P11442 (CLH_RAT) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Clathrin heavy chain 1

Gene names

Name:

Cltc

Organism

Rattus norvegicus (Rat)

Taxonomic identifier

10116 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus

Protein attributes

Sequence length	1675 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (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 structure	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 By similarity.
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.
Sequence similarities	Belongs to the clathrin heavy chain family.

Ontologies

Keywords
Cellular component	Coated pit Cytoplasmic vesicle Membrane
PTM	Acetylation Phosphoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological process	Golgi organization Inferred from mutant phenotype. Source: RGD intracellular protein transport Inferred from electronic annotation. Source: InterPro mitosis Inferred from mutant phenotype. Source: UniProtKB receptor-mediated endocytosis Inferred from mutant phenotype. Source: UniProtKB
Cellular component	T-tubule Inferred from direct assay. Source: RGD clathrin coat of coated pit Inferred from electronic annotation. Source: InterPro clathrin coat of trans-Golgi network vesicle Inferred from electronic annotation. Source: InterPro clathrin-coated endocytic vesicle membrane Traceable author statement. Source: Reactome melanosome Inferred from electronic annotation. Source: UniProtKB-SubCell membrane fraction Inferred from direct assay. Source: RGD spindle Inferred from direct assay. Source: UniProtKB
Molecular function	ankyrin binding Inferred from direct assay. Source: RGD heat shock protein binding Inferred from direct assay. Source: RGD peptide binding Inferred from direct assay. Source: RGD protein C-terminus binding Inferred from physical interaction. Source: RGD structural molecule activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

1

1

Removed Ref.2

Chain

2 – 1675

1674

Clathrin heavy chain 1

PRO_0000205780

Regions

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 By similarity

Region

1550 – 1675

126

Trimerization By similarity

Amino acid modifications

Modified residue

2

1

N-acetylalanine Ref.2

Modified residue

184

1

Phosphotyrosine By similarity

Modified residue

394

1

Phosphothreonine By similarity

Modified residue

634

1

Phosphotyrosine By similarity

Modified residue

899

1

Phosphotyrosine By similarity

Modified residue

1206

1

Phosphotyrosine By similarity

Modified residue

1477

1

Phosphotyrosine By similarity

Modified residue

1487

1

Phosphotyrosine By similarity

Modified residue

1494

1

Phosphoserine By similarity

Secondary structure

1

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1675

Helix Strand Turn

Details...

Beta strand

7 – 14

8

Helix

15 – 18

4

Turn

27 – 29

3

Beta strand

30 – 34

5

Beta strand

37 – 42

6

Beta strand

49 – 54

6

Beta strand

62 – 65

4

Beta strand

71 – 73

3

Beta strand

75 – 78

4

Beta strand

80 – 84

5

Beta strand

87 – 92

6

Turn

93 – 96

4

Beta strand

97 – 103

7

Beta strand

110 – 115

6

Beta strand

118 – 122

5

Beta strand

124 – 135

12

Beta strand

139 – 143

5

Helix

146 – 148

3

Beta strand

152 – 158

7

Beta strand

162 – 173

12

Beta strand

176 – 186

11

Beta strand

191 – 194

4

Beta strand

197 – 205

9

Beta strand

210 – 220

11

Beta strand

227 – 232

6

Beta strand

246 – 249

4

Beta strand

261 – 267

7

Turn

268 – 271

4

Beta strand

272 – 277

6

Beta strand

280 – 286

7

Turn

287 – 289

3

Beta strand

292 – 297

6

Beta strand

303 – 309

7

Turn

310 – 313

4

Beta strand

314 – 319

6

Beta strand

323 – 329

7

Turn

331 – 333

3

Helix

334 – 340

7

Helix

345 – 354

10

Helix

361 – 373

13

Helix

377 – 386

10

Helix

388 – 390

3

Helix

395 – 401

7

Helix

413 – 424

12

Helix

429 – 441

13

Helix

445 – 454

10

Helix

461 – 470

10

Helix

473 – 482

10

Sequences

	Sequence		Length	Mass (Da)
	P11442 [UniParc]. Last modified January 23, 2007. Version 3. Checksum: C10F54C7ED8C5A61	FASTA	1,675	191,599
	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 IWVQVASKYH EQLSTQSLIE LFESFKSFEG LFYFLGSIVN 730 740 750 760 770 780 FSQDPDVHFK YIQAACKTGQ IKEVERICRE SNCYDPERVK NFLKEAKLTD QLPLIIVCDR 790 800 810 820 830 840 FDFVHDLVLY LYRNSLQKYI 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 VELYYKAIQF YLEFKPLLLN DLLMVLSPRL AHTRAVNYFS 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 APPYGQPQPG FGYSM

References

[1]	"Clathrin heavy chain: molecular cloning and complete primary structure." Kirchhausen T., Harrison S.C., Chow E.P., Mattaliano R.J., Ramachandran K.L., Smart J., Brosius J. Proc. Natl. Acad. Sci. U.S.A. 84:8805-8809(1987) [PubMed: 3480512] [Abstract] 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, 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: 9827808] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 1-493.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

J03583 mRNA. Translation: AAA40874.1.

IPI

IPI00193983.

PIR

LRRTH. A39941.

RefSeq

NP_062172.1. NM_019299.1.

UniGene

Rn.3589.

3D structure databases

PDBe
RCSB PDB
PDBj

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	[»]

ProteinModelPortal

P11442.

SMR

P11442. Positions 1-493, 1182-1516.

ModBase

Search...

Protein-protein interaction databases

IntAct

P11442. 1 interaction.

MINT

MINT-93121.

STRING

P11442.

PTM databases

PhosphoSite

P11442.

2D gel databases

World-2DPAGE

0004:P11442.

Proteomic databases

PRIDE

P11442.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

GeneID

54241.

KEGG

rno:54241.

UCSC

NM_019299. rat.

Organism-specific databases

CTD

1213.

RGD

2364. Cltc.

Phylogenomic databases

eggNOG

roNOG05981.

GeneTree

ENSGT00400000022107.

HOVERGEN

HBG005344.

PhylomeDB

P11442.

Enzyme and pathway databases

Reactome

REACT_111984. Signal Transduction.

Gene expression databases

ArrayExpress

P11442.

Genevestigator

P11442.

GermOnline

ENSRNOG00000004291. Rattus norvegicus.

Family and domain databases

InterPro

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]

Gene3D

G3DSA:2.130.10.110. Clathrin_H-chain_link/propller. 1 hit.
G3DSA:1.25.40.10. TPR-like_helical. 3 hits.

KO

K04646.

Pfam

PF00637. Clathrin. 7 hits.
PF09268. Clathrin-link. 1 hit.
PF01394. Clathrin_propel. 3 hits.
[Graphical view]

PIRSF

PIRSF002290. Clathrin_H_chain. 1 hit.

SMART

SM00299. CLH. 7 hits.
[Graphical view]

SUPFAM

SSF48371. ARM-type_fold. 5 hits.
SSF50989. Clathrin_H-chain_propeller_N. 1 hit.

ProtoNet

Search...

Other

NextBio

610700.

Entry information

Entry name

CLH_RAT

Accession

Primary (citable) accession number: P11442

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1989
Last sequence update:	January 23, 2007
Last modified:	November 16, 2011
This is version 101 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program