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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
 
 
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