ID G1SF26_RABIT Unreviewed; 1632 AA.
AC G1SF26;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 11-DEC-2019, sequence version 2.
DT 27-MAR-2024, entry version 73.
DE RecName: Full=Clathrin heavy chain {ECO:0000256|PIRNR:PIRNR002290};
GN Name=CLTCL1 {ECO:0000313|Ensembl:ENSOCUP00000001087.3};
OS Oryctolagus cuniculus (Rabbit).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX NCBI_TaxID=9986 {ECO:0000313|Ensembl:ENSOCUP00000001087.3, ECO:0000313|Proteomes:UP000001811};
RN [1] {ECO:0000313|Ensembl:ENSOCUP00000001087.3, ECO:0000313|Proteomes:UP000001811}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Thorbecke {ECO:0000313|Proteomes:UP000001811};
RX PubMed=21993624; DOI=10.1038/nature10530;
RA Lindblad-Toh K., Garber M., Zuk O., Lin M.F., Parker B.J., Washietl S.,
RA Kheradpour P., Ernst J., Jordan G., Mauceli E., Ward L.D., Lowe C.B.,
RA Holloway A.K., Clamp M., Gnerre S., Alfoldi J., Beal K., Chang J.,
RA Clawson H., Cuff J., Di Palma F., Fitzgerald S., Flicek P., Guttman M.,
RA Hubisz M.J., Jaffe D.B., Jungreis I., Kent W.J., Kostka D., Lara M.,
RA Martins A.L., Massingham T., Moltke I., Raney B.J., Rasmussen M.D.,
RA Robinson J., Stark A., Vilella A.J., Wen J., Xie X., Zody M.C., Baldwin J.,
RA Bloom T., Chin C.W., Heiman D., Nicol R., Nusbaum C., Young S.,
RA Wilkinson J., Worley K.C., Kovar C.L., Muzny D.M., Gibbs R.A., Cree A.,
RA Dihn H.H., Fowler G., Jhangiani S., Joshi V., Lee S., Lewis L.R.,
RA Nazareth L.V., Okwuonu G., Santibanez J., Warren W.C., Mardis E.R.,
RA Weinstock G.M., Wilson R.K., Delehaunty K., Dooling D., Fronik C.,
RA Fulton L., Fulton B., Graves T., Minx P., Sodergren E., Birney E.,
RA Margulies E.H., Herrero J., Green E.D., Haussler D., Siepel A., Goldman N.,
RA Pollard K.S., Pedersen J.S., Lander E.S., Kellis M.;
RT "A high-resolution map of human evolutionary constraint using 29 mammals.";
RL Nature 478:476-482(2011).
RN [2] {ECO:0000313|Ensembl:ENSOCUP00000001087.3}
RP IDENTIFICATION.
RC STRAIN=Thorbecke {ECO:0000313|Ensembl:ENSOCUP00000001087.3};
RG Ensembl;
RL Submitted (NOV-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; G1SF26; -.
DR STRING; 9986.ENSOCUP00000001087; -.
DR PaxDb; 9986-ENSOCUP00000001087; -.
DR Ensembl; ENSOCUT00000001255.3; ENSOCUP00000001087.3; ENSOCUG00000001254.3.
DR eggNOG; KOG0985; Eukaryota.
DR GeneTree; ENSGT00950000183166; -.
DR HOGENOM; CLU_002136_0_0_1; -.
DR InParanoid; G1SF26; -.
DR TreeFam; TF300059; -.
DR Proteomes; UP000001811; Unplaced.
DR Bgee; ENSOCUG00000001254; Expressed in skeletal muscle tissue and 18 other cell types or tissues.
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:0005829; C:cytosol; IEA:GOC.
DR GO; GO:0005770; C:late endosome; IEA:Ensembl.
DR GO; GO:0097443; C:sorting endosome; IEA:Ensembl.
DR GO; GO:0005819; C:spindle; IEA:Ensembl.
DR GO; GO:0005802; C:trans-Golgi network; IEA:Ensembl.
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:0000278; P:mitotic cell cycle; IEA:Ensembl.
DR GO; GO:0046326; P:positive regulation of glucose import; IEA:Ensembl.
DR GO; GO:0006898; P:receptor-mediated endocytosis; IEA:Ensembl.
DR GO; GO:0042147; P:retrograde transport, endosome to Golgi; IEA:Ensembl.
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:SF6; CLATHRIN HEAVY CHAIN 2; 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; 2.
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 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:UP000001811};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT DOMAIN 331..354
FT /note="Clathrin heavy chain linker core motif"
FT /evidence="ECO:0000259|Pfam:PF09268"
SQ SEQUENCE 1632 AA; 184552 MW; 1384A244FAECD3D1 CRC64;
MAQILPIRFQ EHFQLQNLGI NPANIGFSTL TMESDKFICV REKVGEQAQV VIVDMHEPTA
PIRRPISADS AIMNPASKVI ALKAGKTLQI FNIEMKSKMK AHTMSEEVIF WKWISVNTVA
LVTETAVYHW SMEGDSQPTK MFDRHASLAG CQMIHYRADE HHKWLLLIGI AAQQNRVVGA
MQLYSVDRKV SQPIEGHAAA FAEFKIEGNA KPATLFCFAV RSPAGGKLHI IEVGQPAAGN
QPFVKKAVDV FFPPEAQTDF PVAMQIGAKH GVIYLITKAG YLHLYDLESG VCIYMNRISA
DTIFVTAPHE PTSGIIGVNK KGQVLSVCVE EENIVNYATS VLQNPDLGLR LAVRSNLAGA
EELFVRKFSA LFAQGSYAEA ARVAASAPKG ILRTSDTVRK FQSIPAQPGQ ASPLLQYFGI
LLDQGQLNKL ESLELCRPVL QQGRKQLLEK WLKEDKLECS EELGDLVKAA DPTLALSVYL
RANVPSKVIQ CFAETGQFQK IVLYAKKVGY SPDWMFLLRS VMRVSPEQGL QFAQMLVQDA
EPLANMNQIV DIFMENSLIQ QCTSFLLDAL KNNQPAEGHL QTRLLEMNLI HAPQVADAIL
GNQMFTHYDR AHIGQLCEKA GLLQRALEHY TDLYDIKRAV VHTHLLNPEW LVNFFGSLSV
EDSLECLRAM LSANIRQNLQ LCVQVASKYH EQLGTQALVE LFESFKSYEG LFYFLGSIVN
FSQDPDVHLK YIQAACKTGQ IKEVERICRE SSCYNPERVK NFLKEAKLTD QLPLIIVCDR
FDFVHDLVLY LYRNNLQKYI EIYVQKVNPS RIPAVVGGLL DVDCSEDVIK NLIMAVRGQF
STDELVAEVE KRNRLKLLLP WLESRIQEGC EEPATHNALA KIYIDSNNSP ERFLRENAFY
DSSVVGRYCE KRDPHLACVA YERGQCDLDL IKVVQTALSE TQDPEEVSVT VKAFMTADLP
NELIELLEKI VLDNSIFSEH RNLQNLLILT AVKADRTRVM DYISRLDNYD APDIASIAVS
SGLYEEAFAI FRKFDVNASA IQVLIEHIGN LDRAYEFAEK CNEPAVWSQL ARAQLHKELV
KEAIDSFIRA DDPSSYLEVV QAASRSNNWE DLVKFLQMAR KRSHESYVET ELIFALAKTS
RLSELEDCVN GPNNANIQQV GDRCYKEGMY EAAKLLYSSV SNFACLASTL VHLGEYQAAV
DSSRKANSTR TWKEVCFACV DGQEFRLAQL CGLHIVIHAD ELEDLIQYYQ DRGYFEELIS
LLEAALGLER AHMGMFTELA ILYSKFKPQK MPEHLELFWS RVNIPKVLRA AEQAHLWAEL
VFLYDKYEEY DNAVLTMISH PTEAWKEGQF KDVIAKVANV ELYYKALQFY LDYKPLLIND
LLVVLSPRLD HTRTVGFFAK VGQLPLVKPY LRSVQSHNNK SVNEALNQLL TDEEDYQGLR
ASIDAYDNFD NIGLAQRLEK HQLIEFRRIA ACLYKGSNRW AQSVELCKKD HLYKDAMQHA
AESRDAELAT KLLQWFLEEG RRECFAASLF TCYDLLHPDV VLELAWRHNL MDFAMPYFIQ
VMREYLSKVD KLDAWDSLRK QEERMVEPAP LVLGQQLMLT AGPAASPAPA SFPYGYAAAP
AFSQPPVYGF SV
//
