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Database: UniProt
Entry: A0A0K0EQM8_STRER
LinkDB: A0A0K0EQM8_STRER
Original site: A0A0K0EQM8_STRER 
ID   A0A0K0EQM8_STRER        Unreviewed;       814 AA.
AC   A0A0K0EQM8;
DT   14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT   14-OCT-2015, sequence version 1.
DT   24-JAN-2024, entry version 32.
DE   RecName: Full=Protein transport protein SEC23 {ECO:0000256|RuleBase:RU365030};
OS   Strongyloides stercoralis (Threadworm).
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Tylenchina; Panagrolaimomorpha; Strongyloidoidea; Strongyloididae;
OC   Strongyloides.
OX   NCBI_TaxID=6248 {ECO:0000313|Proteomes:UP000035681, ECO:0000313|WBParaSite:SSTP_0001175800.1};
RN   [1] {ECO:0000313|Proteomes:UP000035681}
RP   NUCLEOTIDE SEQUENCE.
RA   Martin A.A.;
RL   Submitted (JUL-2014) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|WBParaSite:SSTP_0001175800.1}
RP   IDENTIFICATION.
RG   WormBaseParasite;
RL   Submitted (AUG-2015) 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; A0A0K0EQM8; -.
DR   STRING; 6248.A0A0K0EQM8; -.
DR   WBParaSite; SSTP_0001175800.1; SSTP_0001175800.1; SSTP_0001175800.
DR   Proteomes; UP000035681; 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: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; 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; 2.
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   Reference proteome {ECO:0000313|Proteomes:UP000035681};
KW   Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|RuleBase:RU365030};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU365030}.
FT   DOMAIN          62..102
FT                   /note="Zinc finger Sec23/Sec24-type"
FT                   /evidence="ECO:0000259|Pfam:PF04810"
FT   DOMAIN          132..441
FT                   /note="Sec23/Sec24 trunk"
FT                   /evidence="ECO:0000259|Pfam:PF04811"
FT   DOMAIN          452..555
FT                   /note="Sec23/Sec24 beta-sandwich"
FT                   /evidence="ECO:0000259|Pfam:PF08033"
FT   DOMAIN          569..667
FT                   /note="Sec23/Sec24 helical"
FT                   /evidence="ECO:0000259|Pfam:PF04815"
FT   DOMAIN          684..770
FT                   /note="Gelsolin-like"
FT                   /evidence="ECO:0000259|Pfam:PF00626"
FT   REGION          211..269
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        246..269
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   814 AA;  91043 MW;  07C5B35941E5BE6C CRC64;
     MASWDDYLHS QQSNDGIQMT WNVWPHSRVD AQKLVVPITT FFTPLKEKPL DSPQQPPLKY
     DPVLCMKSTC KAVLNPLCVV DYRAKIWQCV ICQQRNPFPP HYAMIAENNR PPELYPQFTT
     IEYTLAKATT LSPIFLYMVD LCMGQDEFDA LKEAIQTSLS LLPADAFVGL ITFGRMVELH
     ELNVNHMSRS FVFKGTKEVT TKQIKDVLGL SIGSQPGQRS GPTPAGVPGA PGGGFPMAPG
     QQRPNFAPMG QMNGLPTQQI QQQQQQPIHQ SGSAIPYNKF LQPISECENS INNLIDQLQP
     DRWPVAQGRR PQRATGAAFS VAVTLLENCF PNTGARIMTF VGGACTHGPG MVVGEELKNP
     IRSWHTIKED NATYMRKATK FYDSLAHRTV KNGHVIDIYS CALDQTGLAE MKALYHSTNG
     NVVMADSFKS TLFSQTFQRS FEKDANGHLK MAFNATMEVK VGNGLKIEGV LGCCSSGNIR
     NASVSDQEIG IGGTCQWKFG ALTPRSTIAV VLDVTAQHGT AIPQGARGIV QFVTQYQHSD
     GFKRIRVTTT CRNWADFNTQ QANIAYGFDQ EAAAVVMARL ASWRASNEND TPDALRWLDR
     SLIRLVQKFG DYHKDDPNSF RLNDKFSLFP QFMFHLRRSQ FLQVFNNSPD ETAFYRHVLF
     SENVIESTTM IQPVLFSYSF NGPPEPVLLD TSSILPDRIL LMDDYFHVLI YHGQTIAAWK
     KANYHEDPQY ASFKQLLEAP ISDATAILQE RFPMPRYIVT EYEGSQARFL LSKVNPSLTH
     NNSYSQEGGA PVFTDDVSLQ VFMEHLKKLA VTPS
//
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