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Database: UniProt
Entry: A0A1D5R8V0_MACMU
LinkDB: A0A1D5R8V0_MACMU
Original site: A0A1D5R8V0_MACMU 
ID   A0A1D5R8V0_MACMU        Unreviewed;      1651 AA.
AC   A0A1D5R8V0;
DT   30-NOV-2016, integrated into UniProtKB/TrEMBL.
DT   11-DEC-2019, sequence version 2.
DT   24-JAN-2024, entry version 43.
DE   RecName: Full=Clathrin heavy chain {ECO:0000256|PIRNR:PIRNR002290};
GN   Name=CLTC {ECO:0000313|Ensembl:ENSMMUP00000056740.2,
GN   ECO:0000313|VGNC:VGNC:97754};
OS   Macaca mulatta (Rhesus macaque).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Cercopithecinae; Macaca.
OX   NCBI_TaxID=9544 {ECO:0000313|Ensembl:ENSMMUP00000056740.2, ECO:0000313|Proteomes:UP000006718};
RN   [1] {ECO:0000313|Ensembl:ENSMMUP00000056740.2, ECO:0000313|Proteomes:UP000006718}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=17573 {ECO:0000313|Ensembl:ENSMMUP00000056740.2,
RC   ECO:0000313|Proteomes:UP000006718};
RX   PubMed=17431167; DOI=10.1126/science.1139247;
RA   Gibbs R.A., Rogers J., Katze M.G., Bumgarner R., Weinstock G.M.,
RA   Mardis E.R., Remington K.A., Strausberg R.L., Venter J.C., Wilson R.K.,
RA   Batzer M.A., Bustamante C.D., Eichler E.E., Hahn M.W., Hardison R.C.,
RA   Makova K.D., Miller W., Milosavljevic A., Palermo R.E., Siepel A.,
RA   Sikela J.M., Attaway T., Bell S., Bernard K.E., Buhay C.J.,
RA   Chandrabose M.N., Dao M., Davis C., Delehaunty K.D., Ding Y., Dinh H.H.,
RA   Dugan-Rocha S., Fulton L.A., Gabisi R.A., Garner T.T., Godfrey J.,
RA   Hawes A.C., Hernandez J., Hines S., Holder M., Hume J., Jhangiani S.N.,
RA   Joshi V., Khan Z.M., Kirkness E.F., Cree A., Fowler R.G., Lee S.,
RA   Lewis L.R., Li Z., Liu Y.-S., Moore S.M., Muzny D., Nazareth L.V.,
RA   Ngo D.N., Okwuonu G.O., Pai G., Parker D., Paul H.A., Pfannkoch C.,
RA   Pohl C.S., Rogers Y.-H.C., Ruiz S.J., Sabo A., Santibanez J.,
RA   Schneider B.W., Smith S.M., Sodergren E., Svatek A.F., Utterback T.R.,
RA   Vattathil S., Warren W., White C.S., Chinwalla A.T., Feng Y., Halpern A.L.,
RA   Hillier L.W., Huang X., Minx P., Nelson J.O., Pepin K.H., Qin X.,
RA   Sutton G.G., Venter E., Walenz B.P., Wallis J.W., Worley K.C., Yang S.-P.,
RA   Jones S.M., Marra M.A., Rocchi M., Schein J.E., Baertsch R., Clarke L.,
RA   Csuros M., Glasscock J., Harris R.A., Havlak P., Jackson A.R., Jiang H.,
RA   Liu Y., Messina D.N., Shen Y., Song H.X.-Z., Wylie T., Zhang L., Birney E.,
RA   Han K., Konkel M.K., Lee J., Smit A.F.A., Ullmer B., Wang H., Xing J.,
RA   Burhans R., Cheng Z., Karro J.E., Ma J., Raney B., She X., Cox M.J.,
RA   Demuth J.P., Dumas L.J., Han S.-G., Hopkins J., Karimpour-Fard A.,
RA   Kim Y.H., Pollack J.R., Vinar T., Addo-Quaye C., Degenhardt J., Denby A.,
RA   Hubisz M.J., Indap A., Kosiol C., Lahn B.T., Lawson H.A., Marklein A.,
RA   Nielsen R., Vallender E.J., Clark A.G., Ferguson B., Hernandez R.D.,
RA   Hirani K., Kehrer-Sawatzki H., Kolb J., Patil S., Pu L.-L., Ren Y.,
RA   Smith D.G., Wheeler D.A., Schenck I., Ball E.V., Chen R., Cooper D.N.,
RA   Giardine B., Hsu F., Kent W.J., Lesk A., Nelson D.L., O'brien W.E.,
RA   Pruefer K., Stenson P.D., Wallace J.C., Ke H., Liu X.-M., Wang P.,
RA   Xiang A.P., Yang F., Barber G.P., Haussler D., Karolchik D., Kern A.D.,
RA   Kuhn R.M., Smith K.E., Zwieg A.S.;
RT   "Evolutionary and biomedical insights from the rhesus macaque genome.";
RL   Science 316:222-234(2007).
RN   [2] {ECO:0000313|Ensembl:ENSMMUP00000056740.2}
RP   IDENTIFICATION.
RC   STRAIN=17573 {ECO:0000313|Ensembl:ENSMMUP00000056740.2};
RG   Ensembl;
RL   Submitted (JUL-2023) to UniProtKB.
CC   -!- FUNCTION: Clathrin is the major protein of the polyhedral coat of
CC       coated pits and vesicles. {ECO:0000256|PIRNR:PIRNR002290}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle membrane
CC       {ECO:0000256|PIRNR:PIRNR002290}; Peripheral membrane protein
CC       {ECO:0000256|PIRNR:PIRNR002290}; Cytoplasmic side
CC       {ECO:0000256|PIRNR:PIRNR002290}. Membrane, coated pit
CC       {ECO:0000256|PIRNR:PIRNR002290}; Peripheral membrane protein
CC       {ECO:0000256|PIRNR:PIRNR002290}; Cytoplasmic side
CC       {ECO:0000256|PIRNR:PIRNR002290}. Membrane
CC       {ECO:0000256|ARBA:ARBA00004287}; Peripheral membrane protein
CC       {ECO:0000256|ARBA:ARBA00004287}; Cytoplasmic side
CC       {ECO:0000256|ARBA:ARBA00004287}.
CC   -!- SIMILARITY: Belongs to the clathrin heavy chain family.
CC       {ECO:0000256|ARBA:ARBA00009535, ECO:0000256|PIRNR:PIRNR002290}.
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DR   SMR; A0A1D5R8V0; -.
DR   Ensembl; ENSMMUT00000075775.2; ENSMMUP00000056740.2; ENSMMUG00000010509.4.
DR   VEuPathDB; HostDB:ENSMMUG00000010509; -.
DR   VGNC; VGNC:97754; CLTC.
DR   GeneTree; ENSGT00950000183166; -.
DR   Proteomes; UP000006718; Chromosome 16.
DR   Bgee; ENSMMUG00000010509; Expressed in Ammon's horn and 22 other cell types or tissues.
DR   ExpressionAtlas; A0A1D5R8V0; baseline.
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:0071439; C:clathrin complex; IEA:InterPro.
DR   GO; GO:0032051; F:clathrin light chain binding; IEA:InterPro.
DR   GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
DR   GO; GO:0006886; P:intracellular protein transport; IEA:UniProtKB-UniRule.
DR   GO; GO:0016192; P:vesicle-mediated transport; IEA:InterPro.
DR   Gene3D; 1.25.40.730; -; 1.
DR   Gene3D; 2.130.10.110; Clathrin heavy-chain terminal domain; 1.
DR   Gene3D; 1.25.40.10; Tetratricopeptide repeat domain; 4.
DR   InterPro; IPR016024; ARM-type_fold.
DR   InterPro; IPR000547; Clathrin_H-chain/VPS_repeat.
DR   InterPro; IPR015348; Clathrin_H-chain_linker_core.
DR   InterPro; IPR016025; Clathrin_H-chain_N.
DR   InterPro; IPR022365; Clathrin_H-chain_propeller_rpt.
DR   InterPro; IPR016341; Clathrin_heavy_chain.
DR   InterPro; IPR011990; TPR-like_helical_dom_sf.
DR   PANTHER; PTHR10292:SF7; CLATHRIN HEAVY CHAIN 1; 1.
DR   PANTHER; PTHR10292; CLATHRIN HEAVY CHAIN RELATED; 1.
DR   Pfam; PF00637; Clathrin; 7.
DR   Pfam; PF09268; Clathrin-link; 1.
DR   Pfam; PF13838; Clathrin_H_link; 1.
DR   Pfam; PF01394; Clathrin_propel; 4.
DR   PIRSF; PIRSF002290; Clathrin_H_chain; 1.
DR   SMART; SM00299; CLH; 7.
DR   SUPFAM; SSF48371; ARM repeat; 6.
DR   SUPFAM; SSF50989; Clathrin heavy-chain terminal domain; 1.
DR   PROSITE; PS50236; CHCR; 7.
PE   3: Inferred from homology;
KW   Coated pit {ECO:0000256|ARBA:ARBA00023176, ECO:0000256|PIRNR:PIRNR002290};
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Cytoplasmic vesicle {ECO:0000256|ARBA:ARBA00023329,
KW   ECO:0000256|PIRNR:PIRNR002290};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|PIRNR:PIRNR002290};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006718};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT   DOMAIN          300..323
FT                   /note="Clathrin heavy chain linker core motif"
FT                   /evidence="ECO:0000259|Pfam:PF09268"
FT   REPEAT          506..652
FT                   /note="CHCR"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01006"
FT   REPEAT          655..797
FT                   /note="CHCR"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01006"
FT   REPEAT          802..941
FT                   /note="CHCR"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01006"
FT   REPEAT          948..1093
FT                   /note="CHCR"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01006"
FT   REPEAT          1097..1238
FT                   /note="CHCR"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01006"
FT   REPEAT          1243..1389
FT                   /note="CHCR"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01006"
FT   REPEAT          1392..1535
FT                   /note="CHCR"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01006"
FT   COILED          1572..1602
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   1651 AA;  188938 MW;  85B644547B6E9030 CRC64;
     MESDKFICIR EKVGEQAQVV IIDMNDPSNP IRRPISADSA IMNPASKVIA LKAGKTLQIF
     NIEMKSKMKA HTMTDDVTFW KWISLNTVAL VTDNAVYHWS MEGESQPVKM FDRHSSLAGC
     QIINYRTDAK QKWLLLTGIS AQQNRVVGAM QLYSVDRKVS QPIEGHAASF AQFKMEGNAE
     ESTLFCFAVR GQAGGKLHII EVGTPPTGNQ PFPKKAVDVF FPPEAQNDFP VAMQISEKHD
     VVFLITKYGY IHLYDLETGT CIYMNRISGE TIFVTAPHEA TAGIIGVNRK GQVLSVCVEE
     ENIIPYITNV LQNPDLALRM AVRNNLAGAE ELFARKFNAL FAQGNYSEAA KVAANAPKGI
     LRTPDTIRRF QSVPAQPGQT SPLLQYFGIL LDQGQLNKYE SLELCRPVLQ QGRKQLLEKW
     LKEDKLECSE ELGDLVKSVD PTLALSVYLR ANVPNKVIQC FAETGQVQKI VLYAKKVGYT
     PDWIFLLRNV MRISPDQGQQ FAQMLVQDEE PLADITQIVD VFMEYNLIQQ CTAFLLDALK
     NNRPSEGPLQ TRLLEMNLMH APQVADAILG NQMFTHYDRA HIAQLCEKAG LLQRALEHFT
     DLYDIKRAVV HTHLLNPEWL VNYFGSLSVE DSLECLRAML SANIRQNLQI CVQVASKYHE
     QLSTQSLIEL FESFKSFEGL FYFLGSIVNF SQDPDVHFKY IQAACKTGQI KEVERICRES
     NCYDPERVKN FLKEAKLTDQ LPLIIVCDRF DFVHDLVLYL YRNNLQKYIE IYVQKVNPSR
     LPVVIGGLLD VDCSEDVIKN LILVVRGQFS TDELVAEVEK RNRLKLLLPW LEARIHEGCE
     EPATHNALAK IYIDSNNNPE RFLRENPYYD SRVVGKYCEK RDPHLACVAY ERGQCDLELI
     NVCNENSLFK SLSRYLVRRK DPELWGSVLL ESNPYRRPLI DQVVQTALSE TQDPEEVSVT
     VKAFMTADLP NELIELLEKI VLDNSVFSEH RNLQNLLILT AIKADRTRVM EYINRLDNYD
     APDIANIAIS NELFEEAFAI FRKFDVNTSA VQVLIEHIGN LDRAYEFAER CNEPAVWSQL
     AKAQLQKGMV KEAIDSYIKA DDPSSYMEVV QAANTSGNWE ELVKYLQMAR KKARESYVET
     ELIFALAKTN RLAELEEFIN GPNNAHIQQV GDRCYDEKMY DAAKLLYNNV SNFGRLASTL
     VHLGEYQAAV DGARKANSTR TWKEVCFACV DGKEFRLAQM CGLHIVVHAD ELEELINYYQ
     DRGYFEELIT MLEAALGLER AHMGMFTELA ILYSKFKPQK MREHLELFWS RVNIPKVLRA
     AEQAHLWAEL VFLYDKYEEY DNAIITMMNH PTDAWKEGQF KDIITKVANV ELYYRAIQFY
     LEFKPLLLND LLMVLSPRLD HTRAVNYFSK VKQLPLVKPY LRSVQNHNNK SVNESLNNLF
     ITEEDYQALR TSIDAYDNFD NISLAQRLEK HELIEFRRIA AYLFKGNNRW KQSVELCKKD
     SLYKDAMQYA SESKDTELAE ELLQWFLQEE KRECFGACLF TCYDLLRPDV VLETAWRHNI
     MDFAMPYFIQ VMKEYLTKVD AIKEKVDKLD ASESLRKEEE QATETQPIVY GQPQLMLTAG
     PSVAVPPQAP FGYGYTAPPY GQPQPGFGYS M
//
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