ID A0A5N6KNY3_9ROSI Unreviewed; 1140 AA.
AC A0A5N6KNY3;
DT 26-FEB-2020, integrated into UniProtKB/TrEMBL.
DT 26-FEB-2020, sequence version 1.
DT 27-MAR-2024, entry version 12.
DE RecName: Full=ENTH domain-containing protein {ECO:0000259|PROSITE:PS50942};
GN ORFNames=FH972_021292 {ECO:0000313|EMBL:KAB8336988.1};
OS Carpinus fangiana.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Fagales; Betulaceae; Carpinus.
OX NCBI_TaxID=176857 {ECO:0000313|EMBL:KAB8336988.1, ECO:0000313|Proteomes:UP000327013};
RN [1] {ECO:0000313|EMBL:KAB8336988.1, ECO:0000313|Proteomes:UP000327013}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Cfa_2016G {ECO:0000313|EMBL:KAB8336988.1};
RC TISSUE=Leaf {ECO:0000313|EMBL:KAB8336988.1};
RA Yang X., Wang Z., Zhang L., Hao G., Liu J., Yang Y.;
RT "A chromosomal-level reference genome of Carpinus fangiana (Coryloideae,
RT Betulaceae).";
RL Submitted (JUN-2019) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle, clathrin-coated vesicle
CC {ECO:0000256|ARBA:ARBA00004132}. Vesicle
CC {ECO:0000256|ARBA:ARBA00004373}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00243}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KAB8336988.1}.
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DR EMBL; VIBQ01000009; KAB8336988.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A5N6KNY3; -.
DR Proteomes; UP000327013; Unassembled WGS sequence.
DR GO; GO:0030136; C:clathrin-coated vesicle; IEA:UniProtKB-SubCell.
DR GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0005545; F:1-phosphatidylinositol binding; IEA:InterPro.
DR GO; GO:0030276; F:clathrin binding; IEA:InterPro.
DR GO; GO:0048268; P:clathrin coat assembly; IEA:InterPro.
DR GO; GO:0072583; P:clathrin-dependent endocytosis; IEA:InterPro.
DR CDD; cd16988; ANTH_N_YAP180; 1.
DR Gene3D; 1.25.40.90; -; 1.
DR Gene3D; 1.20.58.150; ANTH domain; 1.
DR Gene3D; 2.120.10.80; Kelch-type beta propeller; 1.
DR InterPro; IPR011417; ANTH_dom.
DR InterPro; IPR014712; ANTH_dom_sf.
DR InterPro; IPR045192; AP180-like.
DR InterPro; IPR013809; ENTH.
DR InterPro; IPR008942; ENTH_VHS.
DR InterPro; IPR011043; Gal_Oxase/kelch_b-propeller.
DR InterPro; IPR015915; Kelch-typ_b-propeller.
DR InterPro; IPR006652; Kelch_1.
DR PANTHER; PTHR22951; CLATHRIN ASSEMBLY PROTEIN; 1.
DR PANTHER; PTHR22951:SF89; PHOSPHATIDYLINOSITOL-BINDING CLATHRIN ASSEMBLY PROTEIN LAP; 1.
DR Pfam; PF07651; ANTH; 1.
DR Pfam; PF01344; Kelch_1; 1.
DR Pfam; PF13854; Kelch_5; 1.
DR SMART; SM00273; ENTH; 1.
DR SUPFAM; SSF48464; ENTH/VHS domain; 1.
DR SUPFAM; SSF50965; Galactose oxidase, central domain; 1.
DR SUPFAM; SSF89009; GAT-like domain; 1.
DR PROSITE; PS50942; ENTH; 1.
PE 4: Predicted;
KW Cytoplasmic vesicle {ECO:0000256|ARBA:ARBA00023329};
KW Golgi apparatus {ECO:0000256|ARBA:ARBA00023034};
KW Membrane {ECO:0000256|PROSITE-ProRule:PRU00243};
KW Reference proteome {ECO:0000313|Proteomes:UP000327013};
KW Transmembrane {ECO:0000256|PROSITE-ProRule:PRU00243};
KW Transmembrane helix {ECO:0000256|PROSITE-ProRule:PRU00243}.
FT TRANSMEM 892..915
FT /note="Helical"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00243"
FT DOMAIN 1..126
FT /note="ENTH"
FT /evidence="ECO:0000259|PROSITE:PS50942"
FT REGION 287..350
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 792..813
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 953..1003
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 287..338
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 957..981
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 982..999
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1140 AA; 124072 MW; 7F2CBDED2BED980F CRC64;
MSSSFEKSVK GATKVKLAPP KSKYIEHILQ ATHSGENGVG EVFRTLQFRL RDSTWTIAFK
ALLVVHLMIR DGEPNITLKY LSQQTPSKVL AVNTYTDVQT QGRNIRSYSR YLVERAKAYA
KTRWDYVGAA PGRLKRLPVE KGLLRETESV QDQIQACLRC GDFFADEPEN EISLTAFRTL
TMDLLALFAA MNEGTIAILE HYFEMSKPDA ERALEIYKTF ASQTDKVVRF LQLARQYENV
TRLEIPKIKH APTNLINSLE EYLHDKDFET NRRQYLAQQE GFNPFQQQAG FTGQQNGFAP
QAQFQPQQQT GFAPQQQFAP QPTGLGFGGY TPQEQQPPMP QQQQQPQPNY AAFASGVQQQ
IPQQQLIPQA TGSNPFRQSM MPQPTNQTNS PFGGAPLMRQ SIRIVPVAEA AMVLSKEPFG
TNQPRHHARQ NDPTDYCKKW SQQSALVNGT LYLYGGRAIT DPSQTSDEWS PPAVANGYMW
SSYSSLYLYG GEYSDNPVAT PDPFALWEFK IGPMSWRSLK SPTTSGGTNA AEPNDAVQPA
AEGAGLSVAS LGRGWYFGGH QDGYTTNGWS QSVTRVYLKS LLEFTFPGYI NTAVDALSDG
QAAGSDGAWR NVTGGGVQES SGFPERADGV LVYVPGFGDQ GIVLGLAGGT NNTFTQMNSI
DVYDVANSMW YRQSTSGEVP AMRVNPCAVV AAAPDGSSYN IYMWGGQNLQ PAGEQIQYDD
MWILSVPSFT WISVGNSTPS GVLGRSGHTC NIWDGQMVVV GGYVGNSVSC DSPGVYVYDL
STLAWVNSFT SRSSVHDNPQ NKQESQADDP NALSGSYGYQ VPEAVQSVIG GSGSGGATII
TPVATATAGP IATGAAATYT TTSTSTNAPG SNNSGSANNL SGDLSTSNAG SIAAGVIAGV
AGIAAIYLGF CAWLYRKRLR QHQRWLSYAH QSVVREANRD TGALAYSGRG KEWPGYTSVA
SPQTESQRLT PYGSSSASQE REREVSPGDF ERRGMARTAK SSTEDLIAGQ EPSFMGIMLH
PRRSLRETKI GPSGCFSKLR PRPSRANGTS RLPHMCYINL CCPAVDFLPH TYLVGIRAIK
KALDLSEHPV LHITVVCWYE SPSGASSAQF LLAFTLDAKT ILSLLAWPAG RATKKDRSIT
//
