ID A0A151XD26_9HYME Unreviewed; 1645 AA.
AC A0A151XD26;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=Clathrin heavy chain {ECO:0000256|PIRNR:PIRNR002290};
GN ORFNames=ALC60_02900 {ECO:0000313|EMBL:KYQ58168.1};
OS Trachymyrmex zeteki.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Formicoidea;
OC Formicidae; Myrmicinae; Trachymyrmex.
OX NCBI_TaxID=64791 {ECO:0000313|EMBL:KYQ58168.1, ECO:0000313|Proteomes:UP000075809};
RN [1] {ECO:0000313|EMBL:KYQ58168.1, ECO:0000313|Proteomes:UP000075809}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tzet28-1 {ECO:0000313|EMBL:KYQ58168.1};
RC TISSUE=Whole body {ECO:0000313|EMBL:KYQ58168.1};
RA Nygaard S., Hu H., Boomsma J., Zhang G.;
RT "Trachymyrmex zeteki WGS genome.";
RL Submitted (SEP-2015) to the EMBL/GenBank/DDBJ databases.
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; KQ982298; KYQ58168.1; -; Genomic_DNA.
DR STRING; 64791.A0A151XD26; -.
DR Proteomes; UP000075809; 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: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; 4.
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:UP000075809};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT DOMAIN 300..323
FT /note="Clathrin heavy chain linker core motif"
FT /evidence="ECO:0000259|Pfam:PF09268"
SQ SEQUENCE 1645 AA; 188442 MW; BFEB563A24DB9C72 CRC64;
MESDKFICVR EKVGDTAQVV IIDMNDSANP IRRPISADSA IMNPASKVIA LKAMKTLQIF
NIEMKSKMKA HTMTEDVVFW KWISLNTLAL VTETAVYHWS MEGDSTPNKM FERHSSLNGC
QIINYRTDPK QTWLLLIGIS AQHNRVVGAM QLYSVERKCS QPIEGHAASF AQFKMEGNGE
PSNLFCFAVR TVQGAKLHII EVGQPPSGNH PFPKKAVDVF FPPEAGNDFP VAMQVSSKYD
VIYLITKYGY IHMYDIESAT CIFMNRISGE TIFVTAPHEA SGGIIGVNRK GQVLSVSVDE
ENIIPYINGV LQNSELALRM AVRNNLSGAE DLFVRKFNML FQNGQYAEAA KVAANAPKGI
LRTPATIQRF QQVPATQGQT SPLLQYFGIL LDQGQLNKYE SLELCRPVLV QGRKQLLEKW
LKEDKLECSE ELGDLVKQAD PTLALSVYLR ANVPNKVIQC FAETGQFQKI VLYAKKVSYT
PDYIFLLRNV MRINPDQGVA FAQMLVQDDE PLADINQIVD IFMEQNMVQQ CTAFLLDALK
NNRPSEGALQ TRLLEMNLMS APQVADAILG NQMFTHYDRA HVAQLCEKAG LLQRALEHYT
DLYDIKRAVV HTHLLSPDWL VGFFGTLSVE DSLECLKAML TANIRQNLQI CIQIATKYHE
QLTTKALIDL FESFKSYEGL FYFLGSIVNF SQDQEVHFKY IQAACKTGQI KEVERICRES
NCYNPERVKN FLKEAKLSDQ LPLIIVCDRF DFVHDLVLYL YRNNLQKYIE IYVQKVNPSR
LPVVVGGLLD VDCSEDIIKN LILVVRGQFS TDELVEEVEK RNRLKLLLPW LESRVHEGCV
EPATHNALAK IYIDSNNNPE RFLKENQFYD SRVVGKYCEK RDPHLACIAY ERGQCDRELI
SVCNENSLFK SEARYLVRRR DPDLWAEVLL ESNPYKRPLI DQVVQTALSE TQDPEDISVT
VKAFMTADLP NELIELLEKI VLDSSVFSDH RNLQNLLILT AIKADRTRVM EYINRLDNYD
APDIANIAIN NELYEEAFAI FKKFDVNTSA IQVLIEQVGN LDRAYEFAER CNEPPVWSQL
ARAQLQQGLV KESIDSFIKA DDPSAYMDVV ETAHRTSHWE DLVRYLQMAR KKARESFIES
ELIYAYARTN RLADLEEFIS GPNHADIQKI GDRCFDDKMY DAAKLLYNNV SNFARLAITL
VHLKEFQGAV DSARKANSTR TWKEVCFACV DSGEFRLAQM CGLHIVVHAD ELEDLINYYQ
DRGHFEELIN LLEAALGLER AHMGMFTELA ILYSKYKPQR MREHLELFWS RVNIPKVLRA
AEQAHLWAEL VFLYDKYEEY DNAVLAMMQH PTEAWREGHF KDVITKVANV ELYYKAIHFY
VEYKPLLLND ILLVLAPRMD HTRSVAYFTR TGHLQLVKPY LRSVQALNNK AINEALNGLL
IDEEDYQGLR TSIDAFDNFD NIALAMQLEK HELIEFRRIA AYLYKGNNRW KQSVELCKKD
RLFRDAMEYA AESRNAEVAE ELLEWFLERG SKDCFAACLF HCYDLLHPDV ILELAWRHRI
LHFAMPYLIQ VAREYITKVD KLEEAESRRI EETDHQEHKP MIMPEPQLML TAGPGMMAPG
YAPQNVYGTP AQVYASTAAY QGYGM
//