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O55012 (PICA_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified May 29, 2013. Version 89. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Phosphatidylinositol-binding clathrin assembly protein
Alternative name(s):
Clathrin assembly lymphoid myeloid leukemia protein
Short name=rCALM
Gene names
Name:Picalm
Synonyms:Calm
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus

Protein attributes

Sequence length640 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Assembly protein recruiting clathrin and adaptor 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 By similarity. UniProtKB Q13492

Subunit structure

Binds clathrin and phosphatidylinositol 4,5-bisphosphate.

Subcellular location

Membrane › clathrin-coated pit By similarity. Golgi apparatus By similarity. Cytoplasmic vesicle › clathrin-coated vesicle By similarity. Note: Colocalized with clathrin in the Golgi area By similarity.

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. Ref.1

Sequence similarities

Contains 1 ENTH (epsin N-terminal homology) domain.

Ontologies

Keywords
   Biological processEndocytosis
   Cellular componentCoated pit
Cytoplasmic vesicle
Golgi apparatus
Membrane
   Coding sequence diversityAlternative splicing
   PTMPhosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processaxonogenesis

Inferred from mutant phenotype PubMed 18842885. Source: BHF-UCL

clathrin coat assembly

Inferred from direct assay PubMed 11190274. Source: RGD

dendrite morphogenesis

Inferred from mutant phenotype PubMed 18842885. Source: BHF-UCL

receptor-mediated endocytosis

Inferred from sequence or structural similarity. Source: UniProtKB

regulation of endocytosis

Inferred from mutant phenotype PubMed 18842885. Source: BHF-UCL

regulation of protein transport

Inferred from mutant phenotype PubMed 18842885. Source: BHF-UCL

   Cellular_componentGolgi apparatus

Inferred from electronic annotation. Source: UniProtKB-SubCell

clathrin coat

Inferred from electronic annotation. Source: InterPro

coated pit

Inferred from sequence or structural similarity. Source: UniProtKB

endosome

Inferred from direct assay PubMed 18842885. Source: BHF-UCL

plasma membrane

Inferred from direct assay PubMed 18842885. Source: BHF-UCL

postsynaptic density

Inferred from direct assay PubMed 17640037. Source: BHF-UCL

postsynaptic membrane

Inferred from direct assay PubMed 15558718PubMed 17640037. Source: BHF-UCL

presynaptic membrane

Inferred from direct assay PubMed 15558718PubMed 17640037. Source: BHF-UCL

synaptic vesicle

Inferred from direct assay PubMed 17640037. Source: BHF-UCL

   Molecular_function1-phosphatidylinositol binding

Inferred from direct assay Ref.2. Source: UniProtKB

SH3 domain binding

Inferred from direct assay PubMed 10926122. Source: RGD

clathrin binding

Inferred from direct assay Ref.2. Source: UniProtKB

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

itself3EBI-915601,EBI-915601
VAMP2P630272EBI-915601,EBI-520113From a different organism.
VAMP3Q158362EBI-915601,EBI-722343From a different organism.
Vamp8O704044EBI-915601,EBI-1812572From a different organism.

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 Ref.1 (identifier: O55012-1)

Also known as: Long;

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 Ref.1 (identifier: O55012-2)

Also known as: Short;

The sequence of this isoform differs from the canonical sequence as follows:
     420-462: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 640640Phosphatidylinositol-binding clathrin assembly protein
PRO_0000187064

Regions

Domain14 – 145132ENTH

Amino acid modifications

Modified residue4361Phosphoserine By similarity

Natural variations

Alternative sequence420 – 46243Missing in isoform 2. Ref.1
VSP_050687

Secondary structure

1 .................................... 640
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 (Long) [UniParc].

Last modified June 1, 1998. Version 1.
Checksum: 7395A92C285FA10A

FASTA64069,286
        10         20         30         40         50         60 
MSGQSLTDRI TAAQHSVTGS AVSKTVCKAT THEIMGPKKK HLDYLIQCTN EMNVNIPQLA 

        70         80         90        100        110        120 
DSLFERTTNS SWVVVFKSLI TTHHLMVYGN ERFIQYLASR NTLFNLSNFL DKSGLQGYDM 

       130        140        150        160        170        180 
STFIRRYSRY LNEKAVSYRQ VAFDFTKVKR GADGVMRTMN TEKLLKTVPI IQNQMDALLD 

       190        200        210        220        230        240 
FNVNSNELTN GVINAAFMLL FKDAIRLFAA YNEGIINLLE KYFDMKKNQC KEGLDIYKKF 

       250        260        270        280        290        300 
LTRMTRISEF LKVAEQVGID RGDIPDLSQA PSSLLDALEQ HLASLEGKKI KDSTAASRAT 

       310        320        330        340        350        360 
TLSNAVSSLA STGLSLTKVD EREKQAALEE EQARLKALKE QRLKELAKKP HTSLTTAASP 

       370        380        390        400        410        420 
VSTSAGGIMT APAIDIFSTP SSSNSTSKLP NDLLDLQQPT FHPSVHAMSA APQVASTWGD 

       430        440        450        460        470        480 
AVDDAIPSLN PFLTKSSGDV HLPISSDVST FTTRTPTHEM FVGFSPSPVT QPHPSAGLNV 

       490        500        510        520        530        540 
DFESVFGNKS TNVAVDSGGG LLKPTVASQN QSLPVAKLPP NKLVSDDLDS SLANLVGNLG 

       550        560        570        580        590        600 
IGNGTTKNDV SCSQPGEKKL TGGSNWQPKV APTTAWSAAT MAPPVMAYPA TTPTGMIGYG 

       610        620        630        640 
IPPQMGSVPV MTQPTLIYSQ PVMRPPNPFG PVPGAQIQFM

« Hide

Isoform 2 (Short) [UniParc].

Checksum: 42CA941426B9E6A4
Show »

FASTA59764,657

References

[1]"Molecular cloning of clathrin assembly protein gene (rCALM) and its differential expression to AP180 in rat brain."
Kim H.-L., Lee S.C.
Exp. Mol. Med. 31:191-196(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), TISSUE SPECIFICITY.
Strain: Sprague-Dawley.
Tissue: Brain.
[2]"Simultaneous binding of PtdIns(4,5)P2 and clathrin by AP180 in the nucleation of clathrin lattices on membranes."
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.
Science 291:1051-1055(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 19-281.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AF041373 mRNA. Translation: AAB97078.1.
AF041374 mRNA. Translation: AAB97079.1.
IPIIPI00194958.
IPI00194959.
RefSeqNP_446006.1. NM_053554.2.
UniGeneRn.24871.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1HF8X-ray2.00A1-289[»]
1HFAX-ray2.00A1-289[»]
1HG2X-ray2.00A1-289[»]
1HG5X-ray2.00A1-289[»]
3ZYKX-ray1.80A/B1-289[»]
3ZYLX-ray1.70A/B1-264[»]
3ZYMX-ray2.03A/B/C1-264[»]
ProteinModelPortalO55012.
SMRO55012. Positions 19-281.
ModBaseSearch...

Protein-protein interaction databases

IntActO55012. 4 interactions.
MINTMINT-4575979.

PTM databases

PhosphoSiteO55012.

Proteomic databases

PaxDbO55012.
PRIDEO55012.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID89816.
KEGGrno:89816.
UCSCRGD:621054. rat.

Organism-specific databases

CTD8301.
RGD621054. Picalm.

Phylogenomic databases

eggNOGNOG267212.
HOVERGENHBG049391.
OrthoDBEOG4C87RV.

Gene expression databases

ArrayExpressO55012.
GenevestigatorO55012.
GermOnlineENSRNOG00000018322. Rattus norvegicus.

Family and domain databases

Gene3D1.20.58.150. 1 hit.
1.25.40.90. 1 hit.
InterProIPR011417. ANTH_dom.
IPR014712. Clathrin_Pinositid-bd_GAT-like.
IPR008942. ENTH_VHS.
IPR013809. Epsin-like_N.
[Graphical view]
PfamPF07651. ANTH. 1 hit.
[Graphical view]
SMARTSM00273. ENTH. 1 hit.
[Graphical view]
SUPFAMSSF48464. ENTH_VHS. 1 hit.
PROSITEPS50942. ENTH. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceO55012.
NextBio617702.

Entry information

Entry namePICA_RAT
AccessionPrimary (citable) accession number: O55012
Secondary accession number(s): O55011
Entry history
Integrated into UniProtKB/Swiss-Prot: March 1, 2004
Last sequence update: June 1, 1998
Last modified: May 29, 2013
This is version 89 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

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