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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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
//