ID A0A168NBT5_ABSGL Unreviewed; 1683 AA.
AC A0A168NBT5;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE RecName: Full=Clathrin heavy chain {ECO:0000256|PIRNR:PIRNR002290};
GN Name=ABSGL_05906.1 scaffold 7570 {ECO:0000313|EMBL:SAM00229.1};
OS Absidia glauca (Pin mould).
OC Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Mucoromycotina;
OC Mucoromycetes; Mucorales; Cunninghamellaceae; Absidia.
OX NCBI_TaxID=4829 {ECO:0000313|EMBL:SAM00229.1};
RN [1] {ECO:0000313|EMBL:SAM00229.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 101.48 {ECO:0000313|EMBL:SAM00229.1};
RA Evans L.H., Alamgir A., Owens N., Weber N.D., Virtaneva K., Barbian K.,
RA Babar A., Rosenke K.;
RL Submitted (APR-2016) 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; LT553165; SAM00229.1; -; Genomic_DNA.
DR STRING; 4829.A0A168NBT5; -.
DR InParanoid; A0A168NBT5; -.
DR OMA; HTRVMDY; -.
DR OrthoDB; 5474327at2759; -.
DR Proteomes; UP000078561; 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; 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:UP000078561};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT DOMAIN 361..384
FT /note="Clathrin heavy chain linker core motif"
FT /evidence="ECO:0000259|Pfam:PF09268"
FT REGION 1651..1671
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1683 AA; 192092 MW; FD92E4D4A7245CDD CRC64;
MAVKCVVSII ILDPSTNPFH ASRFRDPSNT MEQPLPIQFH EHAQLQSLGV NAASIAFNTL
TMESDRFICV RENINGANQV VIIDLHNNNE LLRRPISADS VIMHPTTKVM ALKAARTLQV
FNLELKSKLK SHTMNEDVVF WKWINLKTLG LVTNTAVYHW SIEGDSGPQK VFDRHANLND
TQIINYRVSQ DDKWMVLIGI SGHNGRVVGA MQLYSKERGV SQPIEGHSAS FAELKLDGAQ
SPTKLFAFAV RSATGAAKLQ IIEVDHQEGN PVFQKKAVEV FFPPDAANDF PVSMQVSKKY
GIIYLVTKMG YIHLYDLESG ACIYMNRISA DTIFVTADRD ETGGIIGVNK KGQVLSVSVD
ENVIIPYILN TLNNTQLALA LASRGGLPGA DDLYVGRFNE LFNTGNYNEA AKIAANSPRG
ILRTTQTIDR FRQITGTPNQ LSPILQYFGI LLEKGSLNKY ESLELAKPIL LQNRKPLLEK
WLKEDKLECS EELGDFVKQH DSVLALSVFL RANVPNKVVL CFAENKQYDK ILAYAKTVGF
TPDYSSLLYN IARTDADKAA DFATALVNDE NGPLIEPEKV VDVFQSQNMI QQATSFLLDY
LKNNREQDAG LQTRVLEMNL IHAPQVADAI LGTGMLTHYD RVLVGTLCEK AGLYQRALEH
FTDIHDIKRI IPQTHLLAAE WLVDYFGTLS VDQTLECLKE MLNGNLRQNL QVVVQVAIKY
SEQLQPHNLI EMFESYKSNE GLYYYLGSIV NVSQDPLVHF KYIQAACRTG NIREAERICR
ESSYYDAEKV KNFLKEAKLT DQLPLIIVCD RFNFVHDLVL YLYHNNLQSF IEVYVQKVNP
ARTPEVIGGL LDVGCDEDVI KNLLLSVKGD LSVGKLCEEV EERNRLKLLL PWLNLRVTEG
SQDPDVYNSL AKIYIDTNNN PEPFLKENEY YNPRIVGKYC EKRDPYLAFI CYQKGQCDYE
LVQVTNENSM FKHQARYLVR RRDQELWAFV LQENNEHRRD VIDQIVASAL PECTDPDDVS
AAVKAFMGAE LPNELIELLE KIVLENSAFN DNKTLQNLLI FTAVKADSTR VMDYISRLDN
YDASDVAEVC IGEDLFEEAF TIYKNNNVNA NAIDVLIEKI SDLDRAYEFA NRCNQPDVWS
KLARAQLSNM HVKEAIDSYI RADDASNYIE VSRNASIDGK YDDLVRYMQM ARKQSREPFI
ETELLYAYAK TDRLAELEDF ISSPNIAQIQ EVGDRCYHEH LLEAAKILYS SISNHACLAS
TLVLLKNYQA AVDCARKANS TKVWKEVNAE CIRQNEFRLA QICGLHIIVH AEELDTLVKT
YEANGHFNEL IQLLEAGLGL ERAHMGMFTE LAILYAKYAP EKMMEHLRLF VSRVNIPKVI
RACTDAHLWR ELVFLYVHYD EYDNAVTAMM DHASDAWEHS AFKDIIVKVS NMEIYYKSLR
FYLNEHPLLL NDLLAVLVSR INHTRVVQIF EKSDNIPLIK PYLLSVQEVN NKAINSALNE
LFIEEEDYDA LRESVDRYDH FDPIDIAQRL EKHELLEFRR IAAHLYKRNR RWRQSIALSK
QDRLFKDAME TAAESQDREV AEELLQYFIE VGKRECFSAM LYTCYDLMRP DVVMELAWRH
QLTDFAMPYM LNTMKEQFNK VELLNKEVKE LKEKQSSQEQ QEENAPVMPA ITGGAFGNLR
IGM
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