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P11442

- CLH1_RAT

UniProt

P11442 - CLH1_RAT

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Protein

Clathrin heavy chain 1

Gene

Cltc

Organism
Rattus norvegicus (Rat)
Status
Reviewed - 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.

GO - Molecular functioni

  1. ankyrin binding Source: RGD
  2. heat shock protein binding Source: RGD
  3. peptide binding Source: RGD
  4. protein C-terminus binding Source: RGD
  5. structural molecule activity Source: InterPro

GO - Biological processi

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

Names & Taxonomyi

Protein namesi
Recommended name:
Clathrin heavy chain 1
Gene namesi
Name:Cltc
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
ProteomesiUP000002494: Unplaced

Organism-specific databases

RGDi2364. Cltc.

Subcellular locationi

GO - Cellular componenti

  1. clathrin coat Source: RGD
  2. clathrin-coated endocytic vesicle membrane Source: Reactome
  3. clathrin coat of coated pit Source: InterPro
  4. clathrin coat of trans-Golgi network vesicle Source: InterPro
  5. sarcolemma Source: RGD
  6. spindle Source: UniProtKB
  7. T-tubule Source: RGD
Complete GO annotation...

Keywords - Cellular componenti

Coated pit, Cytoplasmic vesicle, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 16751674Clathrin heavy chain 1PRO_0000205780Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanine1 Publication
Modified residuei184 – 1841PhosphotyrosineBy similarity
Modified residuei394 – 3941PhosphothreonineBy similarity
Modified residuei634 – 6341PhosphotyrosineBy similarity
Modified residuei737 – 7371N6-succinyllysineBy similarity
Modified residuei856 – 8561N6-acetyllysineBy similarity
Modified residuei899 – 8991PhosphotyrosineBy similarity
Modified residuei1206 – 12061PhosphotyrosineBy similarity
Modified residuei1441 – 14411N6-acetyllysine; alternateBy similarity
Modified residuei1441 – 14411N6-succinyllysine; alternateBy similarity
Modified residuei1477 – 14771PhosphotyrosineBy similarity
Modified residuei1487 – 14871PhosphotyrosineBy similarity
Modified residuei1494 – 14941PhosphoserineBy similarity
Modified residuei1501 – 15011N6-acetyllysineBy similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

PaxDbiP11442.
PRIDEiP11442.

2D gel databases

World-2DPAGE0004:P11442.

PTM databases

PhosphoSiteiP11442.

Expressioni

Gene expression databases

GenevestigatoriP11442.

Interactioni

Subunit structurei

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. Interacts with FKBP6 By similarity.By similarity

Binary interactionsi

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

Protein-protein interaction databases

BioGridi248464. 12 interactions.
DIPiDIP-36966N.
IntActiP11442. 4 interactions.
MINTiMINT-93121.
STRINGi10116.ENSRNOP00000052656.

Structurei

Secondary structure

1
1675
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi7 – 148
Helixi15 – 184
Helixi22 – 243
Turni27 – 293
Beta strandi30 – 345
Beta strandi37 – 426
Beta strandi49 – 546
Beta strandi62 – 654
Beta strandi71 – 733
Beta strandi75 – 784
Beta strandi80 – 845
Beta strandi87 – 926
Turni93 – 964
Beta strandi97 – 1037
Beta strandi110 – 1156
Beta strandi118 – 1225
Beta strandi124 – 13512
Beta strandi139 – 1435
Helixi146 – 1483
Beta strandi152 – 1587
Beta strandi162 – 17312
Beta strandi176 – 18611
Beta strandi191 – 1944
Beta strandi197 – 2059
Beta strandi210 – 22011
Beta strandi227 – 2326
Beta strandi246 – 2494
Beta strandi261 – 2677
Turni268 – 2714
Beta strandi272 – 2776
Beta strandi280 – 2867
Turni287 – 2893
Beta strandi292 – 2976
Beta strandi303 – 3097
Turni310 – 3134
Beta strandi314 – 3196
Turni320 – 3223
Beta strandi323 – 3297
Turni331 – 3333
Helixi334 – 3407
Helixi345 – 35410
Helixi361 – 37313
Helixi377 – 38610
Helixi388 – 3903
Helixi395 – 4017
Helixi413 – 42412
Helixi429 – 44113
Helixi445 – 45410
Helixi461 – 47010
Helixi473 – 48210

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1BPOX-ray2.60A/B/C1-494[»]
1C9IX-ray2.90A/B1-359[»]
1C9LX-ray2.90A/B3-359[»]
ProteinModelPortaliP11442.
SMRiP11442. Positions 1-493, 1182-1516.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP11442.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati537 – 683147CHCR 1Add
BLAST
Repeati686 – 828143CHCR 2Add
BLAST
Repeati833 – 972140CHCR 3Add
BLAST
Repeati979 – 1124146CHCR 4Add
BLAST
Repeati1128 – 1269142CHCR 5Add
BLAST
Repeati1274 – 1420147CHCR 6Add
BLAST
Repeati1423 – 1566144CHCR 7Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni2 – 479478Globular terminal domainAdd
BLAST
Regioni24 – 6744WD40-like repeat 1Add
BLAST
Regioni68 – 10740WD40-like repeat 2Add
BLAST
Regioni108 – 14942WD40-like repeat 3Add
BLAST
Regioni150 – 19546WD40-like repeat 4Add
BLAST
Regioni196 – 25762WD40-like repeat 5Add
BLAST
Regioni258 – 30144WD40-like repeat 6Add
BLAST
Regioni302 – 33029WD40-like repeat 7Add
BLAST
Regioni449 – 46517Binding site for the uncoating ATPase, involved in lattice disassemblySequence AnalysisAdd
BLAST
Regioni480 – 52344Flexible linkerAdd
BLAST
Regioni524 – 16751152Heavy chain armAdd
BLAST
Regioni524 – 634111Distal segmentAdd
BLAST
Regioni639 – 16751037Proximal segmentAdd
BLAST
Regioni1213 – 1522310Involved in binding clathrin light chainBy similarityAdd
BLAST
Regioni1550 – 1675126TrimerizationBy similarityAdd
BLAST

Domaini

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 similaritiesi

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

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiNOG314149.
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. 3 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:
EMBL
GenBank
DDBJ
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:
EMBL
GenBank
DDBJ
Links Updated
J03583 mRNA. Translation: AAA40874.1 .
PIRi A39941. LRRTH.
RefSeqi NP_062172.1. NM_019299.1.
UniGenei Rn.3589.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1BPO X-ray 2.60 A/B/C 1-494 [» ]
1C9I X-ray 2.90 A/B 1-359 [» ]
1C9L X-ray 2.90 A/B 3-359 [» ]
ProteinModelPortali P11442.
SMRi P11442. Positions 1-493, 1182-1516.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 248464. 12 interactions.
DIPi DIP-36966N.
IntActi P11442. 4 interactions.
MINTi MINT-93121.
STRINGi 10116.ENSRNOP00000052656.

PTM databases

PhosphoSitei P11442.

2D gel databases

World-2DPAGE 0004:P11442.

Proteomic databases

PaxDbi P11442.
PRIDEi P11442.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 54241.
KEGGi rno:54241.

Organism-specific databases

CTDi 1213.
RGDi 2364. Cltc.

Phylogenomic databases

eggNOGi NOG314149.
HOGENOMi HOG000188877.
HOVERGENi HBG005344.
InParanoidi P11442.
KOi K04646.
PhylomeDBi P11442.

Miscellaneous databases

EvolutionaryTracei P11442.
NextBioi 610700.

Gene expression databases

Genevestigatori P11442.

Family and domain databases

Gene3Di 1.25.40.10. 4 hits.
2.130.10.110. 1 hit.
InterProi IPR016024. 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 ]
Pfami PF00637. Clathrin. 7 hits.
PF09268. Clathrin-link. 1 hit.
PF01394. Clathrin_propel. 3 hits.
[Graphical view ]
PIRSFi PIRSF002290. Clathrin_H_chain. 1 hit.
SMARTi SM00299. CLH. 7 hits.
[Graphical view ]
SUPFAMi SSF48371. SSF48371. 6 hits.
SSF50989. SSF50989. 1 hit.
PROSITEi PS50236. CHCR. 7 hits.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. 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, IDENTIFICATION BY 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.

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: October 29, 2014
This is version 126 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

External Data

Dasty 3