ID M4BYZ2_HYAAE Unreviewed; 1691 AA.
AC M4BYZ2;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 39.
DE RecName: Full=Clathrin heavy chain {ECO:0000256|PIRNR:PIRNR002290};
OS Hyaloperonospora arabidopsidis (strain Emoy2) (Downy mildew agent)
OS (Peronospora arabidopsidis).
OC Eukaryota; Sar; Stramenopiles; Oomycota; Peronosporales; Peronosporaceae;
OC Hyaloperonospora.
OX NCBI_TaxID=559515 {ECO:0000313|EnsemblProtists:HpaP811790, ECO:0000313|Proteomes:UP000011713};
RN [1] {ECO:0000313|Proteomes:UP000011713}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Emoy2 {ECO:0000313|Proteomes:UP000011713};
RX PubMed=21148394; DOI=10.1126/science.1195203;
RA Baxter L., Tripathy S., Ishaque N., Boot N., Cabral A., Kemen E.,
RA Thines M., Ah-Fong A., Anderson R., Badejoko W., Bittner-Eddy P.,
RA Boore J.L., Chibucos M.C., Coates M., Dehal P., Delehaunty K., Dong S.,
RA Downton P., Dumas B., Fabro G., Fronick C., Fuerstenberg S.I., Fulton L.,
RA Gaulin E., Govers F., Hughes L., Humphray S., Jiang R.H., Judelson H.,
RA Kamoun S., Kyung K., Meijer H., Minx P., Morris P., Nelson J.,
RA Phuntumart V., Qutob D., Rehmany A., Rougon-Cardoso A., Ryden P.,
RA Torto-Alalibo T., Studholme D., Wang Y., Win J., Wood J., Clifton S.W.,
RA Rogers J., Van den Ackerveken G., Jones J.D., McDowell J.M., Beynon J.,
RA Tyler B.M.;
RT "Signatures of adaptation to obligate biotrophy in the Hyaloperonospora
RT arabidopsidis genome.";
RL Science 330:1549-1551(2010).
RN [2] {ECO:0000313|EnsemblProtists:HpaP811790}
RP IDENTIFICATION.
RC STRAIN=Emoy2 {ECO:0000313|EnsemblProtists:HpaP811790};
RG EnsemblProtists;
RL Submitted (JUN-2015) 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 EMBL; JH598052; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR STRING; 559515.M4BYZ2; -.
DR EnsemblProtists; HpaT811790; HpaP811790; HpaG811790.
DR VEuPathDB; FungiDB:HpaG811790; -.
DR HOGENOM; CLU_002136_0_0_1; -.
DR InParanoid; M4BYZ2; -.
DR Proteomes; UP000011713; Unassembled WGS sequence.
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; 3.
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:SF1; CLATHRIN HEAVY CHAIN; 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; 1.
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 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:UP000011713};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 78..101
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 308..328
FT /note="Clathrin heavy chain linker core motif"
FT /evidence="ECO:0000259|Pfam:PF09268"
SQ SEQUENCE 1691 AA; 191182 MW; 282B2DD0578C80B5 CRC64;
MESDKFVCVC EQVNGQASVV IVDMAAGNTV QRRPINAEAA IMNPVSKVIA LRAENQLQIF
NMELRAKMKS HLMNEAVVFW RWISVNTIAI VTASAVFHWS IEGDSSPVKI FDRHANLGAG
TQIISYEASA DNQWMLLVGI SQGDGGRIVG NMQLYSMEKK VSQVLLGHAG AFAQMKPPSR
TDDAQVLIFA GTKGDGQPTQ LFIMEVGRDR DAPGGVFRLP PQPIPFAADA QADFPVSMLV
TPGDDVVYMI TKMGYLFLFD THSGKPVYRA RVSQDTTFVT CLESKSKGML GITRRGQLLH
FAINKTKLVP YVVNTLRDSQ LALSLATRLD LPGAEELYFT EFNRLVSVND IQGAARLAAA
SPQGALRTPQ TIQRFQQMPA QPGQPQPILQ YFSVLLEKGT LNKMESIELA RPVLMQGRGQ
LLQKWLSEDK LECSEELGDL VAQSDTTMAL SVYLRAEVPE KVINCFVQRG DFDKIVAYAV
QTNYRCDYTF MLQNLVRANP QGALDFAQKL AVAENGPLVD VNAVVDIFMQ VNRIQETTAF
LLEALKNNRP EEGYLQTRLL EINLLGGSPQ VADAILSNNM FTHYDRPRIA ALCEKAGLFQ
RALEHYTELA DLKRVIVNTQ AINHEFIVTF FGTLTSEISM ELINALMAHN MRQNLQIVVQ
VATKYAEQLG GKELVEVFEK FKSFDGLYFF LGSIVNFSQD PDLHFKYIEA ATKMGQFKEV
ERVCRDSSVY DPVKVKEFLK ESKLQDPRPL IHVCDRYDFV EELTQYLYSN NLMKYIDVYV
TKVSPQKAPI VIGKLLDLDC NEDYIKNLLN QIAQCPVDDL CEQVEKRNRL RLLQPWLETR
VAQGNTETAT HNAIGKIYIT LNKDPQQFLI NNQFYDSDVV GKFCEKLDPA LAYLAYRRAG
GTCDDDLVRV TTENGLFKDL ARYLVERQDL DLWGKVLVKQ EEGEPESPSC RALIDQVVQT
ALPETTNPDE VSTTVRAFMN AELPNELIEL LERIVLQGTD FSTNKNLQNL LILTAIKAGK
EKVMDYVNRL DNFDGPEIAR IAVGEQYQLY EEGFVIYKKT NHNVEAIGVL LDFIKDNERA
YEFADRCNES EVWSRLAKAQ LDQGEVHDSL SAFIKANDAS SYVDVIAAAE RIDNYNELIP
YLKMARNTVK EQYLDTSLIY AYAKTEKYSD LEEFISSPNV AQIQNIGERC YDEGMYTAAK
LLFQNINNNA KLAICYVRLG KFREAVDAAT KANSVGTWKE VNYACVDVNE FRLAALCGLH
IVVHPDHLEE LILHYEKRGH STELLKLMEQ GLGLEGAHAG IFTELAILYS KYMPSKLMEH
IKIFHSRMNV SKILRACEKG LHWDHAVYLY KEDGQFDNAV RTMVDHPVAF SHDLFLDCIQ
KVRNQEIHYK AINFYLEQHP LELTRLLQVL TPNLDHARVV HQLRKSNNLL LVVEYLKDVQ
KENLSAVNEA LNEILLEDED YQALRESVDS YENFDQISLA QKLEKHELLE FRRIAAYLYR
KNKRYPQSVK LSKADKMYKD CIDCASDSDD PELAEDILRF FVSVHDKECF CATLFTCYKL
IRPDVALELA WRHGYTDFVM PYMIQFVKNL NDKVKVLDER TQTQQEPETD AQSLDPAYGM
GGMQPMLAIA PTAYNDPSAQ YGMGMAPGMN MALGMQPNMA MSGMQQNPYA SSQGSMGSMG
SNPYGTSGYQ Y
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