Full text data of CLTCL1
CLTCL1
(CLH22, CLTCL, CLTD)
[Confidence: low (only semi-automatic identification from reviews)]
Clathrin heavy chain 2 (Clathrin heavy chain on chromosome 22; CLH-22)
Clathrin heavy chain 2 (Clathrin heavy chain on chromosome 22; CLH-22)
UniProt
P53675
ID CLH2_HUMAN Reviewed; 1640 AA.
AC P53675; B7Z7U5; Q14017; Q15808; Q15809;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-NOV-1997, sequence version 2.
DT 22-JAN-2014, entry version 125.
DE RecName: Full=Clathrin heavy chain 2;
DE AltName: Full=Clathrin heavy chain on chromosome 22;
DE Short=CLH-22;
GN Name=CLTCL1; Synonyms=CLH22, CLTCL, CLTD;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Fetal brain;
RX PubMed=8733128; DOI=10.1093/hmg/5.5.617;
RA Sirotkin H., Morrow B., Dasgupta R., Goldberg R., Patangali S.R.,
RA Shi G., Cannizzaro L., Shprintzen R., Weissman S., Kucherlapati R.;
RT "Isolation of a new clathrin heavy chain gene with muscle-specific
RT expression from the region commonly deleted in velo-cardio-facial
RT syndrome.";
RL Hum. Mol. Genet. 5:617-624(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND NUCLEOTIDE SEQUENCE [MRNA]
RP OF 1451-1640 (ISOFORM 2).
RC TISSUE=Fetal brain, and Skeletal muscle;
RX PubMed=8733129; DOI=10.1093/hmg/5.5.625;
RA Kedra D., Peyrard M., Fransson I., Collins J.E., Dunham I., Roe B.A.,
RA Dumanski J.P.;
RT "Characterization of a second human clathrin heavy chain polypeptide
RT gene (CLH-22) from chromosome 22q11.";
RL Hum. Mol. Genet. 5:625-631(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), AND VARIANT LYS-691.
RX PubMed=8844170; DOI=10.1006/geno.1996.0386;
RA Long K.R., Trofatter J.A., Ramesh V., McCormick M.K., Buckler A.J.;
RT "Cloning and characterization of a novel human clathrin heavy chain
RT gene (CLTCL).";
RL Genomics 35:466-472(1996).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Testis;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
CC -!- FUNCTION: Clathrin is the major protein of the polyhedral coat of
CC coated pits and vesicles. Two different adapter protein complexes
CC link the clathrin lattice either to the plasma membrane or to the
CC trans-Golgi network (By similarity).
CC -!- SUBUNIT: Clathrin triskelions, composed of 3 heavy chains and 3
CC light chains, are the basic subunits of the clathrin coat. In the
CC presence of light chains, hub assembly is influenced by both the
CC pH and the concentration of calcium (By similarity). May interact
CC with OCRL (By similarity).
CC -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle membrane; Peripheral
CC membrane protein; Cytoplasmic side (By similarity). Membrane,
CC coated pit; Peripheral membrane protein; Cytoplasmic side (By
CC similarity). Note=Cytoplasmic face of coated pits and vesicles (By
CC similarity).
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1; Synonyms=Long, Brain;
CC IsoId=P53675-1; Sequence=Displayed;
CC Name=2; Synonyms=Short, Muscle;
CC IsoId=P53675-2; Sequence=VSP_001100;
CC -!- TISSUE SPECIFICITY: Maximal levels in skeletal muscle. High levels
CC in heart and testis. Low expression detected in all other tissues.
CC -!- DOMAIN: The C-terminal third of the heavy chains forms the hub of
CC the triskelion. This region contains the trimerization domain and
CC the light-chain binding domain involved in the assembly of the
CC clathrin lattice.
CC -!- DOMAIN: The N-terminal seven-bladed beta-propeller is formed by
CC WD40-like repeats, and projects inward from the polyhedral outer
CC clathrin coat. It consitutes a major protein-protein interaction
CC node (By similarity).
CC -!- SIMILARITY: Belongs to the clathrin heavy chain family.
CC -!- SIMILARITY: Contains 7 CHCR (clathrin heavy-chain) repeats.
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
CC and Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/CLTCL1ID361.html";
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DR EMBL; U41763; AAC50494.1; -; mRNA.
DR EMBL; X95486; CAA64752.1; -; mRNA.
DR EMBL; X95487; CAA64753.1; -; mRNA.
DR EMBL; U60802; AAB40908.1; -; mRNA.
DR EMBL; U60803; AAB40909.1; -; mRNA.
DR EMBL; AK302506; BAH13731.1; -; mRNA.
DR EMBL; CH471176; EAX03047.1; -; Genomic_DNA.
DR PIR; G02757; G02757.
DR PIR; T09522; T09522.
DR RefSeq; NP_001826.3; NM_001835.3.
DR RefSeq; NP_009029.3; NM_007098.3.
DR RefSeq; XP_005261336.1; XM_005261279.1.
DR UniGene; Hs.368266; -.
DR ProteinModelPortal; P53675; -.
DR SMR; P53675; 1-493, 1077-1628.
DR IntAct; P53675; 9.
DR MINT; MINT-208273; -.
DR STRING; 9606.ENSP00000263200; -.
DR PhosphoSite; P53675; -.
DR DMDM; 2506298; -.
DR PaxDb; P53675; -.
DR PRIDE; P53675; -.
DR DNASU; 8218; -.
DR Ensembl; ENST00000263200; ENSP00000445677; ENSG00000070371.
DR Ensembl; ENST00000353891; ENSP00000439662; ENSG00000070371.
DR Ensembl; ENST00000427926; ENSP00000441158; ENSG00000070371.
DR GeneID; 8218; -.
DR KEGG; hsa:8218; -.
DR UCSC; uc011agw.1; human.
DR CTD; 8218; -.
DR GeneCards; GC22M019171; -.
DR H-InvDB; HIX0016234; -.
DR HGNC; HGNC:2093; CLTCL1.
DR HPA; HPA041110; -.
DR MIM; 601273; gene.
DR neXtProt; NX_P53675; -.
DR PharmGKB; PA26619; -.
DR eggNOG; NOG314149; -.
DR HOGENOM; HOG000188877; -.
DR HOVERGEN; HBG005344; -.
DR InParanoid; P53675; -.
DR KO; K04646; -.
DR OMA; HESYIET; -.
DR OrthoDB; EOG7Z0JVM; -.
DR PhylomeDB; P53675; -.
DR Reactome; REACT_11123; Membrane Trafficking.
DR ChiTaRS; CLTCL1; human.
DR GenomeRNAi; 8218; -.
DR NextBio; 30943; -.
DR PRO; PR:P53675; -.
DR ArrayExpress; P53675; -.
DR Bgee; P53675; -.
DR CleanEx; HS_CLTCL1; -.
DR Genevestigator; P53675; -.
DR GO; GO:0030132; C:clathrin coat of coated pit; IEA:InterPro.
DR GO; GO:0030130; C:clathrin coat of trans-Golgi network vesicle; IEA:InterPro.
DR GO; GO:0030136; C:clathrin-coated vesicle; IDA:UniProtKB.
DR GO; GO:0005905; C:coated pit; IDA:UniProtKB.
DR GO; GO:0005819; C:spindle; IDA:UniProtKB.
DR GO; GO:0005802; C:trans-Golgi network; IDA:UniProtKB.
DR GO; GO:0004871; F:signal transducer activity; TAS:ProtInc.
DR GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
DR GO; GO:0009653; P:anatomical structure morphogenesis; TAS:ProtInc.
DR GO; GO:0006886; P:intracellular protein transport; IEA:InterPro.
DR GO; GO:0007067; P:mitosis; IDA:UniProtKB.
DR GO; GO:0046326; P:positive regulation of glucose import; IMP:UniProtKB.
DR GO; GO:0006898; P:receptor-mediated endocytosis; IDA:UniProtKB.
DR Gene3D; 1.25.40.10; -; 3.
DR Gene3D; 2.130.10.110; -; 1.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR000547; Clathrin_H-chain/VPS_repeat.
DR InterPro; IPR016025; Clathrin_H-chain_link/propller.
DR InterPro; IPR015348; Clathrin_H-chain_linker_core.
DR InterPro; IPR001473; Clathrin_H-chain_propeller_N.
DR InterPro; IPR022365; Clathrin_H-chain_propeller_rpt.
DR InterPro; IPR016341; Clathrin_heavy_chain.
DR InterPro; IPR011990; TPR-like_helical.
DR Pfam; PF00637; Clathrin; 7.
DR Pfam; PF09268; Clathrin-link; 1.
DR Pfam; PF01394; Clathrin_propel; 2.
DR PIRSF; PIRSF002290; Clathrin_H_chain; 1.
DR SMART; SM00299; CLH; 7.
DR SUPFAM; SSF48371; SSF48371; 6.
DR SUPFAM; SSF50989; SSF50989; 1.
DR PROSITE; PS50236; CHCR; 7.
PE 1: Evidence at protein level;
KW Alternative splicing; Coated pit; Complete proteome;
KW Cytoplasmic vesicle; Membrane; Polymorphism; Reference proteome;
KW Repeat.
FT CHAIN 1 1640 Clathrin heavy chain 2.
FT /FTId=PRO_0000205786.
FT REPEAT 537 683 CHCR 1.
FT REPEAT 686 828 CHCR 2.
FT REPEAT 833 972 CHCR 3.
FT REPEAT 979 1124 CHCR 4.
FT REPEAT 1128 1269 CHCR 5.
FT REPEAT 1274 1420 CHCR 6.
FT REPEAT 1423 1566 CHCR 7.
FT REGION 1 479 Globular terminal domain.
FT REGION 24 67 WD40-like repeat 1.
FT REGION 68 107 WD40-like repeat 2.
FT REGION 108 149 WD40-like repeat 3.
FT REGION 150 195 WD40-like repeat 4.
FT REGION 196 257 WD40-like repeat 5.
FT REGION 258 301 WD40-like repeat 6.
FT REGION 302 330 WD40-like repeat 7.
FT REGION 449 465 Binding site for the uncoating ATPase,
FT involved in lattice disassembly
FT (Potential).
FT REGION 480 523 Flexible linker.
FT REGION 524 1640 Heavy chain arm.
FT REGION 524 634 Distal segment.
FT REGION 639 1640 Proximal segment.
FT REGION 1213 1522 Involved in binding clathrin light chain
FT (By similarity).
FT REGION 1551 1640 Trimerization (By similarity).
FT VAR_SEQ 1479 1535 Missing (in isoform 2).
FT /FTId=VSP_001100.
FT VARIANT 61 61 P -> L (in dbSNP:rs3747059).
FT /FTId=VAR_055653.
FT VARIANT 205 205 K -> R (in dbSNP:rs5746697).
FT /FTId=VAR_055654.
FT VARIANT 279 279 Y -> C (in dbSNP:rs807459).
FT /FTId=VAR_055655.
FT VARIANT 691 691 E -> K (in dbSNP:rs1060374).
FT /FTId=VAR_055656.
FT VARIANT 941 941 K -> R (in dbSNP:rs35398725).
FT /FTId=VAR_055657.
FT VARIANT 945 945 R -> H (in dbSNP:rs36077768).
FT /FTId=VAR_055658.
FT VARIANT 1046 1046 R -> C (in dbSNP:rs712952).
FT /FTId=VAR_055659.
FT VARIANT 1195 1195 N -> S (in dbSNP:rs807547).
FT /FTId=VAR_059214.
FT VARIANT 1316 1316 M -> V (in dbSNP:rs1061325).
FT /FTId=VAR_059215.
FT VARIANT 1394 1394 I -> T (in dbSNP:rs1633399).
FT /FTId=VAR_059216.
FT VARIANT 1592 1592 V -> M (in dbSNP:rs2073738).
FT /FTId=VAR_059217.
FT VARIANT 1620 1620 R -> H (in dbSNP:rs5748024).
FT /FTId=VAR_059218.
FT CONFLICT 193 193 P -> H (in Ref. 1; AAC50494).
FT CONFLICT 215 215 L -> H (in Ref. 1; AAC50494).
FT CONFLICT 320 320 K -> T (in Ref. 2; CAA64752).
FT CONFLICT 530 530 L -> Q (in Ref. 1; AAC50494).
FT CONFLICT 1474 1474 E -> K (in Ref. 3; AAB40908/AAB40909).
FT CONFLICT 1620 1640 RKQEEHVTEPAPLVFDFDGHE -> PPSKRSM (in Ref.
FT 3; AAB40908/AAB40909).
SQ SEQUENCE 1640 AA; 187030 MW; C661E1AB989D8E7F CRC64;
MAQILPVRFQ EHFQLQNLGI NPANIGFSTL TMESDKFICI REKVGEQAQV TIIDMSDPMA
PIRRPISAES AIMNPASKVI ALKAGKTLQI FNIEMKSKMK AHTMAEEVIF WKWVSVNTVA
LVTETAVYHW SMEGDSQPMK MFDRHTSLVG CQVIHYRTDE YQKWLLLVGI SAQQNRVVGA
MQLYSVDRKV SQPIEGHAAA FAEFKMEGNA KPATLFCFAV RNPTGGKLHI IEVGQPAAGN
QPFVKKAVDV FFPPEAQNDF PVAMQIGAKH GVIYLITKYG YLHLYDLESG VCICMNRISA
DTIFVTAPHK PTSGIIGVNK KGQVLSVCVE EDNIVNYATN VLQNPDLGLR LAVRSNLAGA
EKLFVRKFNT LFAQGSYAEA AKVAASAPKG ILRTRETVQK FQSIPAQSGQ ASPLLQYFGI
LLDQGQLNKL ESLELCHLVL QQGRKQLLEK WLKEDKLECS EELGDLVKTT DPMLALSVYL
RANVPSKVIQ CFAETGQFQK IVLYAKKVGY TPDWIFLLRG VMKISPEQGL QFSRMLVQDE
EPLANISQIV DIFMENSLIQ QCTSFLLDAL KNNRPAEGLL QTWLLEMNLV HAPQVADAIL
GNKMFTHYDR AHIAQLCEKA GLLQQALEHY TDLYDIKRAV VHTHLLNPEW LVNFFGSLSV
EDSVECLHAM LSANIRQNLQ LCVQVASKYH EQLGTQALVE LFESFKSYKG LFYFLGSIVN
FSQDPDVHLK YIQAACKTGQ IKEVERICRE SSCYNPERVK NFLKEAKLTD QLPLIIVCDR
FGFVHDLVLY LYRNNLQRYI EIYVQKVNPS RTPAVIGGLL DVDCSEEVIK HLIMAVRGQF
STDELVAEVE KRNRLKLLLP WLESQIQEGC EEPATHNALA KIYIDSNNSP ECFLRENAYY
DSSVVGRYCE KRDPHLACVA YERGQCDLEL IKVCNENSLF KSEARYLVCR KDPELWAHVL
EETNPSRRQL IDQVVQTALS ETRDPEEISV TVKAFMTADL PNELIELLEK IVLDNSVFSE
HRNLQNLLIL TAIKADRTRV MEYISRLDNY DALDIASIAV SSALYEEAFT VFHKFDMNAS
AIQVLIEHIG NLDRAYEFAE RCNEPAVWSQ LAQAQLQKDL VKEAINSYIR GDDPSSYLEV
VQSASRSNNW EDLVKFLQMA RKKGRESYIE TELIFALAKT SRVSELEDFI NGPNNAHIQQ
VGDRCYEEGM YEAAKLLYSN VSNFARLAST LVHLGEYQAA VDNSRKASST RTWKEVCFAC
MDGQEFRFAQ LCGLHIVIHA DELEELMCYY QDRGYFEELI LLLEAALGLE RAHMGMFTEL
AILYSKFKPQ KMLEHLELFW SRVNIPKVLR AAEQAHLWAE LVFLYDKYEE YDNAVLTMMS
HPTEAWKEGQ FKDIITKVAN VELCYRALQF YLDYKPLLIN DLLLVLSPRL DHTWTVSFFS
KAGQLPLVKP YLRSVQSHNN KSVNEALNHL LTEEEDYQGL RASIDAYDNF DNISLAQQLE
KHQLMEFRCI AAYLYKGNNW WAQSVELCKK DHLYKDAMQH AAESRDAELA QKLLQWFLEE
GKRECFAACL FTCYDLLRPD MVLELAWRHN LVDLAMPYFI QVMREYLSKV DKLDALESLR
KQEEHVTEPA PLVFDFDGHE
//
ID CLH2_HUMAN Reviewed; 1640 AA.
AC P53675; B7Z7U5; Q14017; Q15808; Q15809;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-NOV-1997, sequence version 2.
DT 22-JAN-2014, entry version 125.
DE RecName: Full=Clathrin heavy chain 2;
DE AltName: Full=Clathrin heavy chain on chromosome 22;
DE Short=CLH-22;
GN Name=CLTCL1; Synonyms=CLH22, CLTCL, CLTD;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Fetal brain;
RX PubMed=8733128; DOI=10.1093/hmg/5.5.617;
RA Sirotkin H., Morrow B., Dasgupta R., Goldberg R., Patangali S.R.,
RA Shi G., Cannizzaro L., Shprintzen R., Weissman S., Kucherlapati R.;
RT "Isolation of a new clathrin heavy chain gene with muscle-specific
RT expression from the region commonly deleted in velo-cardio-facial
RT syndrome.";
RL Hum. Mol. Genet. 5:617-624(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND NUCLEOTIDE SEQUENCE [MRNA]
RP OF 1451-1640 (ISOFORM 2).
RC TISSUE=Fetal brain, and Skeletal muscle;
RX PubMed=8733129; DOI=10.1093/hmg/5.5.625;
RA Kedra D., Peyrard M., Fransson I., Collins J.E., Dunham I., Roe B.A.,
RA Dumanski J.P.;
RT "Characterization of a second human clathrin heavy chain polypeptide
RT gene (CLH-22) from chromosome 22q11.";
RL Hum. Mol. Genet. 5:625-631(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), AND VARIANT LYS-691.
RX PubMed=8844170; DOI=10.1006/geno.1996.0386;
RA Long K.R., Trofatter J.A., Ramesh V., McCormick M.K., Buckler A.J.;
RT "Cloning and characterization of a novel human clathrin heavy chain
RT gene (CLTCL).";
RL Genomics 35:466-472(1996).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Testis;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
CC -!- FUNCTION: Clathrin is the major protein of the polyhedral coat of
CC coated pits and vesicles. Two different adapter protein complexes
CC link the clathrin lattice either to the plasma membrane or to the
CC trans-Golgi network (By similarity).
CC -!- SUBUNIT: Clathrin triskelions, composed of 3 heavy chains and 3
CC light chains, are the basic subunits of the clathrin coat. In the
CC presence of light chains, hub assembly is influenced by both the
CC pH and the concentration of calcium (By similarity). May interact
CC with OCRL (By similarity).
CC -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle membrane; Peripheral
CC membrane protein; Cytoplasmic side (By similarity). Membrane,
CC coated pit; Peripheral membrane protein; Cytoplasmic side (By
CC similarity). Note=Cytoplasmic face of coated pits and vesicles (By
CC similarity).
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1; Synonyms=Long, Brain;
CC IsoId=P53675-1; Sequence=Displayed;
CC Name=2; Synonyms=Short, Muscle;
CC IsoId=P53675-2; Sequence=VSP_001100;
CC -!- TISSUE SPECIFICITY: Maximal levels in skeletal muscle. High levels
CC in heart and testis. Low expression detected in all other tissues.
CC -!- DOMAIN: The C-terminal third of the heavy chains forms the hub of
CC the triskelion. This region contains the trimerization domain and
CC the light-chain binding domain involved in the assembly of the
CC clathrin lattice.
CC -!- DOMAIN: The N-terminal seven-bladed beta-propeller is formed by
CC WD40-like repeats, and projects inward from the polyhedral outer
CC clathrin coat. It consitutes a major protein-protein interaction
CC node (By similarity).
CC -!- SIMILARITY: Belongs to the clathrin heavy chain family.
CC -!- SIMILARITY: Contains 7 CHCR (clathrin heavy-chain) repeats.
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
CC and Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/CLTCL1ID361.html";
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
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DR EMBL; U41763; AAC50494.1; -; mRNA.
DR EMBL; X95486; CAA64752.1; -; mRNA.
DR EMBL; X95487; CAA64753.1; -; mRNA.
DR EMBL; U60802; AAB40908.1; -; mRNA.
DR EMBL; U60803; AAB40909.1; -; mRNA.
DR EMBL; AK302506; BAH13731.1; -; mRNA.
DR EMBL; CH471176; EAX03047.1; -; Genomic_DNA.
DR PIR; G02757; G02757.
DR PIR; T09522; T09522.
DR RefSeq; NP_001826.3; NM_001835.3.
DR RefSeq; NP_009029.3; NM_007098.3.
DR RefSeq; XP_005261336.1; XM_005261279.1.
DR UniGene; Hs.368266; -.
DR ProteinModelPortal; P53675; -.
DR SMR; P53675; 1-493, 1077-1628.
DR IntAct; P53675; 9.
DR MINT; MINT-208273; -.
DR STRING; 9606.ENSP00000263200; -.
DR PhosphoSite; P53675; -.
DR DMDM; 2506298; -.
DR PaxDb; P53675; -.
DR PRIDE; P53675; -.
DR DNASU; 8218; -.
DR Ensembl; ENST00000263200; ENSP00000445677; ENSG00000070371.
DR Ensembl; ENST00000353891; ENSP00000439662; ENSG00000070371.
DR Ensembl; ENST00000427926; ENSP00000441158; ENSG00000070371.
DR GeneID; 8218; -.
DR KEGG; hsa:8218; -.
DR UCSC; uc011agw.1; human.
DR CTD; 8218; -.
DR GeneCards; GC22M019171; -.
DR H-InvDB; HIX0016234; -.
DR HGNC; HGNC:2093; CLTCL1.
DR HPA; HPA041110; -.
DR MIM; 601273; gene.
DR neXtProt; NX_P53675; -.
DR PharmGKB; PA26619; -.
DR eggNOG; NOG314149; -.
DR HOGENOM; HOG000188877; -.
DR HOVERGEN; HBG005344; -.
DR InParanoid; P53675; -.
DR KO; K04646; -.
DR OMA; HESYIET; -.
DR OrthoDB; EOG7Z0JVM; -.
DR PhylomeDB; P53675; -.
DR Reactome; REACT_11123; Membrane Trafficking.
DR ChiTaRS; CLTCL1; human.
DR GenomeRNAi; 8218; -.
DR NextBio; 30943; -.
DR PRO; PR:P53675; -.
DR ArrayExpress; P53675; -.
DR Bgee; P53675; -.
DR CleanEx; HS_CLTCL1; -.
DR Genevestigator; P53675; -.
DR GO; GO:0030132; C:clathrin coat of coated pit; IEA:InterPro.
DR GO; GO:0030130; C:clathrin coat of trans-Golgi network vesicle; IEA:InterPro.
DR GO; GO:0030136; C:clathrin-coated vesicle; IDA:UniProtKB.
DR GO; GO:0005905; C:coated pit; IDA:UniProtKB.
DR GO; GO:0005819; C:spindle; IDA:UniProtKB.
DR GO; GO:0005802; C:trans-Golgi network; IDA:UniProtKB.
DR GO; GO:0004871; F:signal transducer activity; TAS:ProtInc.
DR GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
DR GO; GO:0009653; P:anatomical structure morphogenesis; TAS:ProtInc.
DR GO; GO:0006886; P:intracellular protein transport; IEA:InterPro.
DR GO; GO:0007067; P:mitosis; IDA:UniProtKB.
DR GO; GO:0046326; P:positive regulation of glucose import; IMP:UniProtKB.
DR GO; GO:0006898; P:receptor-mediated endocytosis; IDA:UniProtKB.
DR Gene3D; 1.25.40.10; -; 3.
DR Gene3D; 2.130.10.110; -; 1.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR000547; Clathrin_H-chain/VPS_repeat.
DR InterPro; IPR016025; Clathrin_H-chain_link/propller.
DR InterPro; IPR015348; Clathrin_H-chain_linker_core.
DR InterPro; IPR001473; Clathrin_H-chain_propeller_N.
DR InterPro; IPR022365; Clathrin_H-chain_propeller_rpt.
DR InterPro; IPR016341; Clathrin_heavy_chain.
DR InterPro; IPR011990; TPR-like_helical.
DR Pfam; PF00637; Clathrin; 7.
DR Pfam; PF09268; Clathrin-link; 1.
DR Pfam; PF01394; Clathrin_propel; 2.
DR PIRSF; PIRSF002290; Clathrin_H_chain; 1.
DR SMART; SM00299; CLH; 7.
DR SUPFAM; SSF48371; SSF48371; 6.
DR SUPFAM; SSF50989; SSF50989; 1.
DR PROSITE; PS50236; CHCR; 7.
PE 1: Evidence at protein level;
KW Alternative splicing; Coated pit; Complete proteome;
KW Cytoplasmic vesicle; Membrane; Polymorphism; Reference proteome;
KW Repeat.
FT CHAIN 1 1640 Clathrin heavy chain 2.
FT /FTId=PRO_0000205786.
FT REPEAT 537 683 CHCR 1.
FT REPEAT 686 828 CHCR 2.
FT REPEAT 833 972 CHCR 3.
FT REPEAT 979 1124 CHCR 4.
FT REPEAT 1128 1269 CHCR 5.
FT REPEAT 1274 1420 CHCR 6.
FT REPEAT 1423 1566 CHCR 7.
FT REGION 1 479 Globular terminal domain.
FT REGION 24 67 WD40-like repeat 1.
FT REGION 68 107 WD40-like repeat 2.
FT REGION 108 149 WD40-like repeat 3.
FT REGION 150 195 WD40-like repeat 4.
FT REGION 196 257 WD40-like repeat 5.
FT REGION 258 301 WD40-like repeat 6.
FT REGION 302 330 WD40-like repeat 7.
FT REGION 449 465 Binding site for the uncoating ATPase,
FT involved in lattice disassembly
FT (Potential).
FT REGION 480 523 Flexible linker.
FT REGION 524 1640 Heavy chain arm.
FT REGION 524 634 Distal segment.
FT REGION 639 1640 Proximal segment.
FT REGION 1213 1522 Involved in binding clathrin light chain
FT (By similarity).
FT REGION 1551 1640 Trimerization (By similarity).
FT VAR_SEQ 1479 1535 Missing (in isoform 2).
FT /FTId=VSP_001100.
FT VARIANT 61 61 P -> L (in dbSNP:rs3747059).
FT /FTId=VAR_055653.
FT VARIANT 205 205 K -> R (in dbSNP:rs5746697).
FT /FTId=VAR_055654.
FT VARIANT 279 279 Y -> C (in dbSNP:rs807459).
FT /FTId=VAR_055655.
FT VARIANT 691 691 E -> K (in dbSNP:rs1060374).
FT /FTId=VAR_055656.
FT VARIANT 941 941 K -> R (in dbSNP:rs35398725).
FT /FTId=VAR_055657.
FT VARIANT 945 945 R -> H (in dbSNP:rs36077768).
FT /FTId=VAR_055658.
FT VARIANT 1046 1046 R -> C (in dbSNP:rs712952).
FT /FTId=VAR_055659.
FT VARIANT 1195 1195 N -> S (in dbSNP:rs807547).
FT /FTId=VAR_059214.
FT VARIANT 1316 1316 M -> V (in dbSNP:rs1061325).
FT /FTId=VAR_059215.
FT VARIANT 1394 1394 I -> T (in dbSNP:rs1633399).
FT /FTId=VAR_059216.
FT VARIANT 1592 1592 V -> M (in dbSNP:rs2073738).
FT /FTId=VAR_059217.
FT VARIANT 1620 1620 R -> H (in dbSNP:rs5748024).
FT /FTId=VAR_059218.
FT CONFLICT 193 193 P -> H (in Ref. 1; AAC50494).
FT CONFLICT 215 215 L -> H (in Ref. 1; AAC50494).
FT CONFLICT 320 320 K -> T (in Ref. 2; CAA64752).
FT CONFLICT 530 530 L -> Q (in Ref. 1; AAC50494).
FT CONFLICT 1474 1474 E -> K (in Ref. 3; AAB40908/AAB40909).
FT CONFLICT 1620 1640 RKQEEHVTEPAPLVFDFDGHE -> PPSKRSM (in Ref.
FT 3; AAB40908/AAB40909).
SQ SEQUENCE 1640 AA; 187030 MW; C661E1AB989D8E7F CRC64;
MAQILPVRFQ EHFQLQNLGI NPANIGFSTL TMESDKFICI REKVGEQAQV TIIDMSDPMA
PIRRPISAES AIMNPASKVI ALKAGKTLQI FNIEMKSKMK AHTMAEEVIF WKWVSVNTVA
LVTETAVYHW SMEGDSQPMK MFDRHTSLVG CQVIHYRTDE YQKWLLLVGI SAQQNRVVGA
MQLYSVDRKV SQPIEGHAAA FAEFKMEGNA KPATLFCFAV RNPTGGKLHI IEVGQPAAGN
QPFVKKAVDV FFPPEAQNDF PVAMQIGAKH GVIYLITKYG YLHLYDLESG VCICMNRISA
DTIFVTAPHK PTSGIIGVNK KGQVLSVCVE EDNIVNYATN VLQNPDLGLR LAVRSNLAGA
EKLFVRKFNT LFAQGSYAEA AKVAASAPKG ILRTRETVQK FQSIPAQSGQ ASPLLQYFGI
LLDQGQLNKL ESLELCHLVL QQGRKQLLEK WLKEDKLECS EELGDLVKTT DPMLALSVYL
RANVPSKVIQ CFAETGQFQK IVLYAKKVGY TPDWIFLLRG VMKISPEQGL QFSRMLVQDE
EPLANISQIV DIFMENSLIQ QCTSFLLDAL KNNRPAEGLL QTWLLEMNLV HAPQVADAIL
GNKMFTHYDR AHIAQLCEKA GLLQQALEHY TDLYDIKRAV VHTHLLNPEW LVNFFGSLSV
EDSVECLHAM LSANIRQNLQ LCVQVASKYH EQLGTQALVE LFESFKSYKG LFYFLGSIVN
FSQDPDVHLK YIQAACKTGQ IKEVERICRE SSCYNPERVK NFLKEAKLTD QLPLIIVCDR
FGFVHDLVLY LYRNNLQRYI EIYVQKVNPS RTPAVIGGLL DVDCSEEVIK HLIMAVRGQF
STDELVAEVE KRNRLKLLLP WLESQIQEGC EEPATHNALA KIYIDSNNSP ECFLRENAYY
DSSVVGRYCE KRDPHLACVA YERGQCDLEL IKVCNENSLF KSEARYLVCR KDPELWAHVL
EETNPSRRQL IDQVVQTALS ETRDPEEISV TVKAFMTADL PNELIELLEK IVLDNSVFSE
HRNLQNLLIL TAIKADRTRV MEYISRLDNY DALDIASIAV SSALYEEAFT VFHKFDMNAS
AIQVLIEHIG NLDRAYEFAE RCNEPAVWSQ LAQAQLQKDL VKEAINSYIR GDDPSSYLEV
VQSASRSNNW EDLVKFLQMA RKKGRESYIE TELIFALAKT SRVSELEDFI NGPNNAHIQQ
VGDRCYEEGM YEAAKLLYSN VSNFARLAST LVHLGEYQAA VDNSRKASST RTWKEVCFAC
MDGQEFRFAQ LCGLHIVIHA DELEELMCYY QDRGYFEELI LLLEAALGLE RAHMGMFTEL
AILYSKFKPQ KMLEHLELFW SRVNIPKVLR AAEQAHLWAE LVFLYDKYEE YDNAVLTMMS
HPTEAWKEGQ FKDIITKVAN VELCYRALQF YLDYKPLLIN DLLLVLSPRL DHTWTVSFFS
KAGQLPLVKP YLRSVQSHNN KSVNEALNHL LTEEEDYQGL RASIDAYDNF DNISLAQQLE
KHQLMEFRCI AAYLYKGNNW WAQSVELCKK DHLYKDAMQH AAESRDAELA QKLLQWFLEE
GKRECFAACL FTCYDLLRPD MVLELAWRHN LVDLAMPYFI QVMREYLSKV DKLDALESLR
KQEEHVTEPA PLVFDFDGHE
//
MIM
601273
*RECORD*
*FIELD* NO
601273
*FIELD* TI
*601273 CLATHRIN, HEAVY POLYPEPTIDE-LIKE 1; CLTCL1
;;CLATHRIN, HEAVY POLYPEPTIDE D; CLTD;;
read moreCLH22;;
CHC22
*FIELD* TX
CLONING
Using a YAC clone containing the velocardiofacial syndrome (VCFS;
192430) critical region on chromosome 22q11 as a substrate for cDNA
selection, Sirotkin et al. (1996) derived a cDNA, which they designated
CLTD, that encodes a protein with a high degree of homology at the amino
acid level to human rat and Drosophila clathrin heavy chain. The CLTD
protein is 7% divergent at the amino acid level from that of the human
clathrin heavy chain gene (CLTC; 118955) located on chromosome
17q11-qter.
Kedra et al. (1996) cloned and characterized a clathrin heavy chain
gene, which they referred to as CLH22. The gene was cloned using a
software-based exon-trapping approach based on sequencing of genomic DNA
present in chromosome 22q11 contigs combined with the use of
exon-prediction computer programs. The 5,470-bp sequence covering the
entire open reading frame encodes a 1,640-amino acid polypeptide that is
identical to the polypeptide described by Sirotkin et al. (1996).
Although expression of the CLTD gene was ubiquitous, it was relatively
low in all tissues except skeletal muscle, testis, and heart. The main
transcript was 6 kb, and alternate transcripts were detected in several
tissues. Kedra et al. (1996) demonstrated loss of expression of the CLTD
gene in 37 out of 46 sporadic meningiomas examined. In genomic DNA from
82 sporadic meningiomas, they demonstrated aberrant restriction patterns
consistent with intragenic rearrangements in 4 tumors. Based on these
findings, the authors proposed that CLTD may be considered a candidate
meningioma tumor suppressor gene.
Long et al. (1996) cloned and characterized a gene they symbolized CLTCL
for 'CLTC-like.' The gene was expressed in all fetal tissues tested and
was selectively expressed in certain adult tissues, particularly
skeletal muscle. They observed alternative splicing of an exon near the
C terminus of the predicted polypeptide.
GENE FUNCTION
Intracellular trafficking of the glucose transporter GLUT4 (138190) from
storage compartments to the plasma membrane is triggered in muscle and
fat during the body's response to insulin. Clathrin is involved in
intracellular trafficking, and in humans, the clathrin heavy-chain
isoform CHC22 is highly expressed in skeletal muscle. Vassilopoulos et
al. (2009) found a role for CHC22 in the formation of insulin-responsive
GLUT4 compartments in human muscle and adipocytes. CHC22 also associated
with expanded GLUT4 compartments in muscle from patients with type 2
diabetes (125853). Tissue-specific introduction of CHC22 in mice, which
have only a pseudogene for this protein, caused aberrant localization of
GLUT4 transport pathway components in their muscle, as well as features
of diabetes. Thus, Vassilopoulos et al. (2009) concluded that
CHC22-dependent membrane trafficking constitutes a species-restricted
pathway in human muscle and fat with potential implications for type 2
diabetes.
MAPPING
Long et al. (1996) used fluorescence in situ hybridization to map CLTCL
to proximal 22q near the region commonly deleted in DiGeorge syndrome
(DGS; 188400) and VCFS.
In the course of comparative mapping of the human 22q11 region in mice,
Puech et al. (1997) found that CLTCL gene, which lies in the center of a
cluster of genes whose homologs reside on chromosome 16, is not located
there in the mouse. A gene they referred to as Cltd-rs-4 was located in
the central region of mouse chromosome 11 that shares a large region of
homology with human chromosome 17. A second human clathrin heavy chain
gene, CLTC, which is 84.7% identical to CLTD, maps to 17q11-qter. Puech
et al. (1997) interpreted their findings as suggesting that either Cltc
and Cltd are tandemly duplicated loci that map to the central region of
mouse chromosome 11 or that the mouse genome does not contain a gene
corresponding to human CLTD. They favored the latter hypothesis.
CYTOGENETICS
Holmes et al. (1997) reported characterization of a balanced
translocation t(21;22)(p12;q11) within the minimal DiGeorge syndrome
critical region in a patient with some features of DGS/VCFS, including
facial dysmorphia, mental retardation, long slender digits, and genital
anomalies (first-degree hypospadias and bilateral cryptorchidism).
Holmes et al. (1997) cloned the breakpoint of the translocation and
showed that it interrupted the CLTCL gene within the DGCR. The
breakpoint of the translocation partner was in a repeated region
telomeric to the rDNA cluster on chromosome 21p, making it unlikely that
the patient's findings were caused by interruption of sequences on 21p.
The chromosome 22 breakpoint, on the other hand, disrupted the 3-prime
coding region of the CLTCL gene and led to a truncated transcript.
*FIELD* RF
1. Holmes, S. E.; Riazi, M. A.; Gong, W.; McDermid, H. E.; Sellinger,
B. T.; Hua, A.; Chen, F.; Wang, Z.; Zhang, G.; Roe, B.; Gonzalez,
I.; McDonald-McGinn, D. M.; Zackai, E.; Emanuel, B. S.; Budarf, M.
L.: Disruption of the clathrin heavy chain-like gene (CLTCL) associated
with features of DGS/VCFS: a balanced (21;22)(p12;q11) translocation. Hum.
Molec. Genet. 6: 357-367, 1997.
2. Kedra, D.; Peyrard, M.; Fransson, I.; Collins, J. E.; Dunham, I.;
Roe, B. A.; Dumanski, J. P.: Characterization of a second human clathrin
heavy chain polypeptide gene (CLH-22) from chromosome 22q11. Hum.
Molec. Genet. 5: 625-631, 1996.
3. Long, K. R.; Trofatter, J. A.; Ramesh, V.; McCormick, M. K.; Buckler,
A. J.: Cloning and characterization of a novel human clathrin heavy
chain gene (CLTCL). Genomics 35: 466-472, 1996.
4. Puech, A.; Saint-Jore, B.; Funke, B.; Gilbert, D. J.; Sirotkin,
H.; Copeland, N. G.; Jenkins, N. A.; Kucherlapati, R.; Morrow, B.;
Skoultchi, A. I.: Comparative mapping of the human 22q11 chromosomal
region and the orthologous region in mice reveals complex changes
in gene organization. Proc. Nat. Acad. Sci. 94: 14608-14613, 1997.
5. Sirotkin, H.; Morrow, B.; DasGupta, R.; Goldberg, R.; Patanjali,
S. R.; Shi, G.; Cannizzaro, L.; Shprintzen, R.; Weissman, S. M.; Kucherlapati,
R.: Isolation of a new clathrin heavy chain gene with muscle-specific
expression from the region commonly deleted in velo-cardio-facial
syndrome. Hum. Molec. Genet. 5: 617-624, 1996.
6. Vassilopoulos, S.; Esk, C.; Hoshino, S.; Funke, B. H.; Chen, C.-Y.;
Plocik, A. M.; Wright, W. E.; Kucherlapati, R.; Brodsky, F. M.: A
role for the CHC22 clathrin heavy-chain isoform in human glucose metabolism. Science 324:
1192-1196, 2009.
*FIELD* CN
Ada Hamosh - updated: 6/16/2009
Victor A. McKusick - updated: 2/6/1998
Mark H. Paalman - updated: 6/3/1997
Victor A. McKusick - updated: 4/21/1997
*FIELD* CD
Moyra Smith: 5/21/1996
*FIELD* ED
alopez: 06/22/2009
terry: 6/16/2009
carol: 4/23/1999
mark: 2/15/1998
terry: 2/6/1998
alopez: 6/4/1997
mark: 6/3/1997
mark: 4/21/1997
terry: 4/8/1997
mark: 5/28/1996
carol: 5/22/1996
*RECORD*
*FIELD* NO
601273
*FIELD* TI
*601273 CLATHRIN, HEAVY POLYPEPTIDE-LIKE 1; CLTCL1
;;CLATHRIN, HEAVY POLYPEPTIDE D; CLTD;;
read moreCLH22;;
CHC22
*FIELD* TX
CLONING
Using a YAC clone containing the velocardiofacial syndrome (VCFS;
192430) critical region on chromosome 22q11 as a substrate for cDNA
selection, Sirotkin et al. (1996) derived a cDNA, which they designated
CLTD, that encodes a protein with a high degree of homology at the amino
acid level to human rat and Drosophila clathrin heavy chain. The CLTD
protein is 7% divergent at the amino acid level from that of the human
clathrin heavy chain gene (CLTC; 118955) located on chromosome
17q11-qter.
Kedra et al. (1996) cloned and characterized a clathrin heavy chain
gene, which they referred to as CLH22. The gene was cloned using a
software-based exon-trapping approach based on sequencing of genomic DNA
present in chromosome 22q11 contigs combined with the use of
exon-prediction computer programs. The 5,470-bp sequence covering the
entire open reading frame encodes a 1,640-amino acid polypeptide that is
identical to the polypeptide described by Sirotkin et al. (1996).
Although expression of the CLTD gene was ubiquitous, it was relatively
low in all tissues except skeletal muscle, testis, and heart. The main
transcript was 6 kb, and alternate transcripts were detected in several
tissues. Kedra et al. (1996) demonstrated loss of expression of the CLTD
gene in 37 out of 46 sporadic meningiomas examined. In genomic DNA from
82 sporadic meningiomas, they demonstrated aberrant restriction patterns
consistent with intragenic rearrangements in 4 tumors. Based on these
findings, the authors proposed that CLTD may be considered a candidate
meningioma tumor suppressor gene.
Long et al. (1996) cloned and characterized a gene they symbolized CLTCL
for 'CLTC-like.' The gene was expressed in all fetal tissues tested and
was selectively expressed in certain adult tissues, particularly
skeletal muscle. They observed alternative splicing of an exon near the
C terminus of the predicted polypeptide.
GENE FUNCTION
Intracellular trafficking of the glucose transporter GLUT4 (138190) from
storage compartments to the plasma membrane is triggered in muscle and
fat during the body's response to insulin. Clathrin is involved in
intracellular trafficking, and in humans, the clathrin heavy-chain
isoform CHC22 is highly expressed in skeletal muscle. Vassilopoulos et
al. (2009) found a role for CHC22 in the formation of insulin-responsive
GLUT4 compartments in human muscle and adipocytes. CHC22 also associated
with expanded GLUT4 compartments in muscle from patients with type 2
diabetes (125853). Tissue-specific introduction of CHC22 in mice, which
have only a pseudogene for this protein, caused aberrant localization of
GLUT4 transport pathway components in their muscle, as well as features
of diabetes. Thus, Vassilopoulos et al. (2009) concluded that
CHC22-dependent membrane trafficking constitutes a species-restricted
pathway in human muscle and fat with potential implications for type 2
diabetes.
MAPPING
Long et al. (1996) used fluorescence in situ hybridization to map CLTCL
to proximal 22q near the region commonly deleted in DiGeorge syndrome
(DGS; 188400) and VCFS.
In the course of comparative mapping of the human 22q11 region in mice,
Puech et al. (1997) found that CLTCL gene, which lies in the center of a
cluster of genes whose homologs reside on chromosome 16, is not located
there in the mouse. A gene they referred to as Cltd-rs-4 was located in
the central region of mouse chromosome 11 that shares a large region of
homology with human chromosome 17. A second human clathrin heavy chain
gene, CLTC, which is 84.7% identical to CLTD, maps to 17q11-qter. Puech
et al. (1997) interpreted their findings as suggesting that either Cltc
and Cltd are tandemly duplicated loci that map to the central region of
mouse chromosome 11 or that the mouse genome does not contain a gene
corresponding to human CLTD. They favored the latter hypothesis.
CYTOGENETICS
Holmes et al. (1997) reported characterization of a balanced
translocation t(21;22)(p12;q11) within the minimal DiGeorge syndrome
critical region in a patient with some features of DGS/VCFS, including
facial dysmorphia, mental retardation, long slender digits, and genital
anomalies (first-degree hypospadias and bilateral cryptorchidism).
Holmes et al. (1997) cloned the breakpoint of the translocation and
showed that it interrupted the CLTCL gene within the DGCR. The
breakpoint of the translocation partner was in a repeated region
telomeric to the rDNA cluster on chromosome 21p, making it unlikely that
the patient's findings were caused by interruption of sequences on 21p.
The chromosome 22 breakpoint, on the other hand, disrupted the 3-prime
coding region of the CLTCL gene and led to a truncated transcript.
*FIELD* RF
1. Holmes, S. E.; Riazi, M. A.; Gong, W.; McDermid, H. E.; Sellinger,
B. T.; Hua, A.; Chen, F.; Wang, Z.; Zhang, G.; Roe, B.; Gonzalez,
I.; McDonald-McGinn, D. M.; Zackai, E.; Emanuel, B. S.; Budarf, M.
L.: Disruption of the clathrin heavy chain-like gene (CLTCL) associated
with features of DGS/VCFS: a balanced (21;22)(p12;q11) translocation. Hum.
Molec. Genet. 6: 357-367, 1997.
2. Kedra, D.; Peyrard, M.; Fransson, I.; Collins, J. E.; Dunham, I.;
Roe, B. A.; Dumanski, J. P.: Characterization of a second human clathrin
heavy chain polypeptide gene (CLH-22) from chromosome 22q11. Hum.
Molec. Genet. 5: 625-631, 1996.
3. Long, K. R.; Trofatter, J. A.; Ramesh, V.; McCormick, M. K.; Buckler,
A. J.: Cloning and characterization of a novel human clathrin heavy
chain gene (CLTCL). Genomics 35: 466-472, 1996.
4. Puech, A.; Saint-Jore, B.; Funke, B.; Gilbert, D. J.; Sirotkin,
H.; Copeland, N. G.; Jenkins, N. A.; Kucherlapati, R.; Morrow, B.;
Skoultchi, A. I.: Comparative mapping of the human 22q11 chromosomal
region and the orthologous region in mice reveals complex changes
in gene organization. Proc. Nat. Acad. Sci. 94: 14608-14613, 1997.
5. Sirotkin, H.; Morrow, B.; DasGupta, R.; Goldberg, R.; Patanjali,
S. R.; Shi, G.; Cannizzaro, L.; Shprintzen, R.; Weissman, S. M.; Kucherlapati,
R.: Isolation of a new clathrin heavy chain gene with muscle-specific
expression from the region commonly deleted in velo-cardio-facial
syndrome. Hum. Molec. Genet. 5: 617-624, 1996.
6. Vassilopoulos, S.; Esk, C.; Hoshino, S.; Funke, B. H.; Chen, C.-Y.;
Plocik, A. M.; Wright, W. E.; Kucherlapati, R.; Brodsky, F. M.: A
role for the CHC22 clathrin heavy-chain isoform in human glucose metabolism. Science 324:
1192-1196, 2009.
*FIELD* CN
Ada Hamosh - updated: 6/16/2009
Victor A. McKusick - updated: 2/6/1998
Mark H. Paalman - updated: 6/3/1997
Victor A. McKusick - updated: 4/21/1997
*FIELD* CD
Moyra Smith: 5/21/1996
*FIELD* ED
alopez: 06/22/2009
terry: 6/16/2009
carol: 4/23/1999
mark: 2/15/1998
terry: 2/6/1998
alopez: 6/4/1997
mark: 6/3/1997
mark: 4/21/1997
terry: 4/8/1997
mark: 5/28/1996
carol: 5/22/1996