [Q7M6Y3-2]
DR RefSeq; NP_001239449.1; NM_001252520.1. [Q7M6Y3-5]
DR RefSeq; NP_001239450.1; NM_001252521.1. [Q7M6Y3-6]
DR RefSeq; NP_001239451.1; NM_001252522.1. [Q7M6Y3-4]
DR RefSeq; NP_001239452.1; NM_001252523.1. [Q7M6Y3-3]
DR RefSeq; NP_001239453.1; NM_001252524.1. [Q7M6Y3-2]
DR RefSeq; NP_666306.2; NM_146194.4. [Q7M6Y3-1]
DR AlphaFoldDB; Q7M6Y3; -.
DR SMR; Q7M6Y3; -.
DR BioGRID; 231417; 10.
DR ELM; Q7M6Y3; -.
DR IntAct; Q7M6Y3; 2.
DR STRING; 10090.ENSMUSP00000051092; -.
DR iPTMnet; Q7M6Y3; -.
DR PhosphoSitePlus; Q7M6Y3; -.
DR SwissPalm; Q7M6Y3; -.
DR EPD; Q7M6Y3; -.
DR jPOST; Q7M6Y3; -.
DR MaxQB; Q7M6Y3; -.
DR PaxDb; Q7M6Y3; -.
DR PeptideAtlas; Q7M6Y3; -.
DR PRIDE; Q7M6Y3; -.
DR ProteomicsDB; 288151; -. [Q7M6Y3-1]
DR ProteomicsDB; 288152; -. [Q7M6Y3-2]
DR ProteomicsDB; 288153; -. [Q7M6Y3-3]
DR ProteomicsDB; 288154; -. [Q7M6Y3-4]
DR ProteomicsDB; 288155; -. [Q7M6Y3-5]
DR ProteomicsDB; 288156; -. [Q7M6Y3-6]
DR Antibodypedia; 17636; 214 antibodies from 34 providers.
DR DNASU; 233489; -.
DR Ensembl; ENSMUST00000049537; ENSMUSP00000051092; ENSMUSG00000039361. [Q7M6Y3-5]
DR Ensembl; ENSMUST00000207225; ENSMUSP00000146659; ENSMUSG00000039361. [Q7M6Y3-2]
DR Ensembl; ENSMUST00000207484; ENSMUSP00000146501; ENSMUSG00000039361. [Q7M6Y3-1]
DR Ensembl; ENSMUST00000208730; ENSMUSP00000146541; ENSMUSG00000039361. [Q7M6Y3-3]
DR Ensembl; ENSMUST00000208742; ENSMUSP00000147016; ENSMUSG00000039361. [Q7M6Y3-6]
DR Ensembl; ENSMUST00000209068; ENSMUSP00000146386; ENSMUSG00000039361. [Q7M6Y3-4]
DR GeneID; 233489; -.
DR KEGG; mmu:233489; -.
DR UCSC; uc009igq.2; mouse. [Q7M6Y3-1]
DR UCSC; uc009igr.2; mouse. [Q7M6Y3-5]
DR UCSC; uc009igs.2; mouse. [Q7M6Y3-6]
DR UCSC; uc009igt.2; mouse. [Q7M6Y3-4]
DR UCSC; uc009igu.2; mouse. [Q7M6Y3-3]
DR CTD; 8301; -.
DR MGI; MGI:2385902; Picalm.
DR VEuPathDB; HostDB:ENSMUSG00000039361; -.
DR eggNOG; KOG0251; Eukaryota.
DR GeneTree; ENSGT00950000183068; -.
DR HOGENOM; CLU_014080_0_0_1; -.
DR InParanoid; Q7M6Y3; -.
DR OMA; XPFSATV; -.
DR OrthoDB; 1592722at2759; -.
DR PhylomeDB; Q7M6Y3; -.
DR TreeFam; TF314861; -.
DR Reactome; R-MMU-432722; Golgi Associated Vesicle Biogenesis.
DR Reactome; R-MMU-8856825; Cargo recognition for clathrin-mediated endocytosis.
DR Reactome; R-MMU-8856828; Clathrin-mediated endocytosis.
DR Reactome; R-MMU-9696264; RND3 GTPase cycle.
DR BioGRID-ORCS; 233489; 9 hits in 77 CRISPR screens.
DR ChiTaRS; Picalm; mouse.
DR PRO; PR:Q7M6Y3; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; Q7M6Y3; protein.
DR Bgee; ENSMUSG00000039361; Expressed in humerus cartilage element and 243 other tissues.
DR ExpressionAtlas; Q7M6Y3; baseline and differential.
DR Genevisible; Q7M6Y3; MM.
DR GO; GO:0009986; C:cell surface; ISO:MGI.
DR GO; GO:0030132; C:clathrin coat of coated pit; ISO:MGI.
DR GO; GO:0005905; C:clathrin-coated pit; IDA:UniProtKB.
DR GO; GO:0030136; C:clathrin-coated vesicle; ISO:MGI.
DR GO; GO:0005769; C:early endosome; ISO:MGI.
DR GO; GO:0005768; C:endosome; ISO:MGI.
DR GO; GO:0070381; C:endosome to plasma membrane transport vesicle; ISO:MGI.
DR GO; GO:0098894; C:extrinsic component of presynaptic endocytic zone membrane; ISO:MGI.
DR GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-SubCell.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
DR GO; GO:0031224; C:intrinsic component of membrane; ISO:MGI.
DR GO; GO:0097418; C:neurofibrillary tangle; ISS:Alzheimers_University_of_Toronto.
DR GO; GO:0043005; C:neuron projection; ISO:MGI.
DR GO; GO:0043025; C:neuronal cell body; ISS:Alzheimers_University_of_Toronto.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
DR GO; GO:0098688; C:parallel fiber to Purkinje cell synapse; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0098794; C:postsynapse; ISO:MGI.
DR GO; GO:0014069; C:postsynaptic density; ISO:MGI.
DR GO; GO:0045211; C:postsynaptic membrane; ISO:MGI.
DR GO; GO:0042734; C:presynaptic membrane; ISO:MGI.
DR GO; GO:0098685; C:Schaffer collateral - CA1 synapse; ISO:MGI.
DR GO; GO:0045202; C:synapse; ISO:MGI.
DR GO; GO:0008021; C:synaptic vesicle; ISO:MGI.
DR GO; GO:0031982; C:vesicle; IDA:Alzheimers_University_of_Toronto.
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; ISO:MGI.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0050750; F:low-density lipoprotein particle receptor binding; ISO:MGI.
DR GO; GO:0005546; F:phosphatidylinositol-4,5-bisphosphate binding; ISO:MGI.
DR GO; GO:0017124; F:SH3 domain binding; ISO:MGI.
DR GO; GO:0031267; F:small GTPase binding; ISO:MGI.
DR GO; GO:0000149; F:SNARE binding; ISO:MGI.
DR GO; GO:0048156; F:tau protein binding; ISO:MGI.
DR GO; GO:0150093; P:amyloid-beta clearance by transcytosis; IMP:ARUK-UCL.
DR GO; GO:0007409; P:axonogenesis; IMP:BHF-UCL.
DR GO; GO:0048268; P:clathrin coat assembly; ISO:MGI.
DR GO; GO:1905224; P:clathrin-coated pit assembly; ISO:MGI.
DR GO; GO:0072583; P:clathrin-dependent endocytosis; IMP:Alzheimers_University_of_Toronto.
DR GO; GO:0048813; P:dendrite morphogenesis; IMP:BHF-UCL.
DR GO; GO:0006897; P:endocytosis; ISO:MGI.
DR GO; GO:0016197; P:endosomal transport; ISO:MGI.
DR GO; GO:0030097; P:hemopoiesis; IMP:UniProtKB.
DR GO; GO:0055072; P:iron ion homeostasis; ISS:Alzheimers_University_of_Toronto.
DR GO; GO:0007611; P:learning or memory; IGI:ARUK-UCL.
DR GO; GO:0097753; P:membrane bending; ISO:MGI.
DR GO; GO:0010629; P:negative regulation of gene expression; ISS:Alzheimers_University_of_Toronto.
DR GO; GO:1902963; P:negative regulation of metalloendopeptidase activity involved in amyloid precursor protein catabolic process; IMP:Alzheimers_University_of_Toronto.
DR GO; GO:2000009; P:negative regulation of protein localization to cell surface; ISO:MGI.
DR GO; GO:1903077; P:negative regulation of protein localization to plasma membrane; ISO:MGI.
DR GO; GO:0048261; P:negative regulation of receptor-mediated endocytosis; ISO:MGI.
DR GO; GO:1902004; P:positive regulation of amyloid-beta formation; IMP:Alzheimers_University_of_Toronto.
DR GO; GO:1902961; P:positive regulation of aspartic-type endopeptidase activity involved in amyloid precursor protein catabolic process; IMP:Alzheimers_University_of_Toronto.
DR GO; GO:0050772; P:positive regulation of axonogenesis; ISO:MGI.
DR GO; GO:1903861; P:positive regulation of dendrite extension; ISO:MGI.
DR GO; GO:0043547; P:positive regulation of GTPase activity; ISO:MGI.
DR GO; GO:1901216; P:positive regulation of neuron death; ISS:Alzheimers_University_of_Toronto.
DR GO; GO:2000809; P:positive regulation of synaptic vesicle clustering; ISO:MGI.
DR GO; GO:1900244; P:positive regulation of synaptic vesicle endocytosis; ISO:MGI.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; ISO:MGI.
DR GO; GO:0031623; P:receptor internalization; ISO:MGI.
DR GO; GO:0006898; P:receptor-mediated endocytosis; IDA:UniProtKB.
DR GO; GO:1902959; P:regulation of aspartic-type endopeptidase activity involved in amyloid precursor protein catabolic process; ISS:Alzheimers_University_of_Toronto.
DR GO; GO:2000369; P:regulation of clathrin-dependent endocytosis; IEA:InterPro.
DR GO; GO:0030100; P:regulation of endocytosis; ISO:MGI.
DR GO; GO:0032880; P:regulation of protein localization; ISO:MGI.
DR GO; GO:0051223; P:regulation of protein transport; ISO:MGI.
DR GO; GO:1900242; P:regulation of synaptic vesicle endocytosis; ISO:MGI.
DR GO; GO:1902803; P:regulation of synaptic vesicle transport; ISO:MGI.
DR GO; GO:2000331; P:regulation of terminal button organization; ISO:MGI.
DR GO; GO:0097494; P:regulation of vesicle size; ISO:MGI.
DR GO; GO:0016185; P:synaptic vesicle budding from presynaptic endocytic zone membrane; IBA:GO_Central.
DR GO; GO:0048488; P:synaptic vesicle endocytosis; ISO:MGI.
DR GO; GO:0016188; P:synaptic vesicle maturation; IMP:Alzheimers_University_of_Toronto.
DR GO; GO:0006900; P:vesicle budding from membrane; ISO:MGI.
DR GO; GO:0035459; P:vesicle cargo loading; IMP:Alzheimers_University_of_Toronto.
DR GO; GO:0016192; P:vesicle-mediated transport; ISO:MGI.
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 InterPro; IPR030412; PICALM.
DR PANTHER; PTHR22951; PTHR22951; 1.
DR PANTHER; PTHR22951:SF16; PTHR22951:SF16; 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 Acetylation; Alternative splicing; Cell membrane; Coated pit;
KW Cytoplasmic vesicle; Developmental protein; Endocytosis; Golgi apparatus;
KW Isopeptide bond; Membrane; Nucleus; Phosphoprotein; Reference proteome;
KW Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q13492"
FT CHAIN 2..660
FT /note="Phosphatidylinositol-binding clathrin assembly
FT protein"
FT /id="PRO_0000187063"
FT DOMAIN 14..145
FT /note="ENTH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00243,
FT ECO:0000305"
FT REGION 221..294
FT /note="Interaction with PIMREG"
FT /evidence="ECO:0000250"
FT REGION 556..580
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000250|UniProtKB:Q13492"
FT MOD_RES 16
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q13492"
FT MOD_RES 20
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q13492"
FT MOD_RES 303
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q13492"
FT MOD_RES 315
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q13492"
FT CROSSLNK 238
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q13492"
FT VAR_SEQ 420..469
FT /note="Missing (in isoform 2, isoform 3 and isoform 4)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:16141072"
FT /id="VSP_050684"
FT VAR_SEQ 506..510
FT /note="Missing (in isoform 2, isoform 3 and isoform 5)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:16141072"
FT /id="VSP_050685"
FT VAR_SEQ 594..601
FT /note="Missing (in isoform 2 and isoform 6)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:16141072"
FT /id="VSP_050686"
FT CONFLICT 522
FT /note="N -> S (in Ref. 2; AAH21491/AAH23843/AAH25566/
FT AAH57683)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 660 AA; 71543 MW; 7FB206508281BCDF CRC64;
MSGQSLTDRI TAAQHSVTGS AVSKTVCKAT THEIMGPKKK HLDYLIQCTN EMNVNIPQLA
DSLFERTTNS SWVVVFKSLI TTHHLMVYGN ERFIQYLASR NTLFNLSNFL DKSGLQGYDM
STFIRRYSRY LNEKAVSYRQ VAFDFTKVKR GADGVMRTMN TEKLLKTVPI IQNQMDALLD
FNVNSNELTN GVINAAFMLL FKDAIRLFAA YNEGIINLLE KYFDMKKNQC KEGLDIYKKF
LTRMTRISEF LKVAEQVGID RGDIPDLSQA PSSLLDALEQ HLASLEGKKI KDSTAASRAT
TLSNAVSSLA STGLSLTKVD EREKQAALEE EQARLKALKE QRLKELAKKP HTSLTTAASP
VSTSAGGIMT APAIDIFSTP SSSNSTSKLP NDLLDLQQPT FHPSVHAMSA APQGASTWGD
PFSATLDAVE DAIPSLNPFL TKSSGDVHLP IASDVSTFTT RTPTHEMFVG FSPSPVAQPH
SSAGLNVDFE SVFGNKSTNV AVDSGGFDEL GGLLKPTVAS QNQSLPVAKL PPNKLVSDDL
DSSLANLVGN LGIGNGTTKN DVSWSQPGEK KLTGGSNWQP KVAPTTAWSA ATMNGMHFPQ
YAPPVMAYPA TTPTGMIGYG IPPQMGSVPV MTQPTLIYSQ PVMRPPNPFG PVSGAQIQFM
