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P49951

- CLH1_BOVIN

UniProt

P49951 - CLH1_BOVIN

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Protein

Clathrin heavy chain 1

Gene

CLTC

Organism
Bos taurus (Bovine)
Status
Reviewed - Annotation score: 4 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. structural molecule activity Source: InterPro

GO - Biological processi

  1. intracellular protein transport Source: InterPro
  2. negative regulation of hyaluronan biosynthetic process Source: UniProtKB
  3. vesicle-mediated transport Source: InterPro
Complete GO annotation...

Names & Taxonomyi

Protein namesi
Recommended name:
Clathrin heavy chain 1
Gene namesi
Name:CLTC
OrganismiBos taurus (Bovine)
Taxonomic identifieri9913 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
ProteomesiUP000009136: Unplaced

Subcellular locationi

GO - Cellular componenti

  1. clathrin coat of coated pit Source: InterPro
  2. clathrin coat of trans-Golgi network vesicle Source: InterPro
  3. membrane coat Source: AgBase
  4. mitochondrion Source: AgBase
Complete GO annotation...

Keywords - Cellular componenti

Coated pit, Cytoplasmic vesicle, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11RemovedBy similarity
Chaini2 – 16751674Clathrin heavy chain 1PRO_0000205777Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanineBy similarity
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

PaxDbiP49951.
PRIDEiP49951.

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. Interacts with OCRL. Interacts with ERBB2. Interacts with FKBP6 (By similarity).By similarity

Protein-protein interaction databases

BioGridi158448. 1 interaction.
IntActiP49951. 7 interactions.
MINTiMINT-122490.
STRINGi9913.ENSBTAP00000022210.

Structurei

Secondary structure

1
1675
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi6 – 149Combined sources
Helixi15 – 184Combined sources
Helixi22 – 243Combined sources
Turni27 – 293Combined sources
Beta strandi30 – 345Combined sources
Beta strandi37 – 426Combined sources
Beta strandi49 – 546Combined sources
Beta strandi62 – 665Combined sources
Beta strandi69 – 735Combined sources
Beta strandi75 – 8410Combined sources
Beta strandi87 – 926Combined sources
Turni93 – 964Combined sources
Beta strandi97 – 1037Combined sources
Beta strandi108 – 1136Combined sources
Beta strandi115 – 13319Combined sources
Beta strandi139 – 1435Combined sources
Helixi146 – 1483Combined sources
Beta strandi152 – 1587Combined sources
Beta strandi164 – 1729Combined sources
Beta strandi177 – 1859Combined sources
Turni186 – 1894Combined sources
Beta strandi190 – 1945Combined sources
Beta strandi197 – 2048Combined sources
Beta strandi213 – 22210Combined sources
Beta strandi225 – 2328Combined sources
Beta strandi246 – 2494Combined sources
Beta strandi261 – 2677Combined sources
Turni268 – 2714Combined sources
Beta strandi272 – 2776Combined sources
Beta strandi280 – 2867Combined sources
Turni287 – 2893Combined sources
Beta strandi292 – 2976Combined sources
Beta strandi303 – 3097Combined sources
Helixi310 – 3123Combined sources
Beta strandi314 – 3196Combined sources
Beta strandi322 – 3298Combined sources
Turni331 – 3333Combined sources
Helixi334 – 3407Combined sources
Helixi345 – 35511Combined sources
Helixi1183 – 11864Combined sources
Turni1187 – 11915Combined sources
Turni1211 – 12133Combined sources
Helixi1214 – 12207Combined sources
Helixi1224 – 12329Combined sources
Turni1233 – 12353Combined sources
Helixi1237 – 124711Combined sources
Helixi1250 – 126213Combined sources
Helixi1266 – 12716Combined sources
Turni1272 – 12787Combined sources
Helixi1280 – 129213Combined sources
Helixi1296 – 130611Combined sources
Helixi1314 – 132512Combined sources
Helixi1329 – 133911Combined sources
Helixi1345 – 13539Combined sources
Turni1354 – 13563Combined sources
Helixi1358 – 136710Combined sources
Helixi1371 – 138010Combined sources
Turni1382 – 13854Combined sources
Helixi1388 – 139710Combined sources
Helixi1402 – 141413Combined sources
Helixi1416 – 14183Combined sources
Helixi1419 – 14268Combined sources
Helixi1427 – 14293Combined sources
Helixi1432 – 144110Combined sources
Turni1445 – 14484Combined sources
Helixi1449 – 14568Combined sources
Helixi1461 – 147313Combined sources
Helixi1477 – 148610Combined sources
Helixi1492 – 14998Combined sources
Helixi1505 – 151511Combined sources

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1B89X-ray2.60A1074-1522[»]
1UTCX-ray2.30A/B1-363[»]
1XI4electron microscopy7.90A/B/C/D/E/F/G/H/I1-1630[»]
1XI5electron microscopy12.00A/B/C/D/E/F/G/H/I1-1630[»]
3GC3X-ray2.20B1-363[»]
3GD1X-ray3.50I1-363[»]
3IYVelectron microscopy7.90A/B/C/D/E/F/G/H/I1-1630[»]
3LVGX-ray7.94A/B/C1074-1675[»]
3LVHX-ray9.00A/B/C1074-1675[»]
3QILX-ray3.92A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T/U/V/W/X1521-1624[»]
ProteinModelPortaliP49951.
SMRiP49951. Positions 1-493, 1182-1516.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP49951.

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 chainAdd
BLAST
Regioni1550 – 1675126TrimerizationAdd
BLAST

Domaini

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.
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 (By similarity).By similarity

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.
HOVERGENiHBG005344.
InParanoidiP49951.
KOiK04646.

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.

P49951 [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 ICVQVASKYH EQLSTQSLIE
710 720 730 740 750
LFESFKSFEG LFYFLGSIVN FSQDPDVHFK YIQAACKTGQ IKEVERICRE
760 770 780 790 800
SNCYDPERVK NFLKEAKLTD QLPLIIVCDR FDFVHDLVLY LYRNNLQKYI
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
VELYYRAIQF YLEFKPLLLN DLLMVLSPRL DHTRAVNYFS 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 APAYGQPQPG FGYSM
Length:1,675
Mass (Da):191,589
Last modified:October 1, 1996 - v1
Checksum:i6C4F2D54801579E2
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U31757 mRNA. Translation: AAC48524.1.
RefSeqiNP_776448.1. NM_174023.2.
UniGeneiBt.44506.

Genome annotation databases

GeneIDi281080.
KEGGibta:281080.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U31757 mRNA. Translation: AAC48524.1 .
RefSeqi NP_776448.1. NM_174023.2.
UniGenei Bt.44506.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1B89 X-ray 2.60 A 1074-1522 [» ]
1UTC X-ray 2.30 A/B 1-363 [» ]
1XI4 electron microscopy 7.90 A/B/C/D/E/F/G/H/I 1-1630 [» ]
1XI5 electron microscopy 12.00 A/B/C/D/E/F/G/H/I 1-1630 [» ]
3GC3 X-ray 2.20 B 1-363 [» ]
3GD1 X-ray 3.50 I 1-363 [» ]
3IYV electron microscopy 7.90 A/B/C/D/E/F/G/H/I 1-1630 [» ]
3LVG X-ray 7.94 A/B/C 1074-1675 [» ]
3LVH X-ray 9.00 A/B/C 1074-1675 [» ]
3QIL X-ray 3.92 A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T/U/V/W/X 1521-1624 [» ]
ProteinModelPortali P49951.
SMRi P49951. Positions 1-493, 1182-1516.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 158448. 1 interaction.
IntActi P49951. 7 interactions.
MINTi MINT-122490.
STRINGi 9913.ENSBTAP00000022210.

Proteomic databases

PaxDbi P49951.
PRIDEi P49951.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 281080.
KEGGi bta:281080.

Organism-specific databases

CTDi 1213.

Phylogenomic databases

eggNOGi NOG314149.
HOVERGENi HBG005344.
InParanoidi P49951.
KOi K04646.

Miscellaneous databases

EvolutionaryTracei P49951.
NextBioi 20805158.

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. "Regulation of clathrin assembly and trimerization defined using recombinant triskelion hubs."
    Liu S.-H., Wong M.L., Craik C.S., Brodsky F.M.
    Cell 83:257-267(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Kidney.
  2. "The connecdenn family, Rab35 guanine nucleotide exchange factors interfacing with the clathrin machinery."
    Marat A.L., McPherson P.S.
    J. Biol. Chem. 285:10627-10637(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH DENND1A; DENND1B AND DENND1C.

Entry informationi

Entry nameiCLH1_BOVIN
AccessioniPrimary (citable) accession number: P49951
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: October 29, 2014
This is version 110 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, 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