LOCUS       NP_004850               1675 aa            linear   PRI 28-APR-2025
DEFINITION  clathrin heavy chain 1 isoform 1 [Homo sapiens].
ACCESSION   NP_004850
VERSION     NP_004850.1
DBSOURCE    REFSEQ: accession NM_004859.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1675)
  AUTHORS   Crowley,H.M., Georgantzoglou,N., Tse,J.Y., Williams,E.A.,
            Mata,D.A., Martin,S.S., Guitart,J., Bridge,J.A. and Linos,K.
  TITLE     Expanding Our Knowledge of Molecular Pathogenesis in Histiocytoses:
            Solitary Soft Tissue Histiocytomas in Children With a Novel
            CLTC::SYK Fusion
  JOURNAL   Am J Surg Pathol 47 (10), 1108-1115 (2023)
   PUBMED   37522373
  REMARK    GeneRIF: Expanding Our Knowledge of Molecular Pathogenesis in
            Histiocytoses: Solitary Soft Tissue Histiocytomas in Children With
            a Novel CLTC::SYK Fusion.
REFERENCE   2  (residues 1 to 1675)
  AUTHORS   Liu,T., Li,J., Wang,X., Huang,T., Wu,W., Li,A., Li,C., Huang,X.,
            Wang,Q., Li,D., Wang,S. and Liang,M.
  TITLE     Knockout of CLTC gene reduces but not completely block SFTSV
            infection
  JOURNAL   PLoS One 18 (8), e0285673 (2023)
   PUBMED   37624798
  REMARK    GeneRIF: Knockout of CLTC gene reduces but not completely block
            SFTSV infection.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 1675)
  AUTHORS   Kliche,J., Garvanska,D.H., Simonetti,L., Badgujar,D.,
            Dobritzsch,D., Nilsson,J., Davey,N.E. and Ivarsson,Y.
  TITLE     Large-scale phosphomimetic screening identifies phospho-modulated
            motif-based protein interactions
  JOURNAL   Mol Syst Biol 19 (7), e11164 (2023)
   PUBMED   37219487
REFERENCE   4  (residues 1 to 1675)
  AUTHORS   Mihalic,F., Simonetti,L., Giudice,G., Sander,M.R., Lindqvist,R.,
            Peters,M.B.A., Benz,C., Kassa,E., Badgujar,D., Inturi,R., Ali,M.,
            Krystkowiak,I., Sayadi,A., Andersson,E., Aronsson,H., Soderberg,O.,
            Dobritzsch,D., Petsalaki,E., Overby,A.K., Jemth,P., Davey,N.E. and
            Ivarsson,Y.
  TITLE     Large-scale phage-based screening reveals extensive pan-viral
            mimicry of host short linear motifs
  JOURNAL   Nat Commun 14 (1), 2409 (2023)
   PUBMED   37100772
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 1675)
  AUTHORS   Georgantzoglou,N., Green,D., Winnick,K.N., Sumegi,J.,
            Charville,G.W., Bridge,J.A. and Linos,K.
  TITLE     Molecular investigation of ALK-rearranged epithelioid fibrous
            histiocytomas identifies CLTC as a novel fusion partner and
            evidence of fusion-independent transcription activation
  JOURNAL   Genes Chromosomes Cancer 61 (8), 471-480 (2022)
   PUBMED   35289445
  REMARK    GeneRIF: Molecular investigation of ALK-rearranged epithelioid
            fibrous histiocytomas identifies CLTC as a novel fusion partner and
            evidence of fusion-independent transcription activation.
REFERENCE   6  (residues 1 to 1675)
  AUTHORS   Murphy,J.E. and Keen,J.H.
  TITLE     Recognition sites for clathrin-associated proteins AP-2 and AP-3 on
            clathrin triskelia
  JOURNAL   J Biol Chem 267 (15), 10850-10855 (1992)
   PUBMED   1587861
REFERENCE   7  (residues 1 to 1675)
  AUTHORS   Dodge,G.R., Kovalszky,I., McBride,O.W., Yi,H.F., Chu,M.L.,
            Saitta,B., Stokes,D.G. and Iozzo,R.V.
  TITLE     Human clathrin heavy chain (CLTC): partial molecular cloning,
            expression, and mapping of the gene to human chromosome 17q11-qter
  JOURNAL   Genomics 11 (1), 174-178 (1991)
   PUBMED   1765375
REFERENCE   8  (residues 1 to 1675)
  AUTHORS   Scarmato,P. and Kirchhausen,T.
  TITLE     Analysis of clathrin light chain-heavy chain interactions using
            truncated mutants of rat liver light chain LCB3
  JOURNAL   J Biol Chem 265 (7), 3661-3668 (1990)
   PUBMED   2406259
REFERENCE   9  (residues 1 to 1675)
  AUTHORS   Corvera,S.
  TITLE     Insulin stimulates the assembly of cytosolic clathrin onto
            adipocyte plasma membranes
  JOURNAL   J Biol Chem 265 (5), 2413-2416 (1990)
   PUBMED   2154445
REFERENCE   10 (residues 1 to 1675)
  AUTHORS   Brodsky,F.M.
  TITLE     Clathrin structure characterized with monoclonal antibodies. II.
            Identification of in vivo forms of clathrin
  JOURNAL   J Cell Biol 101 (6), 2055-2062 (1985)
   PUBMED   4066749
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC091271.8 and BC054489.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            Summary:  Clathrin is a major protein component of the cytoplasmic
            face of intracellular organelles, called coated vesicles and coated
            pits. These specialized organelles are involved in the
            intracellular trafficking of receptors and endocytosis of a variety
            of macromolecules.  The basic subunit of the clathrin coat is
            composed of three heavy chains and three light chains. [provided by
            RefSeq, Jul 2008].
            
            Transcript Variant: This variant (1) represents the shorter
            transcript and encodes the shorter protein (isoform 1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803612.78622.1,
                                           SRR1803612.8414.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000269122.8/ ENSP00000269122.3
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1675
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="17"
                     /map="17q23.1"
     Protein         1..1675
                     /product="clathrin heavy chain 1 isoform 1"
                     /note="clathrin, heavy polypeptide-like 2; clathrin, heavy
                     polypeptide (Hc); clathrin heavy chain 1; clathrin heavy
                     chain on chromosome 17"
                     /calculated_mol_wt=191484
     Region          2..479
                     /region_name="Globular terminal domain"
                     /note="propagated from UniProtKB/Swiss-Prot (Q00610.5)"
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine. /evidence=ECO:0000269|Ref.7,
                     ECO:0007744|PubMed:22223895, ECO:0007744|PubMed:22814378,
                     ECO:0007744|PubMed:25944712; propagated from
                     UniProtKB/Swiss-Prot (Q00610.5)"
     Region          19..56
                     /region_name="Clathrin_propel"
                     /note="Clathrin propeller repeat; pfam01394"
                     /db_xref="CDD:460192"
     Region          24..67
                     /region_name="WD40-like repeat 1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q00610.5)"
     Site            67
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q00610.5)"
     Region          68..107
                     /region_name="WD40-like repeat 2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q00610.5)"
     Site            105
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q68FD5; propagated from
                     UniProtKB/Swiss-Prot (Q00610.5)"
     Region          108..149
                     /region_name="WD40-like repeat 3"
                     /note="propagated from UniProtKB/Swiss-Prot (Q00610.5)"
     Region          148..187
                     /region_name="Clathrin_propel"
                     /note="Clathrin propeller repeat; pfam01394"
                     /db_xref="CDD:460192"
     Region          150..195
                     /region_name="WD40-like repeat 4"
                     /note="propagated from UniProtKB/Swiss-Prot (Q00610.5)"
     Site            184
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:Q68FD5; propagated from
                     UniProtKB/Swiss-Prot (Q00610.5)"
     Region          196..257
                     /region_name="WD40-like repeat 5"
                     /note="propagated from UniProtKB/Swiss-Prot (Q00610.5)"
     Region          198..234
                     /region_name="Clathrin_propel"
                     /note="Clathrin propeller repeat; pfam01394"
                     /db_xref="CDD:460192"
     Region          256..288
                     /region_name="Clathrin_propel"
                     /note="Clathrin propeller repeat; pfam01394"
                     /db_xref="CDD:460192"
     Region          258..301
                     /region_name="WD40-like repeat 6"
                     /note="propagated from UniProtKB/Swiss-Prot (Q00610.5)"
     Region          296..330
                     /region_name="Clathrin_propel"
                     /note="Clathrin propeller repeat; pfam01394"
                     /db_xref="CDD:460192"
     Region          302..330
                     /region_name="WD40-like repeat 7"
                     /note="propagated from UniProtKB/Swiss-Prot (Q00610.5)"
     Region          331..354
                     /region_name="Clathrin-link"
                     /note="Clathrin, heavy-chain linker; pfam09268"
                     /db_xref="CDD:462732"
     Region          356..421
                     /region_name="Clathrin_H_link"
                     /note="Clathrin-H-link; pfam13838"
                     /db_xref="CDD:463995"
     Site            394
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (Q00610.5)"
     Region          449..465
                     /region_name="Binding site for the uncoating ATPase,
                     involved in lattice disassembly. /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q00610.5)"
     Region          457..507
                     /region_name="Involved in spindle localization and
                     interaction with TACC3.
                     /evidence=ECO:0000269|PubMed:23918938"
                     /note="propagated from UniProtKB/Swiss-Prot (Q00610.5)"
     Region          480..523
                     /region_name="Flexible linker"
                     /note="propagated from UniProtKB/Swiss-Prot (Q00610.5)"
     Region          524..1675
                     /region_name="Heavy chain arm"
                     /note="propagated from UniProtKB/Swiss-Prot (Q00610.5)"
     Region          524..634
                     /region_name="Distal segment"
                     /note="propagated from UniProtKB/Swiss-Prot (Q00610.5)"
     Region          541..674
                     /region_name="CLH"
                     /note="Clathrin heavy chain repeat homology; smart00299"
                     /db_xref="CDD:128594"
     Site            634
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (Q00610.5)"
     Region          639..1675
                     /region_name="Proximal segment"
                     /note="propagated from UniProtKB/Swiss-Prot (Q00610.5)"
     Region          686..824
                     /region_name="CLH"
                     /note="Clathrin heavy chain repeat homology; smart00299"
                     /db_xref="CDD:128594"
     Region          833..968
                     /region_name="CLH"
                     /note="Clathrin heavy chain repeat homology; smart00299"
                     /db_xref="CDD:128594"
     Site            856
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (Q00610.5)"
     Site            899
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:Q68FD5; propagated from
                     UniProtKB/Swiss-Prot (Q00610.5)"
     Region          979..1118
                     /region_name="CLH"
                     /note="Clathrin heavy chain repeat homology; smart00299"
                     /db_xref="CDD:128594"
     Region          1105..1131
                     /region_name="TPR repeat"
                     /note="TPR repeat [structural motif]"
                     /db_xref="CDD:276809"
     Region          1128..1265
                     /region_name="CLH"
                     /note="Clathrin heavy chain repeat homology; smart00299"
                     /db_xref="CDD:128594"
     Site            1167
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q68FD5; propagated from
                     UniProtKB/Swiss-Prot (Q00610.5)"
     Site            1206
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:Q68FD5; propagated from
                     UniProtKB/Swiss-Prot (Q00610.5)"
     Region          1213..1522
                     /region_name="Involved in binding clathrin light chain.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q00610.5)"
     Site            1229
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q00610.5)"
     Region          1274..1416
                     /region_name="CLH"
                     /note="Clathrin heavy chain repeat homology; smart00299"
                     /db_xref="CDD:128594"
     Region          1427..1564
                     /region_name="Clathrin"
                     /note="Region in Clathrin and VPS; pfam00637"
                     /db_xref="CDD:459884"
     Site            1441
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (Q00610.5)"
     Site            1477
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0007744|PubMed:19690332; propagated from
                     UniProtKB/Swiss-Prot (Q00610.5)"
     Site            1487
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:Q68FD5; propagated from
                     UniProtKB/Swiss-Prot (Q00610.5)"
     Site            1494
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19369195,
                     ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569;
                     propagated from UniProtKB/Swiss-Prot (Q00610.5)"
     Site            1501
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (Q00610.5)"
     Region          1550..1675
                     /region_name="Trimerization. /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q00610.5)"
     CDS             1..1675
                     /gene="CLTC"
                     /gene_synonym="CHC; CHC17; CLH-17; CLTCL2; Hc; MRD56"
                     /coded_by="NM_004859.4:238..5265"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS32696.1"
                     /db_xref="GeneID:1213"
                     /db_xref="HGNC:HGNC:2092"
                     /db_xref="MIM:118955"
ORIGIN      
        1 maqilpirfq ehlqlqnlgi npanigfstl tmesdkfici rekvgeqaqv viidmndpsn
       61 pirrpisads aimnpaskvi alkagktlqi fniemkskmk ahtmtddvtf wkwislntva
      121 lvtdnavyhw smegesqpvk mfdrhsslag cqiinyrtda kqkwllltgi saqqnrvvga
      181 mqlysvdrkv sqpieghaas faqfkmegna eestlfcfav rgqaggklhi ievgtpptgn
      241 qpfpkkavdv ffppeaqndf pvamqisekh dvvflitkyg yihlydletg tciymnrisg
      301 etifvtaphe atagiigvnr kgqvlsvcve eeniipyitn vlqnpdlalr mavrnnlaga
      361 eelfarkfna lfaqgnysea akvaanapkg ilrtpdtirr fqsvpaqpgq tspllqyfgi
      421 lldqgqlnky eslelcrpvl qqgrkqllek wlkedklecs eelgdlvksv dptlalsvyl
      481 ranvpnkviq cfaetgqvqk ivlyakkvgy tpdwifllrn vmrispdqgq qfaqmlvqde
      541 epladitqiv dvfmeynliq qctaflldal knnrpsegpl qtrllemnlm hapqvadail
      601 gnqmfthydr ahiaqlceka gllqralehf tdlydikrav vhthllnpew lvnyfgslsv
      661 edsleclram lsanirqnlq icvqvaskyh eqlstqslie lfesfksfeg lfyflgsivn
      721 fsqdpdvhfk yiqaacktgq ikevericre sncydpervk nflkeakltd qlpliivcdr
      781 fdfvhdlvly lyrnnlqkyi eiyvqkvnps rlpvviggll dvdcsedvik nlilvvrgqf
      841 stdelvaeve krnrlklllp wlearihegc eepathnala kiyidsnnnp erflrenpyy
      901 dsrvvgkyce krdphlacva yergqcdlel invcnenslf kslsrylvrr kdpelwgsvl
      961 lesnpyrrpl idqvvqtals etqdpeevsv tvkafmtadl pneliellek ivldnsvfse
     1021 hrnlqnllil taikadrtrv meyinrldny dapdianiai snelfeeafa ifrkfdvnts
     1081 avqvliehig nldrayefae rcnepavwsq lakaqlqkgm vkeaidsyik addpssymev
     1141 vqaantsgnw eelvkylqma rkkaresyve telifalakt nrlaeleefi ngpnnahiqq
     1201 vgdrcydekm ydaakllynn vsnfgrlast lvhlgeyqaa vdgarkanst rtwkevcfac
     1261 vdgkefrlaq mcglhivvha deleelinyy qdrgyfeeli tmleaalgle rahmgmftel
     1321 ailyskfkpq kmrehlelfw srvnipkvlr aaeqahlwae lvflydkyee ydnaiitmmn
     1381 hptdawkegq fkdiitkvan velyyraiqf ylefkpllln dllmvlsprl dhtravnyfs
     1441 kvkqlplvkp ylrsvqnhnn ksvneslnnl fiteedyqal rtsidaydnf dnislaqrle
     1501 kheliefrri aaylfkgnnr wkqsvelckk dslykdamqy aseskdtela eellqwflqe
     1561 ekrecfgacl ftcydllrpd vvletawrhn imdfampyfi qvmkeyltkv dkldaseslr
     1621 keeeqatetq pivygqpqlm ltagpsvavp pqapfgygyt appygqpqpg fgysm
//
