ID A0A1E3HTF4_9TREE Unreviewed; 763 AA.
AC A0A1E3HTF4;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 22-FEB-2023, entry version 19.
DE RecName: Full=Protein transport protein SEC23 {ECO:0000256|RuleBase:RU365030};
GN ORFNames=L202_03569 {ECO:0000313|EMBL:ODN79627.1};
OS Cryptococcus amylolentus CBS 6039.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Tremellomycetes;
OC Tremellales; Cryptococcaceae; Cryptococcus.
OX NCBI_TaxID=1295533 {ECO:0000313|EMBL:ODN79627.1, ECO:0000313|Proteomes:UP000094065};
RN [1] {ECO:0000313|EMBL:ODN79627.1, ECO:0000313|Proteomes:UP000094065}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 6039 {ECO:0000313|EMBL:ODN79627.1,
RC ECO:0000313|Proteomes:UP000094065};
RA Cuomo C., Litvintseva A., Heitman J., Chen Y., Sun S., Springer D.,
RA Dromer F., Young S., Zeng Q., Chapman S., Gujja S., Saif S., Birren B.;
RT "Evolution of pathogenesis and genome organization in the Tremellales.";
RL Submitted (JUN-2016) 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: Cytoplasm {ECO:0000256|RuleBase:RU365030}.
CC Cytoplasmic vesicle, COPII-coated vesicle membrane
CC {ECO:0000256|ARBA:ARBA00004299, ECO:0000256|RuleBase:RU365030};
CC Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004299,
CC ECO:0000256|RuleBase:RU365030}; Cytoplasmic side
CC {ECO:0000256|ARBA:ARBA00004299, ECO:0000256|RuleBase:RU365030}.
CC Endoplasmic reticulum membrane {ECO:0000256|ARBA:ARBA00004397,
CC ECO:0000256|RuleBase:RU365030}; Peripheral membrane protein
CC {ECO:0000256|ARBA:ARBA00004397, ECO:0000256|RuleBase:RU365030};
CC Cytoplasmic side {ECO:0000256|ARBA:ARBA00004397,
CC ECO:0000256|RuleBase:RU365030}. Golgi apparatus 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}.
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:ODN79627.1}.
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DR EMBL; AWGJ01000005; ODN79627.1; -; Genomic_DNA.
DR RefSeq; XP_018994474.1; XM_019137448.1.
DR AlphaFoldDB; A0A1E3HTF4; -.
DR STRING; 1295533.A0A1E3HTF4; -.
DR GeneID; 30154878; -.
DR OrthoDB; 5474700at2759; -.
DR Proteomes; UP000094065; 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 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 Golgi apparatus {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:UP000094065};
KW Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|RuleBase:RU365030};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU365030}.
FT DOMAIN 53..93
FT /note="Zinc finger Sec23/Sec24-type"
FT /evidence="ECO:0000259|Pfam:PF04810"
FT DOMAIN 123..385
FT /note="Sec23/Sec24 trunk"
FT /evidence="ECO:0000259|Pfam:PF04811"
FT DOMAIN 397..498
FT /note="Sec23/Sec24 beta-sandwich"
FT /evidence="ECO:0000259|Pfam:PF08033"
FT DOMAIN 512..610
FT /note="Sec23/Sec24 helical"
FT /evidence="ECO:0000259|Pfam:PF04815"
FT DOMAIN 625..712
FT /note="Gelsolin-like"
FT /evidence="ECO:0000259|Pfam:PF00626"
SQ SEQUENCE 763 AA; 85265 MW; CE2C9A36D618196A CRC64;
MSFEDYEDQN GLRLSWNVWP SSRLEATRTV VPISALYTPM KEREEVPPVA YEPVTCKGTS
CKAILNPYCQ VDVRGKMWIC PFCLQRNPFP PQYHHDLSPS NLPTELQPGF TTIEYILSRT
AQVPPIFLYV VDTCLDEDEL KALKETIITS LSLLPPNALV GLITFGTMTM VHELAYPDCP
KAYVFRGSKD YQPKHIADML GLNPSRPMQP MRPGQPIPVN AASKFLMPVQ ACEFQLTNIL
EQLQRDPWPV DQNKRPLRCT GVALSVAVSL LETAFPNTGA RIQLFAGGAA TDGPGLVVGP
ELREPIRSHH DIDRDSVKHF KRATKFYEGL SKRASVNGHA IDIYAGCLDQ VGLLEMKSLT
NATNGFMVIS DSFMTAIFKQ SFLRTLSKDD QGYLKMGFNA TLDITTTKEL KVSGVIGHVI
SANKKSASVG ETEIGIGQTS AWKICSITPK STFAAYFEVV TPTGQNLAPN QSGLIQFVTH
YQHSSGEYRL RVTTCMRHFQ EGGHPTIAAS FDQEAAAVLM ARIAVFKAEI DDSPDVLRWL
DRMLIRLCQK FADYRKEDPT SFQLGPSFSI YPQFMFHLRR SQFLQVFNNS PDETAFYRHI
LNDTDVNNSL IMIQPTLMSY GFDSEPRPVL LDSVSIRPDA ILLLDTFFHI LIFHGETIAQ
WRKANYQEQE DYANFKELLE APVIDAQDLL EDRLPIPRYI VCDQGGSQAR FLLSKLNPST
THMSGASGYG ANPAAGQQIF TDDVSLQVFM EHLKRLAVGA STS
//
