ID A0A0B2PB16_GLYSO Unreviewed; 1691 AA.
AC A0A0B2PB16;
DT 04-MAR-2015, integrated into UniProtKB/TrEMBL.
DT 04-MAR-2015, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE RecName: Full=Clathrin heavy chain {ECO:0000256|PIRNR:PIRNR002290};
GN ORFNames=glysoja_031872 {ECO:0000313|EMBL:KHN04772.1};
OS Glycine soja (Wild soybean).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC NPAAA clade; indigoferoid/millettioid clade; Phaseoleae; Glycine;
OC Glycine subgen. Soja.
OX NCBI_TaxID=3848 {ECO:0000313|EMBL:KHN04772.1};
RN [1] {ECO:0000313|EMBL:KHN04772.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC TISSUE=Root {ECO:0000313|EMBL:KHN04772.1};
RA Lam H.-M., Qi X., Li M.-W., Liu X., Xie M., Ni M., Xu X.;
RT "Identification of a novel salt tolerance gene in wild soybean by whole-
RT genome sequencing.";
RL Submitted (JUL-2014) 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; KN668935; KHN04772.1; -; Genomic_DNA.
DR Proteomes; UP000053555; 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:SF40; 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 Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT DOMAIN 335..358
FT /note="Clathrin heavy chain linker core motif"
FT /evidence="ECO:0000259|Pfam:PF09268"
FT COILED 1608..1642
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 1691 AA; 192199 MW; 42BE538727F28348 CRC64;
MRETLTLPTI GINPQFITFT HVTMESDKYI CVRETAPQNS VVIIDMNMPN QPLRRPITAD
SALMNPNSRI LALKAQLQGT TQDHLQIFNI EMKAKMKSYQ MPEQVVFWKW ITPKLLGIVT
QTSVYHWSIE GDSEPVKMFE RTANLANNQI INYRCDPSEK WLVLIGIVPG SPERPQLVKG
NMQLFSVEQQ RSQALEAHAA SFAQFKVPGN ENPSTLISFA TKTLNAGQII SKLHVIELGA
QPGKPSFSKK QADLFFPPDF ADDFPVAMQI SHKYSLIYVI TKLGLLFVYD LETATAVYRN
RISPDPIFLT SEATSVGGFY AINRRGQVLL ATVNEQTIVN FVSGQLNNLE LAVNLAKRGN
LPGAEKLVVE RFHELFAQTK YKEAAELAAE SPQGILRTPD TVAKFQSVPV QAGQTPPLLQ
YFGTLLTRGK LNAFESLELS RLVVNQNKKN LLENWLAEDK LECSEELGDL VKTVDNDLAL
KIYIKARATP KVVAAFAERR EFDKILIYSK QVGYTPDYLF LLQTILRTDP QGAVNFALMM
SQMEGGCPVD YNTITDLFLQ RNLIREATAF LLDVLKPNLP EHGYLQTKVL EINLVTFPNV
ADAILANGMF SHYDRPRIAQ LCEKAGLYVR SLQHYTELPD IKRVIVNTHA IEPQSLVEFF
GTLSREWALE CMKDLLLVNL RGNLQIIVQV AKEYCEQLGV DACIKLFEQF RSYEGLYFFL
GSYLSSSEDP DIHFKYIEAA AKTGQIKEVE RVTRESSFYD PEKTKNFLME AKLPDARPLI
NVCDRFGFVP DLTHYLYTSN MLRYIEGYVQ KVNPGNAPLV VGQLLDDECP EDFIKGLILS
VRSLLPVEPL VEECEKRNRL RLLTQFLEHL VSEGSQDVHV HNALGKIIID SNNNPEHFLT
TNPYYDSRVV GKYCEKRDPT LAVVAYRRGQ CDDELINVTN KNSLFKLQAR YVVERMDGDL
WEKVLNPDNT YRRQLIDQVV STALPESKSP EQVSAAVKAF MTADLPHELI ELLEKIVLQN
SAFSGNFNLQ NLLILTAIKA DPSRVMDYIN RLDNFDGPAV GEMAVEAQLY EEAFAIFKKF
NLNVQAVNVL LDNIHSIDRA VEFAFRVEED AVWSQVAKAQ LREGLVSDAI ESFIRADDAT
QFLDVIRAAE DGNVYHDLVR YLLMVRQKTK EPKVDSELIY AYAKIDRLSD IEEFILMPNV
ANLQNVGDQL YDEELYEAAK IIFAFISNWA KLAVTLVKLK QFQGAVDAAR KANSAKTWKE
VCFACVDAEE FRLAQICGLN IIIQVDDLEE VSEYYQNRGC FNELISLMES GLGLERAHMG
IFTELGVLYA RYRYEKLMEH IKLFATRLNI PKLIRACDEQ QHWKELTYLY IQYDEFDNAA
TTIMNHSPEA WDHMQFKDVV VKVANVELYY KAVHFYLQEH PDLINDVLNV LALRVDHARV
VDIMRKAGHL RLVKPYMVAV QSNNVSAVNE ALNEIYVEEE DYDRLRESID LHDNFDQIGL
AQKIEKHELL EMRRVAAYIY KKAGRWKQSI ALSKKDNLYK DAMETASQSG DRELAEELLV
YFIDQGKKEC FASCLFVCYD LIRADIALEL AWMNNMIDFA FPYLLQFIRE YTGKVDELVK
DKIEAQNQVK AKEQEEKEVI AQQNMYAQLL PLALPAPPMP GMGGGFAPPP PMGGLGMPPM
PPFGMPPMGS Y
//
