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P49951

- CLH1_BOVIN

UniProt

P49951 - CLH1_BOVIN

Protein

Clathrin heavy chain 1

Gene

CLTC

Organism
Bos taurus (Bovine)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 109 (01 Oct 2014)
      Sequence version 1 (01 Oct 1996)
      Previous versions | rss
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    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. identical protein binding Source: IntAct
    2. 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

    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. melanosome Source: UniProtKB-SubCell
    4. membrane coat Source: AgBase
    5. mitochondrion Source: AgBase

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

    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.
    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.
    [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.

    P49951-1 [UniParc]FASTAAdd to Basket

    « Hide

    MAQILPIRFQ EHLQLQNLGI NPANIGFSTL TMESDKFICI REKVGEQAQV     50
    VIIDMNDPSN PIRRPISADS AIMNPASKVI ALKAGKTLQI FNIEMKSKMK 100
    AHTMTDDVTF WKWISLNTVA LVTDNAVYHW SMEGESQPVK MFDRHSSLAG 150
    CQIINYRTDA KQKWLLLTGI SAQQNRVVGA MQLYSVDRKV SQPIEGHAAS 200
    FAQFKMEGNA EESTLFCFAV RGQAGGKLHI IEVGTPPTGN QPFPKKAVDV 250
    FFPPEAQNDF PVAMQISEKH DVVFLITKYG YIHLYDLETG TCIYMNRISG 300
    ETIFVTAPHE ATAGIIGVNR KGQVLSVCVE EENIIPYITN VLQNPDLALR 350
    MAVRNNLAGA EELFARKFNA LFAQGNYSEA AKVAANAPKG ILRTPDTIRR 400
    FQSVPAQPGQ TSPLLQYFGI LLDQGQLNKY ESLELCRPVL QQGRKQLLEK 450
    WLKEDKLECS EELGDLVKSV DPTLALSVYL RANVPNKVIQ CFAETGQVQK 500
    IVLYAKKVGY TPDWIFLLRN VMRISPDQGQ QFAQMLVQDE EPLADITQIV 550
    DVFMEYNLIQ QCTAFLLDAL KNNRPSEGPL QTRLLEMNLM HAPQVADAIL 600
    GNQMFTHYDR AHIAQLCEKA GLLQRALEHF TDLYDIKRAV VHTHLLNPEW 650
    LVNYFGSLSV EDSLECLRAM LSANIRQNLQ ICVQVASKYH EQLSTQSLIE 700
    LFESFKSFEG LFYFLGSIVN FSQDPDVHFK YIQAACKTGQ IKEVERICRE 750
    SNCYDPERVK NFLKEAKLTD QLPLIIVCDR FDFVHDLVLY LYRNNLQKYI 800
    EIYVQKVNPS RLPVVIGGLL DVDCSEDVIK NLILVVRGQF STDELVAEVE 850
    KRNRLKLLLP WLEARIHEGC EEPATHNALA KIYIDSNNNP ERFLRENPYY 900
    DSRVVGKYCE KRDPHLACVA YERGQCDLEL INVCNENSLF KSLSRYLVRR 950
    KDPELWGSVL LESNPYRRPL IDQVVQTALS ETQDPEEVSV TVKAFMTADL 1000
    PNELIELLEK IVLDNSVFSE HRNLQNLLIL TAIKADRTRV MEYINRLDNY 1050
    DAPDIANIAI SNELFEEAFA IFRKFDVNTS AVQVLIEHIG NLDRAYEFAE 1100
    RCNEPAVWSQ LAKAQLQKGM VKEAIDSYIK ADDPSSYMEV VQAANTSGNW 1150
    EELVKYLQMA RKKARESYVE TELIFALAKT NRLAELEEFI NGPNNAHIQQ 1200
    VGDRCYDEKM YDAAKLLYNN VSNFGRLAST LVHLGEYQAA VDGARKANST 1250
    RTWKEVCFAC VDGKEFRLAQ MCGLHIVVHA DELEELINYY QDRGYFEELI 1300
    TMLEAALGLE RAHMGMFTEL AILYSKFKPQ KMREHLELFW SRVNIPKVLR 1350
    AAEQAHLWAE LVFLYDKYEE YDNAIITMMN HPTDAWKEGQ FKDIITKVAN 1400
    VELYYRAIQF YLEFKPLLLN DLLMVLSPRL DHTRAVNYFS KVKQLPLVKP 1450
    YLRSVQNHNN KSVNESLNNL FITEEDYQAL RTSIDAYDNF DNISLAQRLE 1500
    KHELIEFRRI AAYLFKGNNR WKQSVELCKK DSLYKDAMQY ASESKDTELA 1550
    EELLQWFLQE EKRECFGACL FTCYDLLRPD VVLETAWRHN IMDFAMPYFI 1600
    QVMKEYLTKV DKLDASESLR KEEEQATETQ PIVYGQPQLM LTAGPSVAVP 1650
    PQAPFGYGYT APAYGQPQPG FGYSM 1675
    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.
    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.
    [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 1, 2014
    This is version 109 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