ID A0A091DPG1_FUKDA Unreviewed; 1750 AA.
AC A0A091DPG1;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE RecName: Full=Clathrin heavy chain {ECO:0000256|PIRNR:PIRNR002290};
GN ORFNames=H920_06414 {ECO:0000313|EMBL:KFO32165.1};
OS Fukomys damarensis (Damaraland mole rat) (Cryptomys damarensis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Hystricomorpha; Bathyergidae;
OC Fukomys.
OX NCBI_TaxID=885580 {ECO:0000313|EMBL:KFO32165.1, ECO:0000313|Proteomes:UP000028990};
RN [1] {ECO:0000313|EMBL:KFO32165.1, ECO:0000313|Proteomes:UP000028990}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC TISSUE=Liver {ECO:0000313|EMBL:KFO32165.1};
RA Gladyshev V.N., Fang X.;
RT "The Damaraland mole rat (Fukomys damarensis) genome and evolution of
RT African mole rats.";
RL Submitted (NOV-2013) 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; KN122207; KFO32165.1; -; Genomic_DNA.
DR STRING; 885580.ENSFDAP00000011129; -.
DR eggNOG; KOG0985; Eukaryota.
DR Proteomes; UP000028990; 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; 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, 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:UP000028990};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT DOMAIN 406..429
FT /note="Clathrin heavy chain linker core motif"
FT /evidence="ECO:0000259|Pfam:PF09268"
SQ SEQUENCE 1750 AA; 199729 MW; E8C14E089FC65A51 CRC64;
MGGVLSPGSF RRLSRFRSLR CARFRHCGSL GPWSLRPRPE LFRLSASFLR PQRSPGSSCP
AAPVTGGDCT PPDSAMAQIL PIRFQEHLQL QNLGINPSNI GFSTLTMESD KFICIREKVG
EQAQVVIIDM NDPSNPIRRP ISADSAIMNP ASKVIALKAG KTLQIFNIEM KSKMKAHTMT
DDVTFWKWIS LNTVALVTDN AVYHWSMEGE SQPVKMFDRH SSLAGCQIIN YRTDAKQKWL
LLTGISAQQN RVVGAMQLYS VDRKVSQPIE GHAASFAQFK MEGNAEESTL FCFAVRGQAG
GKLHIIEVGT PPTGNQPFPK KAVDVFFPPE AQNDFPVAMQ ISEKHDVVFL ITKYGYIHLY
DLETGTCIYM NRISGETIFV TAPHEATAGI IGVNRKGQVL SVCVEEENII PYITNVLQNP
DLALRMAVRN NLAGAEELFA RKFNALFAQG NYSEAAKVAA NAPKGILRTP DTIRRFQSVP
AQPGQTSPLL QYFGILLDQG QLNKYESLEL CRPVLQQGRK QLLEKWLKED KLECSEELGD
LVKSVDPTLA LSVYLRANVP NKVIQCFAET GQVQKIVLYA KKVGYTPDWI FLLRNVMRIS
PDQGQQFAQM LVQDEEPLAD ITQIVDVFME YNLIQQCTAF LLDALKNNRP SEGPLQTRLL
EMNLMHAPQV ADAILGNQMF THYDRAHIAQ LCEKAGLLQR ALEHFTDLYD IKRAVVHTHL
LNPEWLVNYF GSLSVEDSLE CLRAMLSANI RQNLQICVQV ASKYHEQLST QSLIELFESF
KSFEGLFYFL GSIVNFSQDP DVHFKYIQAA CKTGQIKEVE RICRESNCYD PERVKNFLKE
AKLTDQLPLI IVCDRFDFVH DLVLYLYRNN LQKYIEIYVQ KVNPSRLPVV IGGLLDVDCS
EDVIKNLILV VRGQFSTDEL VAEVEKRNRL KLLLPWLEAR IHEGCEEPAT HNALAKIYID
SNNNPERFLR ENPYYDSRVV GKYCEKRDPH LACVAYERGQ CDLELINVCN ENSLFKSLSR
YLVRRKDPEL WGSVLLESNP YRRPLIDQVV QTALSETQDP EEVSVTVKAF MTADLPNELI
ELLEKIVLDN SVFSEHRNLQ NLLILTAIKA DRTRVMEYIN RLDNYDAPDI ANIAISNELF
EEAFAIFRKF DVNTSAVQVL IEHIGNLDRA YEFAERCNEP AVWSQLAKAQ LQKGMVKEAI
DSYIKADDPS SYMEVVQAAN TSGNWEELVK YLQMARKKAR ESYVETELIF ALAKTNRLAE
LEEFINGPNN AHIQQVGDRC YDEKMYDAAK LLYNNVSNFG RLASTLVHLG EYQAAVDGAR
KANSTRTWKE VCFACVDGKE FRLAQMCGLH IVVHADELEE LINYYQDRGY FEELITMLEA
ALGLERAHMG MFTELAILYS KFKPQKMREH LELFWSRVNI PKVLRAAEQA HLWAELVFLY
DKYEEYDNAI ITMMNHPTDA WKEGQFKDII TKVANVELYY RAIQFYLEFK PLLLNDLLMV
LSPRLDHTRA VNYFSKVKQL PLVKPYLRSV QNHNNKSVNE SLNNLFITEE DYQALRTSID
AYDNFDNISL AQRLEKHELI EFRRIAAYLF KGNNRWKQSV ELCKKDSLYK DAMQYASESK
DTELAEELLQ WFLQEEKREC FGACLFTCYD LLRPDVVLET AWRHNIMDFA MPYFIQVMKE
YLTKVDKLDA SESLRKEEEQ ATETQPIVYG QPQLMLTAGP SVAVPPQAPF GYGYTAPPYG
QPQPGFGYSM
//
