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   24-JAN-2024, entry version 163.
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,
RC   Pancreas, 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; 12.
DR   ELM; Q7M6Y3; -.
DR   IntAct; Q7M6Y3; 2.
DR   STRING; 10090.ENSMUSP00000146501; -.
DR   GlyGen; Q7M6Y3; 15 sites, 1 O-linked glycan (15 sites).
DR   iPTMnet; Q7M6Y3; -.
DR   MetOSite; Q7M6Y3; -.
DR   PhosphoSitePlus; Q7M6Y3; -.
DR   SwissPalm; Q7M6Y3; -.
DR   EPD; Q7M6Y3; -.
DR   jPOST; Q7M6Y3; -.
DR   MaxQB; Q7M6Y3; -.
DR   PaxDb; 10090-ENSMUSP00000051092; -.
DR   PeptideAtlas; 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   Pumba; Q7M6Y3; -.
DR   Antibodypedia; 17636; 239 antibodies from 34 providers.
DR   DNASU; 233489; -.
DR   Ensembl; ENSMUST00000049537.9; ENSMUSP00000051092.9; ENSMUSG00000039361.12. [Q7M6Y3-5]
DR   Ensembl; ENSMUST00000207225.2; ENSMUSP00000146659.2; ENSMUSG00000039361.12. [Q7M6Y3-2]
DR   Ensembl; ENSMUST00000207484.2; ENSMUSP00000146501.2; ENSMUSG00000039361.12. [Q7M6Y3-1]
DR   Ensembl; ENSMUST00000208730.2; ENSMUSP00000146541.2; ENSMUSG00000039361.12. [Q7M6Y3-3]
DR   Ensembl; ENSMUST00000208742.2; ENSMUSP00000147016.2; ENSMUSG00000039361.12. [Q7M6Y3-6]
DR   Ensembl; ENSMUST00000209068.2; ENSMUSP00000146386.2; ENSMUSG00000039361.12. [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   AGR; MGI:2385902; -.
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; 3667239at2759; -.
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 82 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 246 other cell types or tissues.
DR   ExpressionAtlas; Q7M6Y3; baseline and differential.
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:0016020; C:membrane; ISO:MGI.
DR   GO; GO:0097418; C:neurofibrillary tangle; ISS:Alzheimers_University_of_Toronto.
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: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: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:0006879; P:intracellular iron ion homeostasis; ISO:MGI.
DR   GO; GO:0007611; P:learning or memory; IGI:ARUK-UCL.
DR   GO; GO:0097753; P:membrane bending; ISO:MGI.
DR   GO; GO:0060586; P:multicellular organismal-level iron ion homeostasis; ISS:Alzheimers_University_of_Toronto.
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:0045893; P:positive regulation of DNA-templated transcription; ISO:MGI.
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: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: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   CDD; cd16985; ANTH_N_AP180; 1.
DR   Gene3D; 1.25.40.90; -; 1.
DR   Gene3D; 1.20.58.150; ANTH domain; 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; CLATHRIN ASSEMBLY PROTEIN; 1.
DR   PANTHER; PTHR22951:SF16; PHOSPHATIDYLINOSITOL-BINDING CLATHRIN ASSEMBLY PROTEIN; 1.
DR   Pfam; PF07651; ANTH; 1.
DR   SMART; SM00273; ENTH; 1.
DR   SUPFAM; SSF48464; ENTH/VHS domain; 1.
DR   SUPFAM; SSF89009; GAT-like domain; 1.
DR   PROSITE; PS50942; ENTH; 1.
DR   Genevisible; Q7M6Y3; MM.
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;
FT                   AAH21491/AAH23843/AAH25566/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
//