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P11442 (CLH1_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified May 29, 2013. Version 112. Feed History...

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

Names and origin

Protein namesRecommended name:
Clathrin heavy chain 1
Gene names
Name:Cltc
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 length1675 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Clathrin is the major protein of the polyhedral coat of coated pits and vesicles. Two different adapter protein complexes link the clathrin lattice either to the plasma membrane or to the trans-Golgi network.

Subunit structure

Clathrin triskelions, composed of 3 heavy chains and 3 light chains, are the basic subunits of the clathrin coat. In the presence of light chains, hub assembly is influenced by both the pH and the concentration of calcium. Interacts with HIP1. Interacts with DENND1A, DENND1B and DENND1C By similarity. Interacts with OCRL. Interacts with ERBB2 By similarity.

Subcellular location

Cytoplasmic vesicle membrane; Peripheral membrane protein; Cytoplasmic side. Membrane › coated pit; Peripheral membrane protein; Cytoplasmic side. Melanosome By similarity. Note: Cytoplasmic face of coated pits and vesicles.

Domain

The N-terminal seven-bladed beta-propeller is formed by WD40-like repeats, and projects inward from the polyhedral outer clathrin coat. It consitutes a major protein-protein interaction node.

Sequence similarities

Belongs to the clathrin heavy chain family.

Contains 7 CHCR (clathrin heavy-chain) repeats.

Ontologies

Keywords
   Cellular componentCoated pit
Cytoplasmic vesicle
Membrane
   DomainRepeat
   PTMAcetylation
Phosphoprotein
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processGolgi organization

Inferred from mutant phenotype PubMed 17065556. Source: RGD

intracellular protein transport

Inferred from electronic annotation. Source: InterPro

mitosis

Inferred from mutant phenotype PubMed 15858577. Source: UniProtKB

receptor-mediated endocytosis

Inferred from mutant phenotype PubMed 15858577. Source: UniProtKB

   Cellular_componentT-tubule

Inferred from direct assay PubMed 7536412. Source: RGD

clathrin coat

Inferred from direct assay PubMed 1490999PubMed 17978091. Source: RGD

clathrin coat of coated pit

Inferred from electronic annotation. Source: InterPro

clathrin coat of trans-Golgi network vesicle

Inferred from electronic annotation. Source: InterPro

clathrin-coated endocytic vesicle membrane

Traceable author statement. Source: Reactome

melanosome

Inferred from electronic annotation. Source: UniProtKB-SubCell

spindle

Inferred from direct assay PubMed 15858577. Source: UniProtKB

   Molecular_functionankyrin binding

Inferred from direct assay PubMed 10585476. Source: RGD

heat shock protein binding

Inferred from direct assay PubMed 17978091. Source: RGD

peptide binding

Inferred from direct assay PubMed 1490999. Source: RGD

structural molecule activity

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.2
Chain2 – 16751674Clathrin heavy chain 1
PRO_0000205780

Regions

Repeat537 – 683147CHCR 1
Repeat686 – 828143CHCR 2
Repeat833 – 972140CHCR 3
Repeat979 – 1124146CHCR 4
Repeat1128 – 1269142CHCR 5
Repeat1274 – 1420147CHCR 6
Repeat1423 – 1566144CHCR 7
Region2 – 479478Globular terminal domain
Region24 – 6744WD40-like repeat 1
Region68 – 10740WD40-like repeat 2
Region108 – 14942WD40-like repeat 3
Region150 – 19546WD40-like repeat 4
Region196 – 25762WD40-like repeat 5
Region258 – 30144WD40-like repeat 6
Region302 – 33029WD40-like repeat 7
Region449 – 46517Binding site for the uncoating ATPase, involved in lattice disassembly Potential
Region480 – 52344Flexible linker
Region524 – 16751152Heavy chain arm
Region524 – 634111Distal segment
Region639 – 16751037Proximal segment
Region1213 – 1522310Involved in binding clathrin light chain By similarity
Region1550 – 1675126Trimerization By similarity

Amino acid modifications

Modified residue21N-acetylalanine Ref.2
Modified residue1841Phosphotyrosine By similarity
Modified residue3941Phosphothreonine By similarity
Modified residue6341Phosphotyrosine By similarity
Modified residue8561N6-acetyllysine By similarity
Modified residue8991Phosphotyrosine By similarity
Modified residue12061Phosphotyrosine By similarity
Modified residue14411N6-acetyllysine By similarity
Modified residue14771Phosphotyrosine By similarity
Modified residue14871Phosphotyrosine By similarity
Modified residue14941Phosphoserine By similarity
Modified residue15011N6-acetyllysine By similarity

Secondary structure

1 ......................................................................................... 1675
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P11442 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: C10F54C7ED8C5A61

FASTA1,675191,599
        10         20         30         40         50         60 
MAQILPIRFQ EHLQLQNLGI NPANIGFSTL TMESDKFICI REKVGEQAQV VIIDMNDPSN 

        70         80         90        100        110        120 
PIRRPISADS AIMNPASKVI ALKAGKTLQI FNIEMKSKMK AHTMTDDVTF WKWISLNTVA 

       130        140        150        160        170        180 
LVTDNAVYHW SMEGESQPVK MFDRHSSLAG CQIINYRTDA KQKWLLLTGI SAQQNRVVGA 

       190        200        210        220        230        240 
MQLYSVDRKV SQPIEGHAAS FAQFKMEGNA EESTLFCFAV RGQAGGKLHI IEVGTPPTGN 

       250        260        270        280        290        300 
QPFPKKAVDV FFPPEAQNDF PVAMQISEKH DVVFLITKYG YIHLYDLETG TCIYMNRISG 

       310        320        330        340        350        360 
ETIFVTAPHE ATAGIIGVNR KGQVLSVCVE EENIIPYITN VLQNPDLALR MAVRNNLAGA 

       370        380        390        400        410        420 
EELFARKFNA LFAQGNYSEA AKVAANAPKG ILRTPDTIRR FQSVPAQPGQ TSPLLQYFGI 

       430        440        450        460        470        480 
LLDQGQLNKY ESLELCRPVL QQGRKQLLEK WLKEDKLECS EELGDLVKSV DPTLALSVYL 

       490        500        510        520        530        540 
RANVPNKVIQ CFAETGQVQK IVLYAKKVGY TPDWIFLLRN VMRISPDQGQ QFAQMLVQDE 

       550        560        570        580        590        600 
EPLADITQIV DVFMEYNLIQ QCTAFLLDAL KNNRPSEGPL QTRLLEMNLM HAPQVADAIL 

       610        620        630        640        650        660 
GNQMFTHYDR AHIAQLCEKA GLLQRALEHF TDLYDIKRAV VHTHLLNPEW LVNYFGSLSV 

       670        680        690        700        710        720 
EDSLECLRAM LSANIRQNLQ IWVQVASKYH EQLSTQSLIE LFESFKSFEG LFYFLGSIVN 

       730        740        750        760        770        780 
FSQDPDVHFK YIQAACKTGQ IKEVERICRE SNCYDPERVK NFLKEAKLTD QLPLIIVCDR 

       790        800        810        820        830        840 
FDFVHDLVLY LYRNSLQKYI EIYVQKVNPS RLPVVIGGLL DVDCSEDVIK NLILVVRGQF 

       850        860        870        880        890        900 
STDELVAEVE KRNRLKLLLP WLEARIHEGC EEPATHNALA KIYIDSNNNP ERFLRENPYY 

       910        920        930        940        950        960 
DSRVVGKYCE KRDPHLACVA YERGQCDLEL INVCNENSLF KSLSRYLVRR KDPELWGSVL 

       970        980        990       1000       1010       1020 
LESNPYRRPL IDQVVQTALS ETQDPEEVSV TVKAFMTADL PNELIELLEK IVLDNSVFSE 

      1030       1040       1050       1060       1070       1080 
HRNLQNLLIL TAIKADRTRV MEYINRLDNY DAPDIANIAI SNELFEEAFA IFRKFDVNTS 

      1090       1100       1110       1120       1130       1140 
AVQVLIEHIG NLDRAYEFAE RCNEPAVWSQ LAKAQLQKGM VKEAIDSYIK ADDPSSYMEV 

      1150       1160       1170       1180       1190       1200 
VQAANTSGNW EELVKYLQMA RKKARESYVE TELIFALAKT NRLAELEEFI NGPNNAHIQQ 

      1210       1220       1230       1240       1250       1260 
VGDRCYDEKM YDAAKLLYNN VSNFGRLAST LVHLGEYQAA VDGARKANST RTWKEVCFAC 

      1270       1280       1290       1300       1310       1320 
VDGKEFRLAQ MCGLHIVVHA DELEELINYY QDRGYFEELI TMLEAALGLE RAHMGMFTEL 

      1330       1340       1350       1360       1370       1380 
AILYSKFKPQ KMREHLELFW SRVNIPKVLR AAEQAHLWAE LVFLYDKYEE YDNAIITMMN 

      1390       1400       1410       1420       1430       1440 
HPTDAWKEGQ FKDIITKVAN VELYYKAIQF YLEFKPLLLN DLLMVLSPRL AHTRAVNYFS 

      1450       1460       1470       1480       1490       1500 
KVKQLPLVKP YLRSVQNHNN KSVNESLNNL FITEEDYQAL RTSIDAYDNF DNISLAQRLE 

      1510       1520       1530       1540       1550       1560 
KHELIEFRRI AAYLFKGNNR WKQSVELCKK DSLYKDAMQY ASESKDTELA EELLQWFLQE 

      1570       1580       1590       1600       1610       1620 
EKRECFGACL FTCYDLLRPD VVLETAWRHN IMDFAMPYFI QVMKEYLTKV DKLDASESLR 

      1630       1640       1650       1660       1670 
KEEEQATETQ PIVYGQPQLM LTAGPSVAVP PQAPFGYGYT APPYGQPQPG FGYSM

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References

[1]"Clathrin heavy chain: molecular cloning and complete primary structure."
Kirchhausen T., Harrison S.C., Chow E.P., Mattaliano R.J., Ramachandran K.L., Smart J., Brosius J.
Proc. Natl. Acad. Sci. U.S.A. 84:8805-8809(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]Bienvenut W.V., von Kriegsheim A.F., Kolch W.
Submitted (AUG-2006) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 2-8; 87-96; 177-205; 270-278; 355-382; 838-851; 882-892; 896-903; 1011-1034; 1095-1101; 1123-1130; 1216-1226; 1398-1406; 1435-1441; 1444-1453; 1502-1508; 1536-1545 AND 1610-1620, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT ALA-2, MASS SPECTROMETRY.
Tissue: Pheochromocytoma.
[3]"Atomic structure of clathrin: a beta propeller terminal domain joins an alpha zigzag linker."
Ter Haar E., Musacchio A., Harrison S.C., Kirchhausen T.
Cell 95:563-573(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 1-493, WD40-LIKE REPEATS.
[4]"Peptide-in-groove interactions link target proteins to the beta-propeller of clathrin."
ter Haar E., Harrison S.C., Kirchhausen T.
Proc. Natl. Acad. Sci. U.S.A. 97:1096-1100(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF 1-359, WD40-LIKE REPEATS.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		J03583 mRNA. Translation: AAA40874.1.
IPIIPI00193983.
PIRLRRTH. A39941.
RefSeqNP_062172.1. NM_019299.1.
UniGeneRn.3589.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1BPOX-ray2.60A/B/C1-494[»]
1C9IX-ray2.90A/B1-359[»]
1C9LX-ray2.90A/B3-359[»]
ProteinModelPortalP11442.
SMRP11442. Positions 1-493, 1182-1516.
ModBaseSearch...

Protein-protein interaction databases

IntActP11442. 1 interaction.
MINTMINT-93121.
STRING10116.ENSRNOP00000052656.

PTM databases

PhosphoSiteP11442.

2D gel databases

World-2DPAGE0004:P11442.

Proteomic databases

PaxDbP11442.
PRIDEP11442.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID54241.
KEGGrno:54241.

Organism-specific databases

CTD1213.
RGD2364. Cltc.

Phylogenomic databases

eggNOGNOG314149.
HOGENOMHOG000188877.
HOVERGENHBG005344.
KOK04646.

Enzyme and pathway databases

ReactomeREACT_111984. Signal Transduction.

Gene expression databases

ArrayExpressP11442.
GenevestigatorP11442.
GermOnlineENSRNOG00000004291. Rattus norvegicus.

Family and domain databases

Gene3D1.25.40.10. 4 hits.
2.130.10.110. 1 hit.
InterProIPR016024. ARM-type_fold.
IPR000547. Clathrin_H-chain/VPS_repeat.
IPR016025. Clathrin_H-chain_link/propller.
IPR015348. Clathrin_H-chain_linker_core.
IPR001473. Clathrin_H-chain_propeller_N.
IPR022365. Clathrin_H-chain_propeller_rpt.
IPR016341. Clathrin_heavy_chain.
IPR011990. TPR-like_helical.
[Graphical view]
PfamPF00637. Clathrin. 7 hits.
PF09268. Clathrin-link. 1 hit.
PF01394. Clathrin_propel. 3 hits.
[Graphical view]
PIRSFPIRSF002290. Clathrin_H_chain. 1 hit.
SMARTSM00299. CLH. 7 hits.
[Graphical view]
SUPFAMSSF48371. ARM-type_fold. 5 hits.
SSF50989. Clathrin_H-chain_propeller_N. 1 hit.
PROSITEPS50236. CHCR. 7 hits.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP11442.
NextBio610700.

Entry information

Entry nameCLH1_RAT
AccessionPrimary (citable) accession number: P11442
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1989
Last sequence update: January 23, 2007
Last modified: May 29, 2013
This is version 112 of the entry and version 3 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

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