UniProt: A9T0L4

Database: UniProt
Entry: A9T0L4_PHYPA

LinkDB:  A9T0L4_PHYPA 
Original site:  A9T0L4_PHYPA

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Ontology (7)   
   GO (7)   
Protein sequence (1)   
   RefSeq(pep) (1)   
DNA sequence (1)   
   EMBL (1)   
Protein domain (13)   
   InterPro (7)   
   Pfam (4)   
   PROSITE (1)   
   SMART (1)   
Literature (2)   
   PubMed (2)   
All databases (24)   

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ID   A9T0L4_PHYPA            Unreviewed;      1709 AA.
AC   A9T0L4;
DT   05-FEB-2008, integrated into UniProtKB/TrEMBL.
DT   05-FEB-2008, sequence version 1.
DT   27-MAR-2024, entry version 94.
DE   RecName: Full=Clathrin heavy chain {ECO:0000256|PIRNR:PIRNR002290};
GN   ORFNames=PHYPA_001752 {ECO:0000313|EMBL:PNR63327.1};
OS   Physcomitrium patens (Spreading-leaved earth moss) (Physcomitrella patens).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Bryophyta;
OC   Bryophytina; Bryopsida; Funariidae; Funariales; Funariaceae; Physcomitrium.
OX   NCBI_TaxID=3218 {ECO:0000313|EMBL:PNR63327.1};
RN   [1] {ECO:0000313|EMBL:PNR63327.1, ECO:0000313|Proteomes:UP000006727}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Gransden 2004 {ECO:0000313|EnsemblPlants:Pp3c1_37710V3.1,
RC   ECO:0000313|Proteomes:UP000006727};
RX   PubMed=18079367; DOI=10.1126/science.1150646;
RA   Rensing S.A., Lang D., Zimmer A.D., Terry A., Salamov A., Shapiro H.,
RA   Nishiyama T., Perroud P.-F., Lindquist E.A., Kamisugi Y., Tanahashi T.,
RA   Sakakibara K., Fujita T., Oishi K., Shin-I T., Kuroki Y., Toyoda A.,
RA   Suzuki Y., Hashimoto S.-I., Yamaguchi K., Sugano S., Kohara Y.,
RA   Fujiyama A., Anterola A., Aoki S., Ashton N., Barbazuk W.B., Barker E.,
RA   Bennetzen J.L., Blankenship R., Cho S.H., Dutcher S.K., Estelle M.,
RA   Fawcett J.A., Gundlach H., Hanada K., Heyl A., Hicks K.A., Hughes J.,
RA   Lohr M., Mayer K., Melkozernov A., Murata T., Nelson D.R., Pils B.,
RA   Prigge M., Reiss B., Renner T., Rombauts S., Rushton P.J., Sanderfoot A.,
RA   Schween G., Shiu S.-H., Stueber K., Theodoulou F.L., Tu H., Van de Peer Y.,
RA   Verrier P.J., Waters E., Wood A., Yang L., Cove D., Cuming A.C., Hasebe M.,
RA   Lucas S., Mishler B.D., Reski R., Grigoriev I.V., Quatrano R.S.,
RA   Boore J.L.;
RT   "The Physcomitrella genome reveals evolutionary insights into the conquest
RT   of land by plants.";
RL   Science 319:64-69(2008).
RN   [2] {ECO:0000313|EMBL:PNR63327.1, ECO:0000313|Proteomes:UP000006727}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Gransden 2004 {ECO:0000313|EnsemblPlants:Pp3c1_37710V3.1,
RC   ECO:0000313|Proteomes:UP000006727};
RX   PubMed=29237241; DOI=10.1111/tpj.13801;
RA   Lang D., Ullrich K.K., Murat F., Fuchs J., Jenkins J., Haas F.B.,
RA   Piednoel M., Gundlach H., Van Bel M., Meyberg R., Vives C., Morata J.,
RA   Symeonidi A., Hiss M., Muchero W., Kamisugi Y., Saleh O., Blanc G.,
RA   Decker E.L., van Gessel N., Grimwood J., Hayes R.D., Graham S.W.,
RA   Gunter L.E., McDaniel S.F., Hoernstein S.N.W., Larsson A., Li F.W.,
RA   Perroud P.F., Phillips J., Ranjan P., Rokshar D.S., Rothfels C.J.,
RA   Schneider L., Shu S., Stevenson D.W., Thummler F., Tillich M.,
RA   Villarreal Aguilar J.C., Widiez T., Wong G.K., Wymore A., Zhang Y.,
RA   Zimmer A.D., Quatrano R.S., Mayer K.F.X., Goodstein D., Casacuberta J.M.,
RA   Vandepoele K., Reski R., Cuming A.C., Tuskan G.A., Maumus F., Salse J.,
RA   Schmutz J., Rensing S.A.;
RT   "The Physcomitrella patens chromosome-scale assembly reveals moss genome
RT   structure and evolution.";
RL   Plant J. 93:515-533(2018).
RN   [3] {ECO:0000313|EnsemblPlants:Pp3c1_37710V3.1}
RP   IDENTIFICATION.
RG   EnsemblPlants;
RL   Submitted (DEC-2020) 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; ABEU02000001; PNR63327.1; -; Genomic_DNA.
DR   RefSeq; XP_001772180.1; XM_001772128.1.
DR   STRING; 3218.A9T0L4; -.
DR   PaxDb; 3218-PP1S147_10V6-1; -.
DR   EnsemblPlants; Pp3c1_37710V3.1; Pp3c1_37710V3.1; Pp3c1_37710.
DR   EnsemblPlants; Pp3c1_37710V3.2; Pp3c1_37710V3.2; Pp3c1_37710.
DR   Gramene; Pp3c1_37710V3.1; Pp3c1_37710V3.1; Pp3c1_37710.
DR   Gramene; Pp3c1_37710V3.2; Pp3c1_37710V3.2; Pp3c1_37710.
DR   eggNOG; KOG0985; Eukaryota.
DR   HOGENOM; CLU_002136_0_0_1; -.
DR   InParanoid; A9T0L4; -.
DR   OMA; HTRVMDY; -.
DR   OrthoDB; 5474327at2759; -.
DR   Proteomes; UP000006727; Chromosome 1.
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:0032051; F:clathrin light chain binding; IBA:GO_Central.
DR   GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
DR   GO; GO:0006886; P:intracellular protein transport; IEA:UniProtKB-UniRule.
DR   GO; GO:0006898; P:receptor-mediated endocytosis; IBA:GO_Central.
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; 2.
DR   PIRSF; PIRSF002290; Clathrin_H_chain; 1.
DR   SMART; SM00299; CLH; 7.
DR   SUPFAM; SSF48371; ARM repeat; 5.
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   Coiled coil {ECO:0000256|SAM:Coils};
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:UP000006727};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT   DOMAIN          344..366
FT                   /note="Clathrin heavy chain linker core motif"
FT                   /evidence="ECO:0000259|Pfam:PF09268"
FT   COILED          1617..1652
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   1709 AA;  192847 MW;  E69AB52116E7C740 CRC64;
     MAAASAPITM KEALTLTSLG INQQFVTFTH VTMESDKYIC VRETSPQNSV VIIDMSMPNQ
     PLRRPITADS ALMNPNSRVL ALKALIPGST QDHLQIFNIE LKAKMKSYQM PEQVVFWKWI
     SPRLLGLVTQ TSVYHWTIEG ESEPVKMFER TANLSGNQII NYRCDPAEKW LVLIGIAPGA
     PERPQLVKGN MQLFSVDQQR SQALEAHAAS FASHQVAGND SPSLLIAFTT KTLTAGQLTS
     KLHIIELGAT PGKPGFSKKA ADLFFPPDFA DDFPVSMQIS SKYGLIYVIT KLGLLFVYDL
     ETATAVYRNR ISPDPIFLTA DAPTVGGFYA VNRRGQVLLA TVNEATIIPF VSNQLSNLEL
     AVNLARRGNL PGAEGLVVQR FQELFSQMKY KEAADLAAES PQGILRTPDT VAKFQSVPVQ
     PGQTSPLLQY FGTLLTKGKL NVFESLELSR LVVNQNKKNL LENWLAEDKL ECSEELGDLV
     KTVDNDMALK IYIKARATPK VVAAFAERRE FDKILIYSKQ VGYTPDYLFL LQTILRADPQ
     GAVNFALMMS QLEGGCPVDY NTVTDLFLQR NMIREATAFL LDVLKPNLPE HALLQTKVLE
     INLVTFPNVA DAILANGMFS HYDRPRVAQL CEKAGLYMRA LQHYTELNDI KRVVINTHAI
     EPQGLVEFFG TLSKEWALDC MKELLQVNMR GNLQIIVQVA KEYGEQLGVD ACVKLFESFK
     SFEGLYFFLG AYLSTSEEPE IHYKYIEAAA KTGQIKEVER VTRESNFYPP ERTKNFLMES
     KLPDARPLIN VCDRHGFVPD LTHYLYVNNM LRYIEGYVQK VNPQNAPLVV GQLLDDDCPE
     DFIKGLILSV RSLLPVEPLV DECEKRNRLR LLTQFLEHLV SEGSQDVHVH NALGKIIIDT
     NNNPEHFLTT NPYYDSKVVG KYCEKRDPTL AVVAYKRGNC DDELVNVTNK NSLFKLQARY
     VVERMEPDLW LKVLNPENPC RRQLIDQVVS TALPESKNPE QVSATVKAFM TADLPHELIE
     LLEKIVLQNS AFSGNPNLQN LLILTAIKAD TTRVMDYINR LDNFDGPAVG EIAVGAELYE
     EAFAIFKKFN LNVQAVNVLL DNIRNIDRAV EFAARVEEDD VWSQVGKAQL REGLVSDAIE
     SFIKANDASQ YNEVIDVASG VRAYEDLVRY LNMVRKKVKE AKVDSELIFA YAKLNRLDDI
     EEFIVNPNLA NLQTVGDRLF DGELYEAAKI IFTHISNWAR LASTLVKLHQ FQAAVDAARK
     ANSARTWKEV CFACVDAEEF RLAQICGLNV IVQVDDLEEV SEYYQNRGRF DELISLMESG
     LGLERAHMGI FTELGTLYAR YRPDKLMEHL KLFITRINIP KLIRVCDEQQ HWKELTYLYI
     AYDEYDNAAA TMMSHSPEAW EHMQFKDVAV KVANVELYYK AVYFYLEEYP ELINDLLNVL
     SARVDHTRVV DIMKKAGYLP LVKPYMVAVQ SANNAAVNEA LNNLYIEEED YERLRESIDM
     YDNFDQISMA QRIEKHELLE MRRVGAYIYK RAGRWKQSVA LSKKDNLYKD AMETCSQSGD
     RELAEELLTF FVDKGKKECF AACLYTCYDL IRADVAVELA WMHGMMDFAV PYLLQFLREY
     STKVDDLIKD KLEATEEKKS KEQQEKDVVA ESNMYAQLLP LALPAPPVAG MTGMPGMGGG
     MPMPGMSGMP GMPGMPGMSG YGMPSMSAF
//

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