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Database: UniProt
Entry: A0A087R026_APTFO
LinkDB: A0A087R026_APTFO
Original site: A0A087R026_APTFO 
ID   A0A087R026_APTFO        Unreviewed;      1662 AA.
AC   A0A087R026;
DT   29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   29-OCT-2014, sequence version 1.
DT   27-MAR-2024, entry version 24.
DE   SubName: Full=Clathrin heavy chain 1 {ECO:0000313|EMBL:KFM06830.1};
DE   Flags: Fragment;
GN   ORFNames=AS27_13509 {ECO:0000313|EMBL:KFM06830.1};
OS   Aptenodytes forsteri (Emperor penguin).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Sphenisciformes; Spheniscidae;
OC   Aptenodytes.
OX   NCBI_TaxID=9233 {ECO:0000313|EMBL:KFM06830.1, ECO:0000313|Proteomes:UP000053286};
RN   [1] {ECO:0000313|EMBL:KFM06830.1, ECO:0000313|Proteomes:UP000053286}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BGI_AS27 {ECO:0000313|EMBL:KFM06830.1};
RA   Zhang G., Li C.;
RT   "Genome evolution of avian class.";
RL   Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
CC   -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle membrane
CC       {ECO:0000256|ARBA:ARBA00004180}; Peripheral membrane protein
CC       {ECO:0000256|ARBA:ARBA00004180}; Cytoplasmic side
CC       {ECO:0000256|ARBA:ARBA00004180}. Membrane, coated pit
CC       {ECO:0000256|ARBA:ARBA00004277}; Peripheral membrane protein
CC       {ECO:0000256|ARBA:ARBA00004277}; Cytoplasmic side
CC       {ECO:0000256|ARBA:ARBA00004277}. 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}.
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DR   EMBL; KL226004; KFM06830.1; -; Genomic_DNA.
DR   STRING; 9233.A0A087R026; -.
DR   Proteomes; UP000053286; 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; 5.
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:SF7; CLATHRIN HEAVY CHAIN 1; 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; 5.
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};
KW   Cytoplasmic vesicle {ECO:0000256|ARBA:ARBA00023329};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136};
KW   Reference proteome {ECO:0000313|Proteomes:UP000053286};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT   DOMAIN          318..341
FT                   /note="Clathrin heavy chain linker core motif"
FT                   /evidence="ECO:0000259|Pfam:PF09268"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:KFM06830.1"
FT   NON_TER         1662
FT                   /evidence="ECO:0000313|EMBL:KFM06830.1"
SQ   SEQUENCE   1662 AA;  190061 MW;  EC8F064D19171A6A CRC64;
     QLQNLGINPA NIGFSTLTME SDKFICIREK VGEQAQVVII DMNDPSNPIR RPISADSAIM
     NPASKVIALK AGKTLQIFNI EMKSKMKAHT MTDDVTFWKW ISLNTVALVT DNAVYHWSME
     GESQPVKMFD RHSSLAGCQI INYRTDAKQK WLLLTGISAQ QNRVVGAMQL YSVDRKVSQP
     IEGHAASFAQ FKMEGNAEES TLFCFAVRGQ AGGKLHIIEV GTPPTGNQPF PKKAVDVFFP
     PEAQNDFPVA MQISDKHDVV FLITKYGYIH LYDLETGTCI YMNRISGETI FVTAQHEATA
     GIIGVNRKGQ VLSVCVEEEN IIPYITNVLQ NPDLALRMAV RNNLAGAEEL FARKFNALFA
     QGNYSEAAKV AANAPKGILR TPDTIRRFQS VPAQPGQTSP LLQYFGILLD QGQLNKYESL
     ELCRPVLQQG RKQLLEKWLK EDKLECSEEL GDLVKSVDPT LALSVYLRAN VPNKVIQCFA
     ETGQVQKIVL YAKKVGYTPD WIFLLRNVMR ISPDQGQQFA QMLVQDEEPL ADITQIVDVF
     MEYNLIQQCT AFLLDALKNN RPSEGPLQTR LLEMNLMHAP QVADAILGNQ MFTHYDRAHI
     AQLCEKAGLL QRALEHFTDL YDIKRAVVHT HLLNPEWLVN YFGSLSVEDS LECLRAMLSA
     NIRQNLQICV QVASKYHEQL STQSLIELFE SFKSFEGLFY FLGSIVNFSQ DPDVHFKYIQ
     AACKTGQIKE VERICRESNC YDPERVKNFL KEAKLTDQLP LIIVCDRFDF VHDLVLYLYR
     NNLQKYIEIY VQKVNPSRLP VVIGGLLDVD CSEDVIKNLI LVVRGQFSTD ELVAEVEKRN
     RLKLLLPWLE ARIHEGCEEP ATHNALAKIY IDSNNNPERF LRENPYYDSR VVGKYCEKRD
     PHLACVAYER GQCDLELINV CNENSLFKSL SRYLVRRKDP ELWASVLLES NPYRRPLIDQ
     VVQTALSETQ DPEEVSVTVK AFMTADLPNE LIELLEKIVL DNSVFSEHRN LQNLLILTAI
     KADRTRVMEY INRLDNYDAP DIANIAISNE LFEEAFAIFR KFDVNTSAVQ VLIEHIGNLD
     RAYEFAERCN EPAVWSQLAK AQLQKGMVKE AIDSYIKADD PSSYMEVVQA ANASGNWEEL
     VKYLQMARKK ARESYVETEL IFALAKTNRL AELEEFINGP NNAHIQQVGD RCYDEKMYEA
     AKLLYNNVSN FGRLASTLVH LGEYQAAVDG ARKANSTRTW KEVCFACVDG KEFRLAQMCG
     LHIVVHADEL EELINYYQDR GYFEELITML EAALGLERAH MGMFTELAIL YSKFKPQKMR
     EHLELFWSRV NIPKVLRAAE QAHLWAELVF LYDKYEEYDN AIITMMNHPT DAWKEGQFKD
     IITKVANVEL YYKAVQFYLE FKPLLLNDLL MVLSPRLDHT RAVTFFTKVK QLPLVKPYLR
     SVQNHNNKSV NESLNNLFII EEDYQALRTS IDAYDNFDNI SLAQRLEKHE LIEFRRIAAY
     LFKGNNRWKQ SVELCKKDRL YKDAMQYASE SKDTELAEEL LQWFLQENKR ECFGACLFTC
     YDLLRPDVVL ETAWRHNIMD FAMPYFIQVM KEYLTKVDKL DASESLRKEE EQATETQPIV
     YGQPQLMLTA GPSVAVPPQA PFGYGYTAPP YGQPQPGFGY SM
//
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