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Phosphatidylinositol-binding clathrin assembly protein (Clathrin assembly lymphoid myeloid leukemia protein) (rCALM)

 PICAL_RAT               Reviewed;         640 AA.
O55012; O55011;
01-MAR-2004, integrated into UniProtKB/Swiss-Prot.
01-JUN-1998, sequence version 1.
22-NOV-2017, entry version 126.
RecName: Full=Phosphatidylinositol-binding clathrin assembly protein;
AltName: Full=Clathrin assembly lymphoid myeloid leukemia protein;
Short=rCALM;
Name=Picalm; Synonyms=Calm;
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116 {ECO:0000312|EMBL:AAB97079.1};
[1] {ECO:0000305}
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), AND TISSUE SPECIFICITY.
STRAIN=Sprague-Dawley {ECO:0000312|EMBL:AAB97079.1};
TISSUE=Brain {ECO:0000312|EMBL:AAB97079.1};
PubMed=10630373; DOI=10.1038/emm.1999.31;
Kim H.-L., Lee S.C.;
"Molecular cloning of clathrin assembly protein gene (rCALM) and its
differential expression to AP180 in rat brain.";
Exp. Mol. Med. 31:191-196(1999).
[2] {ECO:0000305}
X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 19-281.
PubMed=11161218; DOI=10.1126/science.291.5506.1051;
Ford M.G., Pearse B.M., Higgins M.K., Vallis Y., Owen D.J., Gibson A.,
Hopkins C.R., Evans P.R., McMahon H.T.;
"Simultaneous binding of PtdIns(4,5)P2 and clathrin by AP180 in the
nucleation of clathrin lattices on membranes.";
Science 291:1051-1055(2001).
-!- FUNCTION: Assembly protein recruiting clathrin and adapter protein
complex 2 (AP2) to cell membranes at sites of coated-pit formation
and clathrin-vesicle assembly. May be required to determine the
amount of membrane to be recycled, possibly by regulating the size
of the clathrin cage. Involved in AP2-dependent clathrin-mediated
endocytosis at the neuromuscular junction.
{ECO:0000250|UniProtKB:Q13492}.
-!- SUBUNIT: Binds clathrin; involves primarily the C-terminal
sequences, but the full-length protein is required for full
binding capacity. Binds phosphatidylinositol 4,5- bisphosphate.
Interacts with PIMREG; this interaction may change the subcellular
location into the nucleus. {ECO:0000250|UniProtKB:Q13492}.
-!- INTERACTION:
Self; NbExp=3; IntAct=EBI-915601, EBI-915601;
P63027:VAMP2 (xeno); NbExp=2; IntAct=EBI-915601, EBI-520113;
Q15836:VAMP3 (xeno); NbExp=2; IntAct=EBI-915601, EBI-722343;
O70404:Vamp8 (xeno); NbExp=4; IntAct=EBI-915601, EBI-1812572;
-!- SUBCELLULAR LOCATION: Membrane, clathrin-coated pit
{ECO:0000250|UniProtKB:Q13492}. Golgi apparatus
{ECO:0000250|UniProtKB:Q13492}. Cytoplasmic vesicle, clathrin-
coated vesicle {ECO:0000250|UniProtKB:Q13492}. Nucleus
{ECO:0000250|UniProtKB:Q13492}. Note=Colocalized with clathrin in
the Golgi area. Interaction with PIMREG may target PICALM to the
nucleus in some cells. {ECO:0000250|UniProtKB:Q13492}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1 {ECO:0000269|PubMed:10630373}; Synonyms=Long
{ECO:0000269|PubMed:10630373};
IsoId=O55012-1; Sequence=Displayed;
Name=2 {ECO:0000269|PubMed:10630373}; Synonyms=Short
{ECO:0000269|PubMed:10630373};
IsoId=O55012-2; Sequence=VSP_050687;
-!- TISSUE SPECIFICITY: Isoform 2 was found in most tissues examined.
Isoform 1 has an overlapping expression pattern but is absent from
lung, heart and pancreas. Both isoforms are widely expressed in
the brain, higher levels are seen in hippocampus, dentate gyrus,
medial habenula nucleus and cerebellar granule cells.
{ECO:0000269|PubMed:10630373}.
-!- SIMILARITY: Belongs to the PICALM/SNAP91 family. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; AF041373; AAB97078.1; -; mRNA.
EMBL; AF041374; AAB97079.1; -; mRNA.
RefSeq; NP_446006.1; NM_053554.2. [O55012-1]
UniGene; Rn.24871; -.
PDB; 1HF8; X-ray; 2.00 A; A=1-289.
PDB; 1HFA; X-ray; 2.00 A; A=1-289.
PDB; 1HG2; X-ray; 2.00 A; A=1-289.
PDB; 1HG5; X-ray; 2.00 A; A=1-289.
PDB; 3ZYK; X-ray; 1.80 A; A/B=1-289.
PDB; 3ZYL; X-ray; 1.70 A; A/B=1-264.
PDB; 3ZYM; X-ray; 2.03 A; A/B/C=1-264.
PDBsum; 1HF8; -.
PDBsum; 1HFA; -.
PDBsum; 1HG2; -.
PDBsum; 1HG5; -.
PDBsum; 3ZYK; -.
PDBsum; 3ZYL; -.
PDBsum; 3ZYM; -.
ProteinModelPortal; O55012; -.
SMR; O55012; -.
BioGrid; 250139; 1.
ELM; O55012; -.
IntAct; O55012; 4.
MINT; MINT-4575979; -.
iPTMnet; O55012; -.
PhosphoSitePlus; O55012; -.
PeptideAtlas; O55012; -.
PRIDE; O55012; -.
GeneID; 89816; -.
KEGG; rno:89816; -.
UCSC; RGD:621054; rat. [O55012-1]
CTD; 8301; -.
RGD; 621054; Picalm.
HOVERGEN; HBG049391; -.
InParanoid; O55012; -.
KO; K20044; -.
PhylomeDB; O55012; -.
EvolutionaryTrace; O55012; -.
PRO; PR:O55012; -.
Proteomes; UP000002494; Unplaced.
GO; GO:0009986; C:cell surface; ISO:RGD.
GO; GO:0005905; C:clathrin-coated pit; ISS:UniProtKB.
GO; GO:0030136; C:clathrin-coated vesicle; IDA:BHF-UCL.
GO; GO:0005769; C:early endosome; ISO:RGD.
GO; GO:0005768; C:endosome; IDA:BHF-UCL.
GO; GO:0070381; C:endosome to plasma membrane transport vesicle; ISO:RGD.
GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-SubCell.
GO; GO:0005622; C:intracellular; ISO:RGD.
GO; GO:0031224; C:intrinsic component of membrane; IMP:ARUK-UCL.
GO; GO:0016020; C:membrane; ISO:RGD.
GO; GO:0097418; C:neurofibrillary tangle; ISS:Alzheimers_University_of_Toronto.
GO; GO:0043025; C:neuronal cell body; ISS:Alzheimers_University_of_Toronto.
GO; GO:0005634; C:nucleus; ISO:RGD.
GO; GO:0005886; C:plasma membrane; IDA:BHF-UCL.
GO; GO:0014069; C:postsynaptic density; IDA:BHF-UCL.
GO; GO:0045211; C:postsynaptic membrane; IDA:BHF-UCL.
GO; GO:0042734; C:presynaptic membrane; IDA:BHF-UCL.
GO; GO:0045202; C:synapse; IDA:RGD.
GO; GO:0008021; C:synaptic vesicle; IDA:BHF-UCL.
GO; GO:0031982; C:vesicle; ISS:Alzheimers_University_of_Toronto.
GO; GO:0005545; F:1-phosphatidylinositol binding; IDA:UniProtKB.
GO; GO:0045296; F:cadherin binding; ISO:RGD.
GO; GO:0035615; F:clathrin adaptor activity; ISS:Alzheimers_University_of_Toronto.
GO; GO:0030276; F:clathrin binding; IDA:UniProtKB.
GO; GO:0032050; F:clathrin heavy chain binding; ISO:RGD.
GO; GO:0042802; F:identical protein binding; IPI:IntAct.
GO; GO:0050750; F:low-density lipoprotein particle receptor binding; ISO:RGD.
GO; GO:0005546; F:phosphatidylinositol-4,5-bisphosphate binding; IMP:ARUK-UCL.
GO; GO:0017137; F:Rab GTPase binding; ISO:RGD.
GO; GO:0017124; F:SH3 domain binding; IDA:RGD.
GO; GO:0007409; P:axonogenesis; IMP:BHF-UCL.
GO; GO:0035459; P:cargo loading into vesicle; ISS:Alzheimers_University_of_Toronto.
GO; GO:0008283; P:cell proliferation; ISS:Alzheimers_University_of_Toronto.
GO; GO:0048268; P:clathrin coat assembly; IDA:RGD.
GO; GO:0072583; P:clathrin-dependent endocytosis; ISS:Alzheimers_University_of_Toronto.
GO; GO:0048813; P:dendrite morphogenesis; IMP:BHF-UCL.
GO; GO:0016197; P:endosomal transport; ISO:RGD.
GO; GO:0030097; P:hemopoiesis; ISO:RGD.
GO; GO:0055072; P:iron ion homeostasis; ISS:Alzheimers_University_of_Toronto.
GO; GO:0098711; P:iron ion import across plasma membrane; ISS:Alzheimers_University_of_Toronto.
GO; GO:0007611; P:learning or memory; ISO:RGD.
GO; GO:0097753; P:membrane bending; ISO:RGD.
GO; GO:0090647; P:modulation of age-related behavioral decline; ISO:RGD.
GO; GO:0010629; P:negative regulation of gene expression; ISS:Alzheimers_University_of_Toronto.
GO; GO:1902963; P:negative regulation of metalloendopeptidase activity involved in amyloid precursor protein catabolic process; ISS:Alzheimers_University_of_Toronto.
GO; GO:2000009; P:negative regulation of protein localization to cell surface; ISO:RGD.
GO; GO:1903077; P:negative regulation of protein localization to plasma membrane; ISO:RGD.
GO; GO:0048261; P:negative regulation of receptor-mediated endocytosis; ISO:RGD.
GO; GO:1900223; P:positive regulation of amyloid-beta clearance; ISO:RGD.
GO; GO:1902004; P:positive regulation of amyloid-beta formation; ISS:Alzheimers_University_of_Toronto.
GO; GO:1902961; P:positive regulation of aspartic-type endopeptidase activity involved in amyloid precursor protein catabolic process; ISS:Alzheimers_University_of_Toronto.
GO; GO:0043547; P:positive regulation of GTPase activity; ISO:RGD.
GO; GO:1901216; P:positive regulation of neuron death; ISS:Alzheimers_University_of_Toronto.
GO; GO:0045893; P:positive regulation of transcription, DNA-templated; ISO:RGD.
GO; GO:0031623; P:receptor internalization; ISO:RGD.
GO; GO:0006898; P:receptor-mediated endocytosis; ISS:UniProtKB.
GO; GO:1902959; P:regulation of aspartic-type endopeptidase activity involved in amyloid precursor protein catabolic process; ISS:Alzheimers_University_of_Toronto.
GO; GO:0030100; P:regulation of endocytosis; IMP:BHF-UCL.
GO; GO:0032880; P:regulation of protein localization; ISO:RGD.
GO; GO:0051223; P:regulation of protein transport; IMP:BHF-UCL.
GO; GO:0097494; P:regulation of vesicle size; ISO:RGD.
GO; GO:0016188; P:synaptic vesicle maturation; ISS:Alzheimers_University_of_Toronto.
GO; GO:0045056; P:transcytosis; ISO:RGD.
GO; GO:0016050; P:vesicle organization; ISO:RGD.
GO; GO:0016192; P:vesicle-mediated transport; IMP:BHF-UCL.
Gene3D; 1.20.58.150; -; 1.
Gene3D; 1.25.40.90; -; 1.
InterPro; IPR011417; ANTH_dom.
InterPro; IPR014712; Clathrin_AP_dom2.
InterPro; IPR013809; ENTH.
InterPro; IPR008942; ENTH_VHS.
InterPro; IPR030412; PICALM.
PANTHER; PTHR22951:SF16; PTHR22951:SF16; 1.
Pfam; PF07651; ANTH; 1.
SMART; SM00273; ENTH; 1.
SUPFAM; SSF48464; SSF48464; 1.
PROSITE; PS50942; ENTH; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Alternative splicing; Coated pit;
Complete proteome; Cytoplasmic vesicle; Endocytosis; Golgi apparatus;
Isopeptide bond; Membrane; Nucleus; Phosphoprotein;
Reference proteome; Ubl conjugation.
INIT_MET 1 1 Removed. {ECO:0000250|UniProtKB:Q13492}.
CHAIN 2 640 Phosphatidylinositol-binding clathrin
assembly protein.
/FTId=PRO_0000187064.
DOMAIN 14 145 ENTH. {ECO:0000255|PROSITE-
ProRule:PRU00243, ECO:0000305}.
REGION 221 294 Interaction with PIMREG. {ECO:0000250}.
MOD_RES 2 2 N-acetylserine.
{ECO:0000250|UniProtKB:Q13492}.
MOD_RES 16 16 Phosphoserine.
{ECO:0000250|UniProtKB:Q13492}.
MOD_RES 20 20 Phosphoserine.
{ECO:0000250|UniProtKB:Q13492}.
MOD_RES 303 303 Phosphoserine.
{ECO:0000250|UniProtKB:Q13492}.
MOD_RES 315 315 Phosphoserine.
{ECO:0000250|UniProtKB:Q13492}.
CROSSLNK 238 238 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:Q13492}.
VAR_SEQ 420 462 Missing (in isoform 2).
{ECO:0000303|PubMed:10630373}.
/FTId=VSP_050687.
HELIX 6 29 {ECO:0000244|PDB:3ZYL}.
STRAND 32 35 {ECO:0000244|PDB:3ZYL}.
HELIX 39 50 {ECO:0000244|PDB:3ZYL}.
HELIX 56 66 {ECO:0000244|PDB:3ZYL}.
HELIX 72 88 {ECO:0000244|PDB:3ZYL}.
HELIX 91 99 {ECO:0000244|PDB:3ZYL}.
HELIX 115 141 {ECO:0000244|PDB:3ZYL}.
TURN 145 147 {ECO:0000244|PDB:3ZYL}.
STRAND 151 154 {ECO:0000244|PDB:1HF8}.
HELIX 155 158 {ECO:0000244|PDB:3ZYL}.
HELIX 161 179 {ECO:0000244|PDB:3ZYL}.
HELIX 185 187 {ECO:0000244|PDB:3ZYL}.
HELIX 191 220 {ECO:0000244|PDB:3ZYL}.
HELIX 222 224 {ECO:0000244|PDB:3ZYL}.
HELIX 227 256 {ECO:0000244|PDB:3ZYL}.
HELIX 261 263 {ECO:0000244|PDB:3ZYL}.
HELIX 267 269 {ECO:0000244|PDB:3ZYK}.
HELIX 275 285 {ECO:0000244|PDB:3ZYK}.
SEQUENCE 640 AA; 69286 MW; 7395A92C285FA10A 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 APQVASTWGD
AVDDAIPSLN PFLTKSSGDV HLPISSDVST FTTRTPTHEM FVGFSPSPVT QPHPSAGLNV
DFESVFGNKS TNVAVDSGGG LLKPTVASQN QSLPVAKLPP NKLVSDDLDS SLANLVGNLG
IGNGTTKNDV SCSQPGEKKL TGGSNWQPKV APTTAWSAAT MAPPVMAYPA TTPTGMIGYG
IPPQMGSVPV MTQPTLIYSQ PVMRPPNPFG PVPGAQIQFM


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