ID A0A183QI64_9TREM Unreviewed; 781 AA.
AC A0A183QI64;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE RecName: Full=Protein transport protein SEC23 {ECO:0000256|RuleBase:RU365030};
OS Schistosoma rodhaini.
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Platyhelminthes; Trematoda;
OC Digenea; Strigeidida; Schistosomatoidea; Schistosomatidae; Schistosoma.
OX NCBI_TaxID=6188 {ECO:0000313|WBParaSite:SROB_0000333401-mRNA-1};
RN [1] {ECO:0000313|WBParaSite:SROB_0000333401-mRNA-1}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (JUN-2016) to UniProtKB.
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|RuleBase:RU365030}.
CC -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle, COPII-coated vesicle
CC membrane {ECO:0000256|RuleBase:RU365030}; Peripheral membrane protein
CC {ECO:0000256|RuleBase:RU365030}; Cytoplasmic side
CC {ECO:0000256|RuleBase:RU365030}. Endoplasmic reticulum membrane
CC {ECO:0000256|RuleBase:RU365030}; Peripheral membrane protein
CC {ECO:0000256|RuleBase:RU365030}; Cytoplasmic side
CC {ECO:0000256|RuleBase:RU365030}. 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, ECO:0000256|RuleBase:RU365030}.
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DR AlphaFoldDB; A0A183QI64; -.
DR STRING; 6188.A0A183QI64; -.
DR WBParaSite; SROB_0000333401-mRNA-1; SROB_0000333401-mRNA-1; SROB_0000333401.
DR GO; GO:0030127; C:COPII vesicle coat; IEA:InterPro.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006888; P:endoplasmic reticulum to Golgi vesicle-mediated transport; IEA:InterPro.
DR GO; GO:0006886; P:intracellular protein transport; IEA:InterPro.
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; 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 Cytoplasm {ECO:0000256|RuleBase:RU365030};
KW Cytoplasmic vesicle {ECO:0000256|ARBA:ARBA00023329,
KW ECO:0000256|RuleBase:RU365030};
KW Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00022824,
KW ECO:0000256|RuleBase:RU365030};
KW ER-Golgi transport {ECO:0000256|ARBA:ARBA00022892,
KW ECO:0000256|RuleBase:RU365030};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU365030};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|RuleBase:RU365030};
KW Protein transport {ECO:0000256|ARBA:ARBA00022927,
KW ECO:0000256|RuleBase:RU365030};
KW Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|RuleBase:RU365030};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU365030}.
FT DOMAIN 58..96
FT /note="Zinc finger Sec23/Sec24-type"
FT /evidence="ECO:0000259|Pfam:PF04810"
FT DOMAIN 126..407
FT /note="Sec23/Sec24 trunk"
FT /evidence="ECO:0000259|Pfam:PF04811"
FT DOMAIN 421..519
FT /note="Sec23/Sec24 beta-sandwich"
FT /evidence="ECO:0000259|Pfam:PF08033"
FT DOMAIN 534..632
FT /note="Sec23/Sec24 helical"
FT /evidence="ECO:0000259|Pfam:PF04815"
FT DOMAIN 649..734
FT /note="Gelsolin-like"
FT /evidence="ECO:0000259|Pfam:PF00626"
SQ SEQUENCE 781 AA; 88391 MW; 30E9477716769FEB CRC64;
MATMAEFIQQ SEINDGIRFS WNAWPISRLE SAQCVVPIGC LYTLFKERYD FPPINYDPVF
CSRCRGILNP YCPFDIRTRT WTCCLCNTRN SFPPQYAGMT EQKLPAELMA QFTTLEYTIP
KVQLVPPIFM FVIDTCIEEP EFTHLKESIQ LSLSFLPPHA FVGLITFGKM VHVHELEAGP
ISKSWVFKGT KDYTGNQIQV RIFTNANQPA SVFNANSPPG APKGVYSAEK QFQQPQMAQL
PYNRLFIQPM ERCDALITDL LTELQPDPWP VPQGKRPLRS VGTALSIAVG LLEAAYPNTG
ARVMLFLGGP CTQGPGMVVD DDLKNIIRSH HDMEKDNCKY MRRAMKHYEG LANRAAQNLH
VVDIFSCSLD QTGLHELRYL TNYTGGHMIM GDSFASNLFQ QTYRRVFNKD ASGSFLMGLA
GQMEVKVKLK VSGCIGPCFS ANVKTPNTGE QEVGIGRTSV WRLNGFTPST TLAIYFEVAT
SAIQMPPGSN GRGYVQFVTQ YQRANGQRKL RVTTVCRNWI DSTTQLPHMI CGFDQEAATV
LIARMAMFKA ETTDSVDVLR WLDRQLIKLC HKFGDYRKDD PTSFRLPGEF SFYPQFMFHM
RRSQFLQVFN NSPDETAYYR HVLNKEDCSN SLLMIQPSLT SFNLDGSEEP VLLDSSSIQP
ERVLLMDSFF LILIYEGDTI AKWKKAGYLD MPEYAHIKQI LDKPRYEAQE LLKTRFPVSR
YVETEHDGSQ ARFLLSKVNP SLTHHTMYSF GQDSGSAVLT DDVSLQGFME HLKKLAVSSS
A
//
