ID A0A439D501_9PEZI Unreviewed; 1936 AA.
AC A0A439D501;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 24-JAN-2024, entry version 12.
DE RecName: Full=Protein transport protein SEC23 {ECO:0000256|ARBA:ARBA00021212};
DE AltName: Full=Protein transport protein sec23 {ECO:0000256|ARBA:ARBA00013451};
GN ORFNames=EKO27_g5622 {ECO:0000313|EMBL:RWA09485.1};
OS Xylaria grammica.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Xylariomycetidae; Xylariales; Xylariaceae; Xylaria.
OX NCBI_TaxID=363999 {ECO:0000313|EMBL:RWA09485.1, ECO:0000313|Proteomes:UP000286045};
RN [1] {ECO:0000313|EMBL:RWA09485.1, ECO:0000313|Proteomes:UP000286045}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IHI A82 {ECO:0000313|EMBL:RWA09485.1,
RC ECO:0000313|Proteomes:UP000286045};
RA Buettner E., Kellner H.;
RT "Draft genome sequence of Xylaria grammica IHI A82.";
RL Submitted (DEC-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Component of the coat protein complex II (COPII) which
CC promotes the formation of transport vesicles from the endoplasmic
CC reticulum (ER). The coat has two main functions, the physical
CC deformation of the endoplasmic reticulum membrane into vesicles and the
CC selection of cargo molecules. {ECO:0000256|ARBA:ARBA00025471}.
CC -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle, COPII-coated vesicle
CC membrane {ECO:0000256|ARBA:ARBA00004299}; Peripheral membrane protein
CC {ECO:0000256|ARBA:ARBA00004299}; Cytoplasmic side
CC {ECO:0000256|ARBA:ARBA00004299}. Endoplasmic reticulum membrane
CC {ECO:0000256|ARBA:ARBA00004397}; Peripheral membrane protein
CC {ECO:0000256|ARBA:ARBA00004397}; Cytoplasmic side
CC {ECO:0000256|ARBA:ARBA00004397}. Golgi apparatus membrane
CC {ECO:0000256|ARBA:ARBA00004255}; Peripheral membrane protein
CC {ECO:0000256|ARBA:ARBA00004255}; Cytoplasmic side
CC {ECO:0000256|ARBA:ARBA00004255}. 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 SEC23/SEC24 family. SEC23 subfamily.
CC {ECO:0000256|ARBA:ARBA00009210}.
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:RWA09485.1}.
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DR EMBL; RYZI01000152; RWA09485.1; -; Genomic_DNA.
DR STRING; 363999.A0A439D501; -.
DR Proteomes; UP000286045; Unassembled WGS sequence.
DR GO; GO:0030127; C:COPII vesicle coat; IEA:InterPro.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0090114; P:COPII-coated vesicle budding; IEA:InterPro.
DR GO; GO:0006886; P:intracellular protein transport; IEA:InterPro.
DR CDD; cd01478; Sec23-like; 1.
DR CDD; cd11287; Sec23_C; 1.
DR Gene3D; 2.60.40.1670; beta-sandwich domain of Sec23/24; 1.
DR Gene3D; 1.20.120.730; Sec23/Sec24 helical domain; 1.
DR Gene3D; 3.40.20.10; Severin; 1.
DR Gene3D; 3.40.50.410; von Willebrand factor, type A domain; 1.
DR Gene3D; 2.30.30.380; Zn-finger domain of Sec23/24; 1.
DR InterPro; IPR029006; ADF-H/Gelsolin-like_dom_sf.
DR InterPro; IPR007123; Gelsolin-like_dom.
DR InterPro; IPR036180; Gelsolin-like_dom_sf.
DR InterPro; IPR037364; Sec23.
DR InterPro; IPR006900; Sec23/24_helical_dom.
DR InterPro; IPR036175; Sec23/24_helical_dom_sf.
DR InterPro; IPR006896; Sec23/24_trunk_dom.
DR InterPro; IPR012990; Sec23_24_beta_S.
DR InterPro; IPR037550; Sec23_C.
DR InterPro; IPR036465; vWFA_dom_sf.
DR InterPro; IPR006895; Znf_Sec23_Sec24.
DR InterPro; IPR036174; Znf_Sec23_Sec24_sf.
DR PANTHER; PTHR11141; PROTEIN TRANSPORT PROTEIN SEC23; 1.
DR PANTHER; PTHR11141:SF0; PROTEIN TRANSPORT PROTEIN SEC23; 1.
DR Pfam; PF00626; Gelsolin; 1.
DR Pfam; PF08033; Sec23_BS; 1.
DR Pfam; PF04815; Sec23_helical; 1.
DR Pfam; PF04811; Sec23_trunk; 1.
DR Pfam; PF04810; zf-Sec23_Sec24; 1.
DR SUPFAM; SSF81995; beta-sandwich domain of Sec23/24; 1.
DR SUPFAM; SSF82754; C-terminal, gelsolin-like domain of Sec23/24; 1.
DR SUPFAM; SSF81811; Helical domain of Sec23/24; 1.
DR SUPFAM; SSF53300; vWA-like; 1.
DR SUPFAM; SSF82919; Zn-finger domain of Sec23/24; 1.
PE 3: Inferred from homology;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Cytoplasmic vesicle {ECO:0000256|ARBA:ARBA00023329};
KW Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00022824};
KW ER-Golgi transport {ECO:0000256|ARBA:ARBA00022892};
KW Golgi apparatus {ECO:0000256|ARBA:ARBA00023034};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Protein transport {ECO:0000256|ARBA:ARBA00022927};
KW Reference proteome {ECO:0000313|Proteomes:UP000286045};
KW Transport {ECO:0000256|ARBA:ARBA00022448};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 1222..1261
FT /note="Zinc finger Sec23/Sec24-type"
FT /evidence="ECO:0000259|Pfam:PF04810"
FT DOMAIN 1289..1557
FT /note="Sec23/Sec24 trunk"
FT /evidence="ECO:0000259|Pfam:PF04811"
FT DOMAIN 1568..1672
FT /note="Sec23/Sec24 beta-sandwich"
FT /evidence="ECO:0000259|Pfam:PF08033"
FT DOMAIN 1686..1784
FT /note="Sec23/Sec24 helical"
FT /evidence="ECO:0000259|Pfam:PF04815"
FT DOMAIN 1801..1887
FT /note="Gelsolin-like"
FT /evidence="ECO:0000259|Pfam:PF00626"
FT REGION 111..199
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 250..505
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 512..531
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 544..574
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1007..1095
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1133..1153
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 918..945
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 143..163
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 180..196
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 344..399
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 409..432
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 473..505
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 512..530
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 556..574
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1007..1031
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1038..1054
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1060..1088
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1936 AA; 212668 MW; 0447D92A8276BFB7 CRC64;
MVSQDKTVGG VLVFLGPNLR QINVALEQVD IATLRELATV LRTTGPPPDR PVTHDDCLRL
SGSGEPRRWS LQSLRRSKRM KLQRHYSQSH LPENVIPGTT VEGHRYNAIS TRIPKTNNND
ADGPWFRSQY PVFLPQPQSQ PSSPASRPSA WPERSSSKPV SYSGTEKGAA AGDHRNSPRS
TSRPINRDHS RSRALSNRVS TDRLLRAMLN PVDEGYEQDL GTSLRMLSSQ NNTAVEQAQM
HTLPLMAVDE EETDRSGSEH SKPAAPTHIT LPTKPSRDEM RRQSPAVSPE ARGSPRSPRS
PGRSPRRPAN IHVQASLAVP KEKLAPESPG FPNMLATMTF PHPPKGSRPS SSASTAPSIA
DSPGSRPIVQ PRTSSRRAAT STSVSAASLN ELIMQTRPSS RRTKSDRPTR AGTPANSDTA
MNEASTGSRP PTALSVALGE ADQGLTSHSG SIGPPCEESI APSGGGGEEC QRGSLASQLT
ATTDSSRQST STYNSSCSSS ASELSAQSKL TIIPPKTYGE STQASRPVEP SISEQCADVE
ITESQTTATG KDGVDLTEAG HPDLDEKHEE PEKPSLQLST TLNLNTKANQ QPQSIIERRL
ARKAKVREYK MRDLDASRTD VVDSPILGYF SPNLPPEYDP PTQGASALAN GLRRPSTLSM
ATTISEASNE TVRNTDAKAP ADPHHELPLV EDRCEMEATR KAPPSPGIQL KISAVNATDI
EPIYPPTPHW HTSGITLSPI MVVADVESRP GSPTLRFSTL ARPETSSPRV RLKPLKISPH
SRQKSLSVTI SRNPTTGAIE RSASAPIDHK FNRRSLMTMP TPPMSPEAAH SSKRLSLPPV
QLNLPVTPRD RTAPSRFQEW HYSHTEERKI DSGLRSMTLK ERVRREKLQK EKEITDIVAK
TVGLPQKQTE YNDEPHPLPL EQNNTESLEK RLQRLERNND AWLSAMKPLL EAMARTLDDM
RVDDRSRSLR MSDFVIDMEA EARRVTHSRR GDGENTATAT WQSFSRMEGG GMKTRNRLMS
SSSTPLSPVE QELDNSPILD SGAPTLTSTG LSMPGKKAES GEWSDLDPLI RELGSMPRKS
KEEQEAGDSR GGGVNGLNPL MRDLMSASQL CAEGYLARLA GSVVAIADKG GVEGKDASGD
PAQPPSSDTN TDNRLRPLVL AIMDFEALKE QWSEVEDRDG VRLSWNVFPS SRVEASRLVV
PIGALYTPLK EKPDTPLLQF EPVTCKQPCR SVLNPFCQVD VRARLWICPF CLSRNPLPPH
YKDINTNAIP PELHPSNTTI EYRLSRPAPS PPIFLYVVDT CQEDDSLAAL KESLVMSLSL
LPENALVGLI TFGTMVQVHE IGYTECAKSY VFRGSKEYAA KQVQEMLGLL APSLRPGVPQ
QQPGRPMMPM GPATRFLLPV QQCEFQLTKV LEQLQKDPWP VANDRRSLRC SGVALSVAVG
LLESSFQNAG GRIMMFAGGP ATEGPGMVVG PELREPIRSH HDIDRDNIKY YKKALKFYDN
LAKRTAHNGH IIDIFAGCLD QVGLLEMKGL CNSTGGNMIL TDSFTSSMFK QSFIRVFEKD
ADDNLLMGFN AVLEVLTTKE LKVTGLIGHA VSLNKKSTSV GETECGIGNT CSWKMCGIDP
NASYGIYFEI ASQSGPTQHQ QGQQKGMMQF LTYYQHSSGQ FHLRVTTIAR NLSGPAGDPA
IAQSFDQEAA AVLMSRIAVF KAEVDDGPDV LRWVDRMLIR LCSRFADYRK DDPSSFRLEK
NFTLYPQFMF HLRRSQFLQV FNNSPDETAF YRHVLNHEDV SNSLIMIQPT LDSYTFDQDG
GQPVLLDSTS IQPTHILLLD TFFHILIFHG ETIAEWKKAG YQDQEGYENF ATLLEQPKED
ARDLIGDRFP LPRFIVCDAG GSQARFLLSK LNPSTTHTTG AYGGVGAQTA QTIFTDDVSL
QTFMDHLMKL AVSGTS
//
