ID U4L5Z7_PYROM Unreviewed; 1687 AA.
AC U4L5Z7;
DT 11-DEC-2013, integrated into UniProtKB/TrEMBL.
DT 11-DEC-2013, sequence version 1.
DT 27-MAR-2024, entry version 49.
DE RecName: Full=Clathrin heavy chain {ECO:0000256|PIRNR:PIRNR002290};
GN ORFNames=PCON_11326 {ECO:0000313|EMBL:CCX11732.1};
OS Pyronema omphalodes (strain CBS 100304) (Pyronema confluens).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Pezizomycetes;
OC Pezizales; Pyronemataceae; Pyronema.
OX NCBI_TaxID=1076935 {ECO:0000313|EMBL:CCX11732.1};
RN [1] {ECO:0000313|EMBL:CCX11732.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS100304 {ECO:0000313|EMBL:CCX11732.1};
RC TISSUE=Vegetative mycelium {ECO:0000313|EMBL:CCX11732.1};
RX PubMed=24068976; DOI=10.1371/journal.pgen.1003820;
RA Traeger S., Altegoer F., Freitag M., Gabaldon T., Kempken F., Kumar A.,
RA Marcet-Houben M., Poggeler S., Stajich J.E., Nowrousian M.;
RT "The genome and development-dependent transcriptomes of Pyronema confluens:
RT a window into fungal evolution.";
RL PLoS Genet. 9:E1003820-E1003820(2013).
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|PIRNR:PIRNR002290}.
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DR EMBL; HF935642; CCX11732.1; -; Genomic_DNA.
DR STRING; 1076935.U4L5Z7; -.
DR eggNOG; KOG0985; Eukaryota.
DR OMA; HCYDLLH; -.
DR OrthoDB; 5474327at2759; -.
DR Proteomes; UP000018144; 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; 4.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR000547; Clathrin_H-chain/VPS_repeat.
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; PF13838; Clathrin_H_link; 1.
DR Pfam; PF01394; Clathrin_propel; 3.
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|PIRNR:PIRNR002290};
KW Cytoplasmic vesicle {ECO:0000256|ARBA:ARBA00023329,
KW ECO:0000256|PIRNR:PIRNR002290}; Membrane {ECO:0000256|PIRNR:PIRNR002290}.
FT REGION 1617..1644
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1617..1634
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1687 AA; 190847 MW; 4CA493AFED63F619 CRC64;
MAPLPIQFTE LLSLTQLDIA PTSIGFNTTT LESDRYICVR EKSDEASAQV VIIDLHNNNE
ITRRTIKADS AIMHWSRNII ALKAQRTLQI FDLDAKGKLK SYAMPEDVVF WKWISERSLG
LVTDTAVFHW DILDPAQAAP VKVFDRHVNL QGSQIINYRV NSDEKWMVVV GISSQQGRVV
GNLQLYSKDR TISQAIEGHA AAFAEIRMEG APSPTKLFTF SVRTPQGAKL HVVEVDHPAG
NPVFQKKAVD VYFPAEATND FPVAMQVSSR FSIIYLVTKY GFIHLYDLET GTCIFMNRIS
SETIFTTARH DSTSGILCVN RKGQVLSVSV DDNQIIPYLL QNPANSQLAI NLASRAGLAG
ADDLYQQQFN QLMAQNNFVE AAKVAANSPR GFLRTPQTIE KFKAVPAPPG QLSVILQYFG
MLLDKTTLNK YETIELVKPV LAQNRKHLLE KWLKEKKLEC TEELGDIVRP HDINMALEIY
LAANAPQKVV AAYAETGQFD KILPYAAETG YNPDYTGLLQ HIVRMNPEKG SEFANQLAGH
EGGALVDIDR VVDVFLSQSM IQAATAFLLT ALEKNNPEQG HQQTRLLEIN LLNAPQVAAA
ILGNNMFTYY DKAKIAQLCE NAGLFQQALE HYEDPAAIKR VLCNNAAGLN ADFVAGFFGR
MSVEDSLDCL KEMLRVNIRQ NLQIVVTIAT KYSDLLGPHR LIAMFESFKN FEGLYYYLGT
VVNLTEDGDV VFKYIEAATK CGQTSEVTRI CRENNFFNPE KVKNFLKEVP LTDYLPLIVV
CDRFNFVHDL ILYLYRNQQF ASIESYVQKV NPSRTPAVIG GLLDVDCDEN TVKGLLQSVP
ASMVPVDELV AEVERRNRLK MLLPFLESML AAGNEQTAVY NALAKIYIDS NNNPEKFLKE
NDKYDTAIVG SYCEKRDPYL AFIAYEKGQN DLELVKITNE NSMFKHQARY LVARRDPELW
QFVLSPNNIH RRPLVDQVVA TAVPESTDPE DVSTAVQSFL QNDLPTELLE LLEKIILEPS
AFSDNSNLQN LIILTAVKAD KARVMDYINR LNNYDGPDIA NICIENGLFE EALEVYKKAN
AHSDAINVLI EHIVSIDRAY AYADRVDLPE VWSRLGKAQI DGLRISDGID SYIRANDPSN
YLEVIEMSSR AGKHDELIKY LQMCRKTLRE PPIDSAMALS LARVNKLHEL EDFLNAANVA
NIEETGDLAY EEGLHQAAKI FFTSISNWAK LATTLVYLEE YQNAVECARK ANNIKVWKQV
HEACVAKKEF RLSQICGLNL IVHAEELHDV VRQYERAGYF DELISLLENG LGLERAHMGM
FTELGIALTK YHPEKVMEHL KLFWGRINIP KMIRACESAH LWPELIFLYC HYDEWDNAAL
AMMERAADAW EHQSFKDIIV KVANLEIYYR ALNFYLQEQP RMITDLLASL APRIDVARVV
RMFEQSDNIP LIKPFLLNVQ TQNNKVVNNA INDLLIEEED YKTLRDSVEN YDNYDPVELA
QRLEQHELVF FRQVAANIYR KHKRWSQSIA LSKQDKLFKD AIETAAVSGR EDVVDELLRY
FVDIGNRECY AAMLYACYDL IPVHTVMEIS WRYGLNDYAM PFMINVMREQ SMKISTLEKD
NEERKQREAS QQKTEEETPI LGRGPLMITA GSMGGAPQPY GNGMMPQQTG MMPQATGFAP
QPTGFGF
//
