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Q05140 (AP180_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 100. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Clathrin coat assembly protein AP180
Alternative name(s):
91 kDa synaptosomal-associated protein
Clathrin coat-associated protein AP180
Gene names
Name:Snap91
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 length915 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Adaptins are components of the adapter complexes which link clathrin to receptors in coated vesicles. Clathrin-associated protein complexes are believed to interact with the cytoplasmic tails of membrane proteins, leading to their selection and concentration. Binding of AP180 to clathrin triskelia induces their assembly into 60-70 nm coats.

Subunit structure

Binds AP2A2. Interacts with AP2B1; clathrin competes with SNAP91. Ref.4 Ref.5 Ref.6 Ref.7 Ref.8

Subcellular location

Cell membrane. Membrane › coated pit; Peripheral membrane protein; Cytoplasmic side. Note: Component of the coat surrounding the cytoplasmic face of coated vesicles in the plasma membrane.

Domain

Possesses a three domain structure: the N-terminal 300 residues harbor a clathrin binding site, an acidic middle domain 450 residues, interrupted by an Ala-rich segment, and the C-terminal domain (166 residues).

Post-translational modification

Thr-310 can be modified by the addition of N-acetylglucosamine which can be further phosphorylated. The form with phosphorylated O-linked N-acetylglucosamine is predominant in brain synaptosomes. There is no evidence for direct Thr-310 phosphorylation (Ref.3). Ref.3

Sequence similarities

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

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q05140-1)

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 (identifier: Q05140-2)

The sequence of this isoform differs from the canonical sequence as follows:
     614-632: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 915915Clathrin coat assembly protein AP180
PRO_0000193866

Regions

Domain14 – 145132ENTH
Compositional bias410 – 4134Poly-Thr
Compositional bias535 – 5395Poly-Ala
Compositional bias547 – 5504Poly-Ala
Compositional bias678 – 6836Poly-Ser
Compositional bias723 – 7297Poly-Ser

Amino acid modifications

Modified residue3061Phosphoserine
Modified residue3121Phosphothreonine By similarity
Modified residue3131Phosphoserine Ref.3
Modified residue3161Phosphoserine By similarity
Modified residue6001Phosphoserine Ref.3
Modified residue6401Phosphoserine Ref.3
Modified residue6461Phosphoserine Ref.3
Glycosylation3101O-linked (GlcNAc) Ref.3

Natural variations

Alternative sequence614 – 63219Missing in isoform 2.
VSP_000173

Sequences

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

Last modified November 1, 1996. Version 1.
Checksum: 32EC1B38EC5DF8C0

FASTA91593,519
        10         20         30         40         50         60 
MSGQTLTDRI AAAQYSVTGS AVARAVCKAT THEVMGPKKK HLDYLIQATN ETNVNIPQMA 

        70         80         90        100        110        120 
DTLFERATNS SWVVVFKALV TTHHLMVHGN ERFIQYLASR NTLFNLSNFL DKSGSHGYDM 

       130        140        150        160        170        180 
STFIRRYSRY LNEKAFSYRQ MAFDFARVKK GADGVMRTMV PEKLLKSMPI LQGQIDALLE 

       190        200        210        220        230        240 
FDVHPNELTN GVINAAFMLL FKDLIKLFAC YNDGVINLLE KFFEMKKGQC KDALEIYKRF 

       250        260        270        280        290        300 
LTRMTRVSEF LKVADEVGID KGDIPDLTQA PSSLMETLEQ HLNTLEGKKP GNNEGSGAPS 

       310        320        330        340        350        360 
PLSKSSPATT VTSPNSTPAK TIDTSPPVDI FATASAAAPV SSAKPSSDLL DLQPDFSGAR 

       370        380        390        400        410        420 
AGAAAPVPPP TGGATAWGDL LGEDSLAALS SVPSEAPISD PFAPEPSPPT TTTEPASASA 

       430        440        450        460        470        480 
SATTAVTAAT TEVDLFGDAF AASPGEAPAA SEGATAPATP APVAAALDAC SGNDPFAPSE 

       490        500        510        520        530        540 
GSAEAAPELD LFAMKPPETS APVVTPTAST APPVPATAPS PAPTAVAATA ATTTAAAAAT 

       550        560        570        580        590        600 
TTATTSAAAA TTAAAPPALD IFGDLFDSAP EVAAASKPDV APSIDLFGTD AFSSPPRGAS 

       610        620        630        640        650        660 
PVPESSLTAD LLSGSGFHCA EDDRHVPLFF TAVDAFAAPS PASTASPAKA ESSGVIDLFG 

       670        680        690        700        710        720 
DAFGSSASET QPAPQAVSSS SASADLLAGF GGSFMAPSTT PVTPAQNNLL QPNFEAAFGT 

       730        740        750        760        770        780 
TPSTSSSSSF DPSGDLLMPT MAPSGQPAPV SMVPPSPAMS ASKGLGSDLD SSLASLVGNL 

       790        800        810        820        830        840 
GISGTTSKKG DLQWNAGEKK LTGGANWQPK VTPATWSAGV PPQGTVPPTS SVPPGAGAPS 

       850        860        870        880        890        900 
VGQPGAGYGM PPAGTGMTMM PQQPVMFAQP MMRPPFGAAA VPGTQLSPSP TPATQSPKKP 

       910 
PAKDPLADLN IKDFL

« Hide

Isoform 2 [UniParc].

Checksum: 41417E79D1044984
Show »

FASTA89691,431

References

[1]"Clathrin assembly protein AP180: primary structure, domain organization and identification of a clathrin binding site."
Morris S.A., Schroeder S., Plessmann U., Weber K., Ungewickell E.
EMBO J. 12:667-675(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
Tissue: Brain.
[2]Lubec G., Kang S.U., Lubec S.
Submitted (SEP-2007) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 25-39 AND 247-252 (ISOFORMS 1/2), MASS SPECTROMETRY.
Strain: Sprague-Dawley.
Tissue: Brain.
[3]"A novel post-translational modification in nerve terminals: O-linked N-acetylglucosamine phosphorylation."
Graham M.E., Thaysen-Andersen M., Bache N., Craft G.E., Larsen M.R., Packer N.H., Robinson P.J.
J. Proteome Res. 10:2725-2733(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 305-320 (ISOFORMS 1/2), PROTEIN SEQUENCE OF 598-649 (ISOFORM 2), GLYCOSYLATION AT THR-310, PHOSPHORYLATION AT SER-313; SER-313; SER-600; SER-640 AND SER-646, MASS SPECTROMETRY.
[4]"A structural explanation for the binding of multiple ligands by the alpha-adaptin appendage domain."
Owen D.J., Vallis Y., Noble M.E.M., Hunter J.B., Dafforn T.R., Evans P.R., McMahon H.T.
Cell 97:805-815(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH AP2A2.
[5]"Crystal structure of the alpha appendage of AP-2 reveals a recruitment platform for clathrin-coat assembly."
Traub L.M., Downs M.A., Westrich J.L., Fremont D.H.
Proc. Natl. Acad. Sci. U.S.A. 96:8907-8912(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH AP2A2.
[6]"The structure and function of the beta 2-adaptin appendage domain."
Owen D.J., Vallis Y., Pearse B.M.F., McMahon H.T., Evans P.R.
EMBO J. 19:4216-4227(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH AP2B1.
[7]"Molecular switches involving the AP-2 beta2 appendage regulate endocytic cargo selection and clathrin coat assembly."
Edeling M.A., Mishra S.K., Keyel P.A., Steinhauser A.L., Collins B.M., Roth R., Heuser J.E., Owen D.J., Traub L.M.
Dev. Cell 10:329-342(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH AP2B1.
[8]"Role of the AP2 beta-appendage hub in recruiting partners for clathrin-coated vesicle assembly."
Schmid E.M., Ford M.G.J., Burtey A., Praefcke G.J.K., Peak-Chew S.-Y., Mills I.G., Benmerah A., McMahon H.T.
PLoS Biol. 4:E262-E262(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH AP2B1.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		X68877 mRNA. Translation: CAA48748.1.
X68878 mRNA. Translation: CAA48749.1.
IPIIPI00215134.
IPI00391854.
PIRS36326.
S36327.
RefSeqNP_113916.1. NM_031728.1.
UniGeneRn.11022.

3D structure databases

DisProtDP00225.
ProteinModelPortalQ05140.
SMRQ05140. Positions 19-281.
ModBaseSearch...

Protein-protein interaction databases

IntActQ05140. 1 interaction.
MINTMINT-101133.
STRING10116.ENSRNOP00000030821.

PTM databases

PhosphoSiteQ05140.

Proteomic databases

PaxDbQ05140.
PRIDEQ05140.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID65178.
KEGGrno:65178.
UCSCRGD:69276. rat.

Organism-specific databases

CTD9892.
RGD69276. Snap91.

Phylogenomic databases

eggNOGNOG267212.
HOGENOMHOG000015763.
HOVERGENHBG049391.
InParanoidQ05140.

Gene expression databases

ArrayExpressQ05140.
GenevestigatorQ05140.
GermOnlineENSRNOG00000023861. 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

NextBio614072.

Entry information

Entry nameAP180_RAT
AccessionPrimary (citable) accession number: Q05140
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1996
Last modified: May 1, 2013
This is version 100 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents