ExPASy logo ExPASy Home page Site Map Search ExPASy Contact us Swiss-Prot
Notice: This page will be replaced with www.uniprot.org. Please send us your feedback!
Search for

UniProtKB/Swiss-Prot entry P49951

[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

Note: most headings are clickable, even if they don't appear as links. They link to the user manual or other documents.
Entry information
Entry name CLH1_BOVIN
Primary accession number P49951
Secondary accession numbers None
Integrated into Swiss-Prot on October 1, 1996
Sequence was last modified on October 1, 1996 (Sequence version 1)
Annotations were last modified on    February 10, 2009 (Entry version 69)
Name and origin of the protein
Protein name Clathrin heavy chain 1
Synonyms None
Gene name
Name: CLTC
From
Bos taurus (Bovine) [TaxID: 9913] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Ruminantia; Pecora; Bovidae; Bovinae; Bos.
Protein existence 1: Evidence at protein level;
References
[1]
 NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Kidney;
DOI=10.1016/0092-8674(95)90167-1; PubMed=7585943 [NCBI, ExPASy, EBI, Israel, Japan]
Liu S.-H., Wong M.L., Craik C.S., Brodsky F.M.;
"Regulation of clathrin assembly and trimerization defined using recombinant triskelion hubs.";
Cell 83:257-267(1995).
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: 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.
  • INTERACTION:
    Q9UJY4:GGA2 (xeno); NbExp=1; IntAct=EBI-448355, EBI-447646;
  • 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 C-terminal third of the heavy chains forms the hub of the triskelion. This region contains the trimerization domain and the light-chain binding domain involved in the assembly of the clathrin lattice.
  • SIMILARITY: Belongs to the clathrin heavy chain family.
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
U31757; AAC48524.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
IPI IPI00688816; -.
RefSeq NP_776448.1; -.
UniGene Bt.44506
3D structure databases
PDB
1B89; X-ray; 2.60 A; A=1074-1522.[ExPASy / RCSB / EBI]
1UTC; X-ray; 2.30 A; A/B=1-363.[ExPASy / RCSB / EBI]
1XI4; EM; 7.90 A; A/B/C/D/E/F/G/H/I=1-1630.[ExPASy / RCSB / EBI]
1XI5; EM; 12.00 A; A/B/C/D/E/F/G/H/I=1-1630.[ExPASy / RCSB / EBI]
Detailed list of linked structures.
PDBsum 1B89; -.
1UTC; -.
1XI4; -.
1XI5; -.
SMR P49951; 1-493.
ModBase P49951.
Protein-protein interaction databases
IntAct P49951; 1.
Ontologies
GO
GO:0030132; Cellular component: clathrin coat of coated pit (inferred from electronic annotation from InterPro).
GO:0030130; Cellular component: clathrin coat of trans-Golgi network vesicle (inferred from electronic annotation from InterPro).
GO:0042470; Cellular component: melanosome (inferred from electronic annotation from UniProtKB-SubCell).
GO:0005739; Cellular component: mitochondrion (inferred from sequence or structural similarity from AgBase).
GO:0005515; Molecular function: protein binding (inferred from physical interaction from IntAct).
GO:0005198; Molecular function: structural molecule activity (inferred from electronic annotation from InterPro).
GO:0006886; Biological process: intracellular protein transport (inferred from electronic annotation from InterPro).
GO:0016192; Biological process: vesicle-mediated transport (inferred from electronic annotation from InterPro).
QuickGo view.
Family and domain databases
InterPro IPR000547; Clathrin_H-chain/VPS_repeat.
IPR016025; Clathrin_H-chain_link/propller.
IPR015348; Clathrin_H-chain_linker_core.
IPR001473; Clathrin_H-chain_propeller_N.
IPR016341; Clathrin_heavy_chain.
IPR011990; TPR-like_helical.
Graphical view of domain structure.
Gene3D G3DSA:2.130.10.110; Clathrin_H-chain_link/propller; 1.
G3DSA:1.25.40.10; TPR-like_helical; 1.
Pfam PF00637; Clathrin; 7.
PF09268; Clathrin-link; 1.
PF01394; Clathrin_propel; 7.
Pfam graphical view of domain structure.
PIRSF PIRSF002290; Clathrin_H_chain; 1.
SMART SM00299; CLH; 7.
SMART graphical view of domain structure.
Genome annotation databases
GeneID 281080; -.
KEGG bta:281080; -.
Phylogenomic databases
HOVERGEN P49951; -.
Other
ProtoNet P49951.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Acetylation; Coated pit; Cytoplasmic vesicle; Membrane; Phosphoprotein.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom    To Length Description FTId
INIT_MET   1      1        Removed (By similarity). 
CHAIN   2   1675  1674     Clathrin heavy chain 1. PRO_0000205777
REGION   2    479  478     Globular terminal domain. 
REGION   449    465  17     Binding site for the uncoating ATPase, involved in lattice disassembly (Potential). 
REGION   480    523  44     Flexible linker. 
REGION   524   1675  1152     Heavy chain arm. 
REGION   524    634  111     Distal segment. 
REGION   639   1675  1037     Proximal segment. 
REGION   1213   1522  310     Involved in binding clathrin light chain. 
REGION   1550   1675  126     Trimerization. 
MOD_RES   2      2        N-acetylalanine (By similarity). 
MOD_RES   394    394        Phosphothreonine (By similarity). 
MOD_RES   634    634        Phosphotyrosine (By similarity). 
MOD_RES   883    883        Phosphotyrosine (By similarity). 
MOD_RES   899    899        Phosphotyrosine (By similarity). 
MOD_RES   1494   1494        Phosphoserine (By similarity). 
STRAND   6     14  9      
HELIX   15     18  4      
HELIX   22     24  3      
TURN   27     29  3      
STRAND   33     44  12      
STRAND   47     54  8      
STRAND   62     65  4      
STRAND   69     73  5      
STRAND   75     84  10      
STRAND   87     92  6      
TURN   93     96  4      
STRAND   97    103  7      
STRAND   110    122  13      
STRAND   124    135  12      
STRAND   139    143  5      
HELIX   146    148  3      
STRAND   152    158  7      
STRAND   164    173  10      
STRAND   176    185  10      
TURN   186    189  4      
STRAND   190    194  5      
STRAND   197    204  8      
STRAND   213    222  10      
STRAND   225    232  8      
STRAND   246    249  4      
STRAND   261    267  7      
TURN   268    271  4      
STRAND   272    277  6      
STRAND   280    286  7      
TURN   287    289  3      
STRAND   292    297  6      
STRAND   303    309  7      
TURN   310    313  4      
STRAND   314    319  6      
STRAND   322    329  8      
TURN   331    333  3      
HELIX   334    340  7      
HELIX   345    354  10      
HELIX   1183   1186  4      
TURN   1187   1191  5      
TURN   1211   1213  3      
HELIX   1214   1220  7      
HELIX   1224   1232  9      
TURN   1233   1235  3      
HELIX   1237   1247  11      
HELIX   1250   1262  13      
HELIX   1266   1271  6      
TURN   1272   1278  7      
HELIX   1280   1292  13      
HELIX   1296   1306  11      
HELIX   1314   1325  12      
HELIX   1329   1339  11      
HELIX   1345   1353  9      
TURN   1354   1356  3      
HELIX   1358   1367  10      
HELIX   1371   1380  10      
TURN   1382   1385  4      
HELIX   1388   1397  10      
HELIX   1402   1414  13      
HELIX   1416   1418  3      
HELIX   1419   1426  8      
HELIX   1427   1429  3      
HELIX   1432   1441  10      
TURN   1445   1448  4      
HELIX   1449   1456  8      
HELIX   1461   1473  13      
HELIX   1477   1486  10      
HELIX   1492   1499  8      
HELIX   1505   1515  11      
Sequence information
Length: 1675 AA [This is the length of the unprocessed precursor] Molecular weight: 191589 Da [This is the MW of the unprocessed precursor] CRC64: 6C4F2D54801579E2 [This is a checksum on the sequence] 
        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 ICVQVASKYH EQLSTQSLIE LFESFKSFEG LFYFLGSIVN 

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

       790        800        810        820        830        840 
FDFVHDLVLY LYRNNLQKYI 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 VELYYRAIQF YLEFKPLLLN DLLMVLSPRL DHTRAVNYFS 

      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 APAYGQPQPG FGYSM
P49951 in FASTA format

View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

BLAST logo BLAST submission on ExPASy/SIB
or at NCBI (USA) 		Tools Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
PROSITE logo ScanProsite, MotifScan SWISS-MODEL Submit a homology modeling request to SWISS-MODEL
NPSA logo NPSA Sequence analysis tools

ExPASy logo ExPASy Home page Site Map Search ExPASy Contact us Swiss-Prot
Hosted by ch flag SIB Switzerland Mirror sites: Australia Brazil Canada China Korea
Notice: This page will be replaced with www.uniprot.org. Please send us your feedback!