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Protein

Clathrin heavy chain 1

Gene

Cltc

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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 (By similarity). Acts as component of the TACC3/ch-TOG/clathrin complex proposed to contribute to stabilization of kinetochore fibers of the mitotic spindle by acting as inter-microtubule bridge (PubMed:15858577,PubMed:16968737). The TACC3/ch-TOG/clathrin complex is required for the maintenance of kinetochore fiber tension (By similarity). Plays a role in early autophagosome formation (By similarity).By similarity2 Publications

GO - Molecular functioni

  • ankyrin binding Source: RGD
  • heat shock protein binding Source: RGD
  • peptide binding Source: RGD
  • protein C-terminus binding Source: RGD
  • structural molecule activity Source: InterPro

GO - Biological processi

  • Golgi organization Source: RGD
  • intracellular protein transport Source: InterPro
  • mitotic nuclear division Source: UniProtKB
  • negative regulation of hyaluronan biosynthetic process Source: UniProtKB
  • receptor-mediated endocytosis Source: UniProtKB
Complete GO annotation...

Keywords - Biological processi

Autophagy

Enzyme and pathway databases

ReactomeiR-RNO-177504. Retrograde neurotrophin signalling.

Names & Taxonomyi

Protein namesi
Recommended name:
Clathrin heavy chain 1
Gene namesi
Name:Cltc
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Unplaced

Organism-specific databases

RGDi2364. Cltc.

Subcellular locationi

GO - Cellular componenti

  • clathrin coat Source: RGD
  • clathrin-coated endocytic vesicle membrane Source: Reactome
  • clathrin coat of coated pit Source: InterPro
  • clathrin coat of trans-Golgi network vesicle Source: InterPro
  • melanosome Source: UniProtKB-SubCell
  • sarcolemma Source: RGD
  • spindle Source: UniProtKB
  • terminal bouton Source: ParkinsonsUK-UCL
  • T-tubule Source: RGD
Complete GO annotation...

Keywords - Cellular componenti

Coated pit, Cytoplasm, Cytoplasmic vesicle, Cytoskeleton, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemoved1 Publication
ChainiPRO_00002057802 – 1675Clathrin heavy chain 1Add BLAST1674

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylalanine1 Publication1
Modified residuei67PhosphoserineBy similarity1
Modified residuei105PhosphothreonineCombined sources1
Modified residuei184PhosphotyrosineBy similarity1
Modified residuei394PhosphothreonineCombined sources1
Modified residuei634PhosphotyrosineBy similarity1
Modified residuei737N6-succinyllysineBy similarity1
Modified residuei856N6-acetyllysineBy similarity1
Modified residuei899PhosphotyrosineBy similarity1
Modified residuei1167PhosphoserineBy similarity1
Modified residuei1206PhosphotyrosineBy similarity1
Modified residuei1229PhosphoserineBy similarity1
Modified residuei1441N6-acetyllysine; alternateBy similarity1
Modified residuei1441N6-succinyllysine; alternateBy similarity1
Modified residuei1477PhosphotyrosineBy similarity1
Modified residuei1487PhosphotyrosineBy similarity1
Modified residuei1494PhosphoserineCombined sources1
Modified residuei1501N6-acetyllysineBy similarity1

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

PaxDbiP11442.
PRIDEiP11442.

2D gel databases

World-2DPAGE0004:P11442.

PTM databases

iPTMnetiP11442.
PhosphoSitePlusiP11442.

Interactioni

Subunit structurei

Clathrin triskelions, composed of 3 heavy chains and 3 light chains, are the basic subunits of the clathrin coat (PubMed:16968737). In the presence of light chains, hub assembly is influenced by both the pH and the concentration of calcium (By similarity). Interacts with HIP1 (By similarity). Interacts with DENND1A, DENND1B and DENND1C (By similarity). Interacts with OCRL (By similarity). Interacts with ERBB2 (By similarity). Interacts with FKBP6 (By similarity). Interacts with CKAP5 and TACC3 forming the TACC3/ch-TOG/clathrin complex located at spindle inter-microtubules bridges; the complex implicates clathrin triskelions; TACC3 and CLTC are proposed to form a composite microtubule interaction surface (By similarity). Interacts with ATG16L1 (via N-terminus) (By similarity).By similarity1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
OCRLQ019685EBI-397997,EBI-6148898From a different organism.

GO - Molecular functioni

  • ankyrin binding Source: RGD
  • heat shock protein binding Source: RGD
  • protein C-terminus binding Source: RGD

Protein-protein interaction databases

BioGridi248464. 13 interactors.
DIPiDIP-36966N.
IntActiP11442. 5 interactors.
MINTiMINT-93121.
STRINGi10116.ENSRNOP00000005987.

Structurei

Secondary structure

11675
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi7 – 14Combined sources8
Helixi15 – 18Combined sources4
Helixi22 – 24Combined sources3
Turni27 – 29Combined sources3
Beta strandi30 – 34Combined sources5
Beta strandi37 – 42Combined sources6
Beta strandi49 – 54Combined sources6
Beta strandi62 – 65Combined sources4
Beta strandi71 – 73Combined sources3
Beta strandi75 – 78Combined sources4
Beta strandi80 – 84Combined sources5
Beta strandi87 – 92Combined sources6
Turni93 – 96Combined sources4
Beta strandi97 – 103Combined sources7
Beta strandi110 – 115Combined sources6
Beta strandi118 – 122Combined sources5
Beta strandi124 – 135Combined sources12
Beta strandi139 – 143Combined sources5
Helixi146 – 148Combined sources3
Beta strandi152 – 158Combined sources7
Beta strandi162 – 173Combined sources12
Beta strandi176 – 186Combined sources11
Beta strandi191 – 194Combined sources4
Beta strandi197 – 205Combined sources9
Beta strandi210 – 220Combined sources11
Beta strandi227 – 232Combined sources6
Beta strandi246 – 249Combined sources4
Beta strandi261 – 267Combined sources7
Turni268 – 271Combined sources4
Beta strandi272 – 277Combined sources6
Beta strandi280 – 286Combined sources7
Turni287 – 289Combined sources3
Beta strandi292 – 297Combined sources6
Beta strandi303 – 309Combined sources7
Turni310 – 313Combined sources4
Beta strandi314 – 319Combined sources6
Turni320 – 322Combined sources3
Beta strandi323 – 329Combined sources7
Turni331 – 333Combined sources3
Helixi334 – 340Combined sources7
Helixi345 – 354Combined sources10
Helixi361 – 373Combined sources13
Helixi377 – 386Combined sources10
Helixi388 – 390Combined sources3
Helixi395 – 401Combined sources7
Helixi413 – 424Combined sources12
Helixi429 – 441Combined sources13
Helixi445 – 454Combined sources10
Helixi461 – 470Combined sources10
Helixi473 – 482Combined sources10

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1BPOX-ray2.60A/B/C1-494[»]
1C9IX-ray2.90A/B1-359[»]
1C9LX-ray2.90A/B3-359[»]
ProteinModelPortaliP11442.
SMRiP11442.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP11442.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Repeati537 – 683CHCR 1Add BLAST147
Repeati686 – 828CHCR 2Add BLAST143
Repeati833 – 972CHCR 3Add BLAST140
Repeati979 – 1124CHCR 4Add BLAST146
Repeati1128 – 1269CHCR 5Add BLAST142
Repeati1274 – 1420CHCR 6Add BLAST147
Repeati1423 – 1566CHCR 7Add BLAST144

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni2 – 479Globular terminal domainAdd BLAST478
Regioni24 – 67WD40-like repeat 1Add BLAST44
Regioni68 – 107WD40-like repeat 2Add BLAST40
Regioni108 – 149WD40-like repeat 3Add BLAST42
Regioni150 – 195WD40-like repeat 4Add BLAST46
Regioni196 – 257WD40-like repeat 5Add BLAST62
Regioni258 – 301WD40-like repeat 6Add BLAST44
Regioni302 – 330WD40-like repeat 7Add BLAST29
Regioni449 – 465Binding site for the uncoating ATPase, involved in lattice disassemblySequence analysisAdd BLAST17
Regioni480 – 523Flexible linkerAdd BLAST44
Regioni524 – 1675Heavy chain armAdd BLAST1152
Regioni524 – 634Distal segmentAdd BLAST111
Regioni639 – 1675Proximal segmentAdd BLAST1037
Regioni1213 – 1522Involved in binding clathrin light chainBy similarityAdd BLAST310
Regioni1550 – 1675TrimerizationBy similarityAdd BLAST126

Domaini

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

Sequence similaritiesi

Belongs to the clathrin heavy chain family.Curated
Contains 7 CHCR (clathrin heavy-chain) repeats.PROSITE-ProRule annotation

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiKOG0985. Eukaryota.
ENOG410XPH1. LUCA.
HOGENOMiHOG000188877.
HOVERGENiHBG005344.
InParanoidiP11442.
KOiK04646.
PhylomeDBiP11442.

Family and domain databases

Gene3Di1.25.40.10. 4 hits.
2.130.10.110. 1 hit.
InterProiIPR016024. 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_dom.
[Graphical view]
PfamiPF00637. Clathrin. 7 hits.
PF09268. Clathrin-link. 1 hit.
PF01394. Clathrin_propel. 5 hits.
[Graphical view]
PIRSFiPIRSF002290. Clathrin_H_chain. 1 hit.
SMARTiSM00299. CLH. 7 hits.
[Graphical view]
SUPFAMiSSF48371. SSF48371. 6 hits.
SSF50989. SSF50989. 1 hit.
PROSITEiPS50236. CHCR. 7 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P11442-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAQILPIRFQ EHLQLQNLGI NPANIGFSTL TMESDKFICI REKVGEQAQV
60 70 80 90 100
VIIDMNDPSN PIRRPISADS AIMNPASKVI ALKAGKTLQI FNIEMKSKMK
110 120 130 140 150
AHTMTDDVTF WKWISLNTVA LVTDNAVYHW SMEGESQPVK MFDRHSSLAG
160 170 180 190 200
CQIINYRTDA KQKWLLLTGI SAQQNRVVGA MQLYSVDRKV SQPIEGHAAS
210 220 230 240 250
FAQFKMEGNA EESTLFCFAV RGQAGGKLHI IEVGTPPTGN QPFPKKAVDV
260 270 280 290 300
FFPPEAQNDF PVAMQISEKH DVVFLITKYG YIHLYDLETG TCIYMNRISG
310 320 330 340 350
ETIFVTAPHE ATAGIIGVNR KGQVLSVCVE EENIIPYITN VLQNPDLALR
360 370 380 390 400
MAVRNNLAGA EELFARKFNA LFAQGNYSEA AKVAANAPKG ILRTPDTIRR
410 420 430 440 450
FQSVPAQPGQ TSPLLQYFGI LLDQGQLNKY ESLELCRPVL QQGRKQLLEK
460 470 480 490 500
WLKEDKLECS EELGDLVKSV DPTLALSVYL RANVPNKVIQ CFAETGQVQK
510 520 530 540 550
IVLYAKKVGY TPDWIFLLRN VMRISPDQGQ QFAQMLVQDE EPLADITQIV
560 570 580 590 600
DVFMEYNLIQ QCTAFLLDAL KNNRPSEGPL QTRLLEMNLM HAPQVADAIL
610 620 630 640 650
GNQMFTHYDR AHIAQLCEKA GLLQRALEHF TDLYDIKRAV VHTHLLNPEW
660 670 680 690 700
LVNYFGSLSV EDSLECLRAM LSANIRQNLQ IWVQVASKYH EQLSTQSLIE
710 720 730 740 750
LFESFKSFEG LFYFLGSIVN FSQDPDVHFK YIQAACKTGQ IKEVERICRE
760 770 780 790 800
SNCYDPERVK NFLKEAKLTD QLPLIIVCDR FDFVHDLVLY LYRNSLQKYI
810 820 830 840 850
EIYVQKVNPS RLPVVIGGLL DVDCSEDVIK NLILVVRGQF STDELVAEVE
860 870 880 890 900
KRNRLKLLLP WLEARIHEGC EEPATHNALA KIYIDSNNNP ERFLRENPYY
910 920 930 940 950
DSRVVGKYCE KRDPHLACVA YERGQCDLEL INVCNENSLF KSLSRYLVRR
960 970 980 990 1000
KDPELWGSVL LESNPYRRPL IDQVVQTALS ETQDPEEVSV TVKAFMTADL
1010 1020 1030 1040 1050
PNELIELLEK IVLDNSVFSE HRNLQNLLIL TAIKADRTRV MEYINRLDNY
1060 1070 1080 1090 1100
DAPDIANIAI SNELFEEAFA IFRKFDVNTS AVQVLIEHIG NLDRAYEFAE
1110 1120 1130 1140 1150
RCNEPAVWSQ LAKAQLQKGM VKEAIDSYIK ADDPSSYMEV VQAANTSGNW
1160 1170 1180 1190 1200
EELVKYLQMA RKKARESYVE TELIFALAKT NRLAELEEFI NGPNNAHIQQ
1210 1220 1230 1240 1250
VGDRCYDEKM YDAAKLLYNN VSNFGRLAST LVHLGEYQAA VDGARKANST
1260 1270 1280 1290 1300
RTWKEVCFAC VDGKEFRLAQ MCGLHIVVHA DELEELINYY QDRGYFEELI
1310 1320 1330 1340 1350
TMLEAALGLE RAHMGMFTEL AILYSKFKPQ KMREHLELFW SRVNIPKVLR
1360 1370 1380 1390 1400
AAEQAHLWAE LVFLYDKYEE YDNAIITMMN HPTDAWKEGQ FKDIITKVAN
1410 1420 1430 1440 1450
VELYYKAIQF YLEFKPLLLN DLLMVLSPRL AHTRAVNYFS KVKQLPLVKP
1460 1470 1480 1490 1500
YLRSVQNHNN KSVNESLNNL FITEEDYQAL RTSIDAYDNF DNISLAQRLE
1510 1520 1530 1540 1550
KHELIEFRRI AAYLFKGNNR WKQSVELCKK DSLYKDAMQY ASESKDTELA
1560 1570 1580 1590 1600
EELLQWFLQE EKRECFGACL FTCYDLLRPD VVLETAWRHN IMDFAMPYFI
1610 1620 1630 1640 1650
QVMKEYLTKV DKLDASESLR KEEEQATETQ PIVYGQPQLM LTAGPSVAVP
1660 1670
PQAPFGYGYT APPYGQPQPG FGYSM
Length:1,675
Mass (Da):191,599
Last modified:January 23, 2007 - v3
Checksum:iC10F54C7ED8C5A61
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J03583 mRNA. Translation: AAA40874.1.
PIRiA39941. LRRTH.
RefSeqiNP_062172.1. NM_019299.1.
UniGeneiRn.3589.

Genome annotation databases

GeneIDi54241.
KEGGirno:54241.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J03583 mRNA. Translation: AAA40874.1.
PIRiA39941. LRRTH.
RefSeqiNP_062172.1. NM_019299.1.
UniGeneiRn.3589.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1BPOX-ray2.60A/B/C1-494[»]
1C9IX-ray2.90A/B1-359[»]
1C9LX-ray2.90A/B3-359[»]
ProteinModelPortaliP11442.
SMRiP11442.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi248464. 13 interactors.
DIPiDIP-36966N.
IntActiP11442. 5 interactors.
MINTiMINT-93121.
STRINGi10116.ENSRNOP00000005987.

PTM databases

iPTMnetiP11442.
PhosphoSitePlusiP11442.

2D gel databases

World-2DPAGE0004:P11442.

Proteomic databases

PaxDbiP11442.
PRIDEiP11442.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi54241.
KEGGirno:54241.

Organism-specific databases

CTDi1213.
RGDi2364. Cltc.

Phylogenomic databases

eggNOGiKOG0985. Eukaryota.
ENOG410XPH1. LUCA.
HOGENOMiHOG000188877.
HOVERGENiHBG005344.
InParanoidiP11442.
KOiK04646.
PhylomeDBiP11442.

Enzyme and pathway databases

ReactomeiR-RNO-177504. Retrograde neurotrophin signalling.

Miscellaneous databases

EvolutionaryTraceiP11442.
PROiP11442.

Family and domain databases

Gene3Di1.25.40.10. 4 hits.
2.130.10.110. 1 hit.
InterProiIPR016024. 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_dom.
[Graphical view]
PfamiPF00637. Clathrin. 7 hits.
PF09268. Clathrin-link. 1 hit.
PF01394. Clathrin_propel. 5 hits.
[Graphical view]
PIRSFiPIRSF002290. Clathrin_H_chain. 1 hit.
SMARTiSM00299. CLH. 7 hits.
[Graphical view]
SUPFAMiSSF48371. SSF48371. 6 hits.
SSF50989. SSF50989. 1 hit.
PROSITEiPS50236. CHCR. 7 hits.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiCLH1_RAT
AccessioniPrimary (citable) accession number: P11442
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1989
Last sequence update: January 23, 2007
Last modified: November 30, 2016
This is version 144 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.