CLH_SCHPO
ID CLH_SCHPO Reviewed; 1666 AA.
AC Q10161;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 25-MAY-2022, entry version 150.
DE RecName: Full=Probable clathrin heavy chain;
GN Name=chc1; ORFNames=SPAC26A3.05;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
RN [2]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-392 AND SER-393, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=18257517; DOI=10.1021/pr7006335;
RA Wilson-Grady J.T., Villen J., Gygi S.P.;
RT "Phosphoproteome analysis of fission yeast.";
RL J. Proteome Res. 7:1088-1097(2008).
CC -!- FUNCTION: Clathrin is the major protein of the polyhedral coat of
CC coated pits and vesicles. {ECO:0000250}.
CC -!- SUBUNIT: Clathrin triskelions, composed of 3 heavy chains and 3 light
CC chains, are the basic subunits of the clathrin coat. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle membrane {ECO:0000250};
CC Peripheral membrane protein {ECO:0000250}; Cytoplasmic side
CC {ECO:0000250}. Membrane, coated pit {ECO:0000250}; Peripheral membrane
CC protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Note=Cytoplasmic
CC face of coated pits and vesicles. {ECO:0000250}.
CC -!- DOMAIN: The C-terminal third of the heavy chains forms the hub of the
CC triskelion. This region contains the trimerization domain and the
CC light-chain binding domain involved in the assembly of the clathrin
CC lattice.
CC -!- DOMAIN: The N-terminal seven-bladed beta-propeller is formed by WD40-
CC like repeats, and projects inward from the polyhedral outer clathrin
CC coat. It constitutes a major protein-protein interaction node (By
CC similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the clathrin heavy chain family. {ECO:0000305}.
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DR EMBL; CU329670; CAA93228.1; -; Genomic_DNA.
DR PIR; T38393; T38393.
DR RefSeq; NP_594148.1; NM_001019572.2.
DR AlphaFoldDB; Q10161; -.
DR SMR; Q10161; -.
DR BioGRID; 278555; 6.
DR STRING; 4896.SPAC26A3.05.1; -.
DR iPTMnet; Q10161; -.
DR MaxQB; Q10161; -.
DR PaxDb; Q10161; -.
DR PRIDE; Q10161; -.
DR EnsemblFungi; SPAC26A3.05.1; SPAC26A3.05.1:pep; SPAC26A3.05.
DR GeneID; 2542078; -.
DR KEGG; spo:SPAC26A3.05; -.
DR PomBase; SPAC26A3.05; chc1.
DR VEuPathDB; FungiDB:SPAC26A3.05; -.
DR eggNOG; KOG0985; Eukaryota.
DR HOGENOM; CLU_002136_0_0_1; -.
DR InParanoid; Q10161; -.
DR OMA; QVNEACV; -.
DR PhylomeDB; Q10161; -.
DR Reactome; R-SPO-196025; Formation of annular gap junctions.
DR Reactome; R-SPO-432720; Lysosome Vesicle Biogenesis.
DR Reactome; R-SPO-437239; Recycling pathway of L1.
DR Reactome; R-SPO-8856828; Clathrin-mediated endocytosis.
DR Reactome; R-SPO-8866427; VLDLR internalisation and degradation.
DR Reactome; R-SPO-8964038; LDL clearance.
DR Reactome; R-SPO-9013420; RHOU GTPase cycle.
DR Reactome; R-SPO-9013424; RHOV GTPase cycle.
DR PRO; PR:Q10161; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0030479; C:actin cortical patch; IDA:PomBase.
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; IBA:GO_Central.
DR GO; GO:0005737; C:cytoplasm; HDA:PomBase.
DR GO; GO:0005829; C:cytosol; IEA:GOC.
DR GO; GO:0032051; F:clathrin light chain binding; IBA:GO_Central.
DR GO; GO:0005198; F:structural molecule activity; ISO:PomBase.
DR GO; GO:0006895; P:Golgi to endosome transport; IBA:GO_Central.
DR GO; GO:0006886; P:intracellular protein transport; IC:PomBase.
DR GO; GO:0006898; P:receptor-mediated endocytosis; IBA:GO_Central.
DR Gene3D; 1.25.40.10; -; 4.
DR Gene3D; 2.130.10.110; -; 1.
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 Pfam; PF00637; Clathrin; 7.
DR Pfam; PF09268; Clathrin-link; 1.
DR Pfam; PF01394; Clathrin_propel; 1.
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 Coated pit; Cytoplasmic vesicle; Membrane; Phosphoprotein;
KW Reference proteome; Repeat.
FT CHAIN 1..1666
FT /note="Probable clathrin heavy chain"
FT /id="PRO_0000205784"
FT REPEAT 534..680
FT /note="CHCR 1"
FT REPEAT 683..825
FT /note="CHCR 2"
FT REPEAT 830..969
FT /note="CHCR 3"
FT REPEAT 975..1120
FT /note="CHCR 4"
FT REPEAT 1124..1265
FT /note="CHCR 5"
FT REPEAT 1270..1415
FT /note="CHCR 6"
FT REPEAT 1418..1561
FT /note="CHCR 7"
FT REGION 24..67
FT /note="WD40-like repeat 1"
FT REGION 68..107
FT /note="WD40-like repeat 2"
FT REGION 108..148
FT /note="WD40-like repeat 3"
FT REGION 149..194
FT /note="WD40-like repeat 4"
FT REGION 195..255
FT /note="WD40-like repeat 5"
FT REGION 256..299
FT /note="WD40-like repeat 6"
FT REGION 300..328
FT /note="WD40-like repeat 7"
FT MOD_RES 392
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 393
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
SQ SEQUENCE 1666 AA; 190018 MW; 16A6E84FEA2A7EA9 CRC64;
MAQQLPIRFS EVLQLASVGI QPSSFGFANV TLESDKYVCV RDNPNGVNQV VIVDLEDPSN
VLRRPISADS VILHPKKKII ALKAQRQLQV FDLEAKAKIN SYVMNQDVVY WTWISDSVIG
MVTDTSVFHW TVSGSDPVKM FDRHSSLNGT QIISYKSNYN EEWFTLIGIS SRDNRIAGNL
QLYSKKRKVS QPLESHASAF AVIQPEGVDH EVQVLALASR LPTGSKLSIV EVDRNPNNPA
FATKTVDLFF PPEAVNDFPI AIEIGSTYNV AYVVTKYGFI HVYDLETAKC IYMNRVSGES
IFVTTAHKSV NGLMAINRKG QVLSVSINPE TIIPYILSNL NDPGLAVRMA SHANLPGADN
LYMQQFQQLM AQGNYSEAAK VAASSPRGIL RTSQVIDQFK LIQAAPGQIA PILQYFGTLL
DKGPLNEHET IELARPVLAQ NRIQLLEKWY GENKLACTEA LGDLVKPYNT PFALKIYETA
NVPNKVVMCL SELGDFGKLA TYTSQQNITP DYVSLLQNLV RVNPDQAAEF ATQMFNSNPS
INLEKIVDIF MSQNLVQQAT AFLLDALKDD NPEHSHLQTR LLEINLINAP QVADAILGNQ
MFTHFDRAVI ASLCERAGLV QRALELYDKP ADIKRVIVHS NLLNPEWLMN YFSRFSPDEV
YDYLREMLRS NLRQNLQIVV QIATRYSDLV GAQRIIEMFE KFKTFEGLYY YLGSIVNITE
DPEVVYKYIQ AACLMNQFTE VERICRDNNV YNPEKVKNLL KEAKLADQLP LILVCDRYDF
VNDLVFYLFR NNMFQFIEIY VQRINPSKTP QVVGALLDID CDEELVQNLL MSVVGQVPVD
ELVEEVERRN RLKLLLPYLE SLLQSGSQDR AIYDALAKIY IDSNNNPEVF LKENNFYDTL
TVGKYCEKRD PYLAFIAYEK GGNDTEIINL CNENSMFKQL ARYLLKRSDS NLWSEVLQDS
AYRRPLLDQV IATAVPESSD PEAVSIVVKA LMEVDLPSQL IELLEKIVLQ PSSFSENANL
QNLLFLTAIK ADKSRVMEYI DKLDKYDVDE IAEIAIENGL YEEAFRIYKI HNKHEQAMKV
LVEDIVSLDR AQDYAETVEQ PEVWSRLAKA QLDGIRIPDA IESYLKADDP SNYSEVIELA
SRAGKYEELI KYLLMARSKM HEPDVDSALL IAYAKTNQLT EMETFLIGSN VADVKAVGDE
CFESKNYEAA KLMYSSISNW SMLATTLVYL GEYQGAVDCA RKANSIKVWK QVGTACIDKR
EFRLAQICGL NLIVHAEELP GLIRLYEERG YFEEVISLME AGLGLERAHM AFYTELAILY
AKYKPERMME HLKLFWGRLN MAKVIRACDQ MHLWNEAVFL YVHDQSYDNA AAVMMEQPEA
FDHQSFKDII VHVANLELYY RALNFYLEQH PMLLTDLLAA LTPRIDHPRV IRIFEKSENT
PLILNFMVAI QHLNIQAVNH AYNDLLIEME DYQSLQDSIE NYDHFDAIAL ARRLEKHSLL
EFRRIAAYIY RKNKRWTQSI ELSKQDRFYK DAIITARDSD QTTIAEDLMK YFVEIGNYEC
FAAILYTCYH LLRNDLVMEI SWRKGLQDYA YPYFINFQCE MFSKVLNLEK DLKDRQAVKS
EEESASTIGA GILGNTLMLT QGPMANNNDQ FDSFQQASPM PRLGNF
