(data stored in SCRATCH zone)

SWISSPROT: C1E1W7_MICCC

ID   C1E1W7_MICCC            Unreviewed;      1691 AA.
AC   C1E1W7;
DT   26-MAY-2009, integrated into UniProtKB/TrEMBL.
DT   26-MAY-2009, sequence version 1.
DT   05-JUL-2017, entry version 39.
DE   RecName: Full=Clathrin heavy chain {ECO:0000256|PIRNR:PIRNR002290};
GN   ORFNames=MICPUN_105289 {ECO:0000313|EMBL:ACO61813.1};
OS   Micromonas commoda (strain RCC299 / NOUM17 / CCMP2709) (Picoplanktonic
OS   green alga).
OC   Eukaryota; Viridiplantae; Chlorophyta; prasinophytes; Mamiellophyceae;
OC   Mamiellales; Mamiellaceae; Micromonas.
OX   NCBI_TaxID=296587 {ECO:0000313|EMBL:ACO61813.1, ECO:0000313|Proteomes:UP000002009};
RN   [1] {ECO:0000313|EMBL:ACO61813.1, ECO:0000313|Proteomes:UP000002009}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RCC299 / NOUM17 {ECO:0000313|Proteomes:UP000002009};
RX   PubMed=19359590; DOI=10.1126/science.1167222;
RA   Worden A.Z., Lee J.H., Mock T., Rouze P., Simmons M.P., Aerts A.L.,
RA   Allen A.E., Cuvelier M.L., Derelle E., Everett M.V., Foulon E.,
RA   Grimwood J., Gundlach H., Henrissat B., Napoli C., McDonald S.M.,
RA   Parker M.S., Rombauts S., Salamov A., Von Dassow P., Badger J.H.,
RA   Coutinho P.M., Demir E., Dubchak I., Gentemann C., Eikrem W.,
RA   Gready J.E., John U., Lanier W., Lindquist E.A., Lucas S., Mayer K.F.,
RA   Moreau H., Not F., Otillar R., Panaud O., Pangilinan J., Paulsen I.,
RA   Piegu B., Poliakov A., Robbens S., Schmutz J., Toulza E., Wyss T.,
RA   Zelensky A., Zhou K., Armbrust E.V., Bhattacharya D., Goodenough U.W.,
RA   Van de Peer Y., Grigoriev I.V.;
RT   "Green evolution and dynamic adaptations revealed by genomes of the
RT   marine picoeukaryotes Micromonas.";
RL   Science 324:268-272(2009).
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}.
CC   -!- SIMILARITY: Belongs to the clathrin heavy chain family.
CC       {ECO:0000256|PIRNR:PIRNR002290}.
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DR   EMBL; CP001324; ACO61813.1; -; Genomic_DNA.
DR   RefSeq; XP_002500555.1; XM_002500509.1.
DR   GeneID; 8242171; -.
DR   KEGG; mis:MICPUN_105289; -.
DR   HOGENOM; HOG000188877; -.
DR   InParanoid; C1E1W7; -.
DR   KO; K04646; -.
DR   Proteomes; UP000002009; Chromosome 3.
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:0048268; P:clathrin coat assembly; 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; 1.25.40.10; -; 4.
DR   Gene3D; 1.25.40.30; -; 1.
DR   InterPro; IPR016024; ARM-type_fold.
DR   InterPro; IPR000547; Clathrin_H-chain/VPS_repeat.
DR   InterPro; IPR012331; Clathrin_H-chain_linker.
DR   InterPro; IPR015348; Clathrin_H-chain_linker_core.
DR   InterPro; IPR001473; Clathrin_H-chain_propeller_N.
DR   InterPro; IPR022365; Clathrin_H-chain_propeller_rpt.
DR   InterPro; IPR016341; Clathrin_heavy_chain.
DR   InterPro; IPR011990; TPR-like_helical_dom.
DR   Pfam; PF00637; Clathrin; 7.
DR   Pfam; PF09268; Clathrin-link; 1.
DR   Pfam; PF01394; Clathrin_propel; 2.
DR   PIRSF; PIRSF002290; Clathrin_H_chain; 1.
DR   SMART; SM00299; CLH; 7.
DR   SUPFAM; SSF48371; SSF48371; 5.
DR   SUPFAM; SSF50989; SSF50989; 1.
DR   PROSITE; PS50236; CHCR; 7.
PE   3: Inferred from homology;
DR   PRODOM; C1E1W7.
DR   SWISS-2DPAGE; C1E1W7.
KW   Coated pit {ECO:0000256|PIRNR:PIRNR002290};
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Complete proteome {ECO:0000313|Proteomes:UP000002009};
KW   Cytoplasmic vesicle {ECO:0000256|PIRNR:PIRNR002290};
KW   Membrane {ECO:0000256|PIRNR:PIRNR002290};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002009}.
FT   DOMAIN      346    366       Clathrin-link. {ECO:0000259|Pfam:
FT                                PF09268}.
FT   REPEAT      549    695       CHCR. {ECO:0000256|PROSITE-ProRule:
FT                                PRU01006}.
FT   REPEAT      698    840       CHCR. {ECO:0000256|PROSITE-ProRule:
FT                                PRU01006}.
FT   REPEAT      845    984       CHCR. {ECO:0000256|PROSITE-ProRule:
FT                                PRU01006}.
FT   REPEAT      991   1136       CHCR. {ECO:0000256|PROSITE-ProRule:
FT                                PRU01006}.
FT   REPEAT     1140   1281       CHCR. {ECO:0000256|PROSITE-ProRule:
FT                                PRU01006}.
FT   REPEAT     1286   1431       CHCR. {ECO:0000256|PROSITE-ProRule:
FT                                PRU01006}.
FT   REPEAT     1434   1577       CHCR. {ECO:0000256|PROSITE-ProRule:
FT                                PRU01006}.
FT   COILED     1626   1649       {ECO:0000256|SAM:Coils}.
SQ   SEQUENCE   1691 AA;  189755 MW;  465174038173D4AF CRC64;
     MAAPPVTVKE VVSLTSSGIN PQNISFTNLT MESEKFICVR ETGAANSVVI VDMAQPMTPM
     KRPITADSAL MNPAAKVIAL KATVAGTAQD HLQIFNIDTK SKMKSHQMPE SVVYWRWISP
     SLMGIVTNTA VYHWSMEGDS EPQKMFDRTG NLNGCQIIAY RASQDMKWFS VVGIAAGDPS
     RPGLVKGKMQ LFSKELGRSQ ELDAHACAFS THQVTGNSVK SQVIAFAQKT VMPDGNVASK
     LHVIELGAQA GQTPFQKRQA ELFFPPEFMD DFPVNMSISE KYGVIYVVTK MGLLFVYDLE
     TATAIYRNKV SNDPVFLACD SPSTGGVYAV NRRGQVLLLN LNEPAVVPFI SGQLNNVSLA
     LQVAVRGGLP GAESLVKPKF EQLFAAGDIK GAAECAADSP KGILRNPETI ARFKAIPAQP
     GAAPPLLQYF GICLQRGTLN KVEGVELARL VLAQNKKQLL DTWMAEDKIE CSEELGDLLQ
     SVDADMALRV YIKAKANTKV VAALAARGEF EKMGKYCEMA DYKPDYSYLL QSTLMSNPQG
     AVTIALQVSK MNPPPLDYNT VADLFLQRNM IREATSFLLD VLKEDREDQA AMQTKVLEIN
     LVTFPNVADA ILGQGKLTHY DRPRIAQLCE KAGLYMRALE HYTEVSDLKR CCVNTHSIDP
     QALLEWFGTL SREWALECIK ELLVSNPRQN LQIIVNVCKE YTEQIGADAI LKLLEEHNSS
     EGMFFYLGAL VATSTEPDHH QKYIEAAAKT GQIKEVERIT RESEHYDPEK AKVFLMEAKL
     PDARPLINVC DRFDMVDDLT TFLYQNKMLR YIEGYVQKVN PSNTPVVVGA LLDLECDEDF
     VQNLILSVRS LLPVGPLVEE VSKRNRLKML TPFLENLVAE GSTNADVHNA LGMILIDSNT
     NPEHFLTTNE YYDSKVVGKY CEKRDPNLAC VAYKRGNCDL ELVEVTNKNS LFKLQSRYVV
     ERMDADLWEH VLAEDNPHRR QLIDQVVSTA LPESKNPEQV SVTVKAFMTA EMPQELIELL
     EKIVIQNSAF SNNPNLQNLL ILTAIKADTT RVMDYINRLD AFNGPEVGEI AVGNELYEEA
     FAIFKKFDLH VDAMKVLLEN LENLERGEEY ANKVDLPEVW SQLAKAYLSQ DLVSAAVAAY
     IKAKYTDDYL AVIDVAKRAD DFDSMVKYLA MVRKKVKEPK VDSELCYAYA KTDKLAELEE
     FITQPNAAKL DNVGDRCFDE GLYEAAKVLF TTCSNWGRLA STLVKLHKFS EAVDAARKAN
     NTRTWKEICF ACVDEGEFRL AQLCALNIIV NADELEEISE YYQVRGRYEE LLSLMEAGVG
     LERAHMGIFT ELGILYAKFK PEKLMEHLKL FSTRINIPKL IRACEEMHAW KELSFLYIAY
     DEYDNAAGVM MAHPDAWEHV GFKDVCVKVA NLEIYYKALE FYLVSHPTQL NDLLTVLTPR
     IDHSRVVALM RQANHLPLIK PYLQAVQNTN MVAVNDAVNE LCLEEEDFES LRTSIDTYDN
     FDQMSLANKC EKHELLEFRR IAGFLYQKNA KWTKSVELSK KDGLYKDAME AAAQSGDKDI
     AGDLLQFFIE QENKECFAAM LYNCYDLLKP DEVLEIAWMK GLMEYAMPYM IQVMKDYTNK
     VDVLVEDKKD RNKEKADQEK EKVEQQMNQN MYAQLLPAAL PAPGMETTGG MNNPGMYGQM
     GGVQPGMYGG Y
//

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