ID A0A0D2VIM4_CAPO3 Unreviewed; 882 AA.
AC A0A0D2VIM4;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 24-JAN-2024, entry version 35.
DE RecName: Full=Protein transport protein SEC23 {ECO:0000256|RuleBase:RU365030};
GN ORFNames=CAOG_008493 {ECO:0000313|EMBL:KJE89842.1};
OS Capsaspora owczarzaki (strain ATCC 30864).
OC Eukaryota; Filasterea; Capsaspora.
OX NCBI_TaxID=595528 {ECO:0000313|EMBL:KJE89842.1, ECO:0000313|Proteomes:UP000008743};
RN [1] {ECO:0000313|Proteomes:UP000008743}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=ATCC 30864 {ECO:0000313|Proteomes:UP000008743};
RA Russ C., Cuomo C., Burger G., Gray M.W., Holland P.W.H., King N.,
RA Lang F.B.F., Roger A.J., Ruiz-Trillo I., Young S.K., Zeng Q., Gargeya S.,
RA Alvarado L., Berlin A., Chapman S.B., Chen Z., Freedman E., Gellesch M.,
RA Goldberg J., Griggs A., Gujja S., Heilman E., Heiman D., Howarth C.,
RA Mehta T., Neiman D., Pearson M., Roberts A., Saif S., Shea T., Shenoy N.,
RA Sisk P., Stolte C., Sykes S., White J., Yandava C., Haas B., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Capsaspora owczarzaki ATCC 30864.";
RL Submitted (FEB-2011) 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|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}.
CC -!- SIMILARITY: Belongs to the SEC23/SEC24 family. SEC23 subfamily.
CC {ECO:0000256|RuleBase:RU365030}.
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DR EMBL; KE346361; KJE89842.1; -; Genomic_DNA.
DR RefSeq; XP_011270075.1; XM_011271773.1.
DR AlphaFoldDB; A0A0D2VIM4; -.
DR STRING; 595528.A0A0D2VIM4; -.
DR EnsemblProtists; KJE89842; KJE89842; CAOG_008493.
DR GeneID; 23301890; -.
DR eggNOG; KOG1986; Eukaryota.
DR InParanoid; A0A0D2VIM4; -.
DR OrthoDB; 463590at2759; -.
DR PhylomeDB; A0A0D2VIM4; -.
DR Proteomes; UP000008743; 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: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; 3.40.50.410; von Willebrand factor, type A domain; 1.
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; IPR036174; Znf_Sec23_Sec24_sf.
DR PANTHER; PTHR11141; PROTEIN TRANSPORT PROTEIN SEC23; 1.
DR PANTHER; PTHR11141:SF6; PROTEIN TRANSPORT PROTEIN SEC23; 1.
DR Pfam; PF08033; Sec23_BS; 1.
DR Pfam; PF04815; Sec23_helical; 1.
DR Pfam; PF04811; Sec23_trunk; 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|RuleBase:RU365030};
KW Endoplasmic reticulum {ECO:0000256|RuleBase:RU365030};
KW ER-Golgi transport {ECO:0000256|RuleBase:RU365030};
KW Membrane {ECO:0000256|RuleBase:RU365030};
KW Metal-binding {ECO:0000256|RuleBase:RU365030};
KW Protein transport {ECO:0000256|RuleBase:RU365030};
KW Reference proteome {ECO:0000313|Proteomes:UP000008743};
KW Transport {ECO:0000256|RuleBase:RU365030};
KW Zinc {ECO:0000256|RuleBase:RU365030}.
FT DOMAIN 303..457
FT /note="Sec23/Sec24 trunk"
FT /evidence="ECO:0000259|Pfam:PF04811"
FT DOMAIN 516..602
FT /note="Sec23/Sec24 beta-sandwich"
FT /evidence="ECO:0000259|Pfam:PF08033"
FT DOMAIN 614..712
FT /note="Sec23/Sec24 helical"
FT /evidence="ECO:0000259|Pfam:PF04815"
FT REGION 76..104
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 147..203
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 170..203
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 882 AA; 96214 MW; 08547E6626EAE880 CRC64;
MSVHSAGVTP AMAAVALNTS SVRACTRMVP KTVALAQASG LPFGLHLSTM SGQEMRLVDE
ELLAYKPDPA AVLRSGRQDD ATVQALSPQN ASAAGVAGPG ASRGGSTVLG LPVAESFVGL
TFVVPDSREN TATPVLIPAS RRDASVGEAL ASAAPHGQAE AEPSRRGGAH LLSPQSQSGN
VAQQQQQPSQ TLQQPRVSSP ISGMTSFVTQ RNSLLIPSKA PVVHLPPDSC NACRGYFNRH
CVSLSSGDWK CCLCPHINPP LRRAVRPEEL MHDTIEYNVA QDTPLAMAHP EPVIVLLFDE
NIPQSHVKET IIALKNTLDD MPRSAKVAVV TFSTLVSVYR LTATASSSSD VFPGSTLLSL
DDAAQLSESL DSYIVPLHAN LLAVMRAVYL SNRSTGPTSS PAAAKCCLGS ALAVAETLLK
QWTRRSNTPQ LPRGSQIIVF ASGHPSYGPG AVVEEHEMMD VLVNIVCIGF AYFCIPVLRS
AIQPSGGTLV MHNEVRQEMA ADLRFLLLQP YGRDGRVSYK CSTNSIELTH VIGPASPLRD
TDKMGADDLC FLATVRPHQS LGVLFEVVRD ITDENVFFQF TSQYTNPMGD LVHRVTTLRY
STTTDRAALL DSADTDACVA FIAKQAILAS RDGATPAQIV SQLDYQLGFV LKAHSDFDRF
NHQTKLVLPT AIEDLPSRMY HLRRSPMLAT QMQPADDIEY LRSIFLQSDV VTCRKMIEPL
MFEVSDCGTF TPLSLSTLSL WPDRTILVDY ETHIHVWLGL AVVNKLQAEA IHAGATKLDM
ASHAPMTWCH KYVRRASMTW CHKYVRRASS LRFPHPQFIA MLTPAHNDTI ALNLIDAPDL
ARLSVEQLQS HLERFPKSDE WSLRNYLRFI QTLDMKHRPA PL
//
