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Database: UniProt
Entry: A0A452CE68_BALAS
LinkDB: A0A452CE68_BALAS
Original site: A0A452CE68_BALAS 
ID   A0A452CE68_BALAS        Unreviewed;       782 AA.
AC   A0A452CE68;
DT   08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT   08-MAY-2019, sequence version 1.
DT   24-JAN-2024, entry version 17.
DE   RecName: Full=Protein transport protein SEC23 {ECO:0000256|RuleBase:RU365030};
GN   Name=SEC23A {ECO:0000313|RefSeq:XP_028021284.1};
OS   Balaenoptera acutorostrata scammoni (North Pacific minke whale)
OS   (Balaenoptera davidsoni).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Whippomorpha; Cetacea; Mysticeti;
OC   Balaenopteridae; Balaenoptera.
OX   NCBI_TaxID=310752 {ECO:0000313|Proteomes:UP000261681, ECO:0000313|RefSeq:XP_028021284.1};
RN   [1] {ECO:0000313|RefSeq:XP_028021284.1}
RP   IDENTIFICATION.
RC   TISSUE=Muscle {ECO:0000313|RefSeq:XP_028021284.1};
RG   RefSeq;
RL   Submitted (JAN-2023) 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|ARBA:ARBA00004397, ECO:0000256|RuleBase:RU365030};
CC       Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004397,
CC       ECO:0000256|RuleBase:RU365030}; Cytoplasmic side
CC       {ECO:0000256|ARBA:ARBA00004397, ECO:0000256|RuleBase:RU365030}.
CC       Cytoplasm, cytosol {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|RuleBase:RU365030}.
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DR   RefSeq; XP_028021284.1; XM_028165483.1.
DR   STRING; 310752.A0A452CE68; -.
DR   InParanoid; A0A452CE68; -.
DR   OrthoDB; 5474700at2759; -.
DR   Proteomes; UP000261681; Unplaced.
DR   GO; GO:0030127; C:COPII vesicle coat; IEA:InterPro.
DR   GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
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; 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:SF7; PROTEIN TRANSPORT PROTEIN SEC23A; 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   Reference proteome {ECO:0000313|Proteomes:UP000261681};
KW   Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|RuleBase:RU365030};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU365030}.
FT   DOMAIN          58..98
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          418..521
FT                   /note="Sec23/Sec24 beta-sandwich"
FT                   /evidence="ECO:0000259|Pfam:PF08033"
FT   DOMAIN          535..633
FT                   /note="Sec23/Sec24 helical"
FT                   /evidence="ECO:0000259|Pfam:PF04815"
FT   DOMAIN          649..735
FT                   /note="Gelsolin-like"
FT                   /evidence="ECO:0000259|Pfam:PF00626"
SQ   SEQUENCE   782 AA;  88046 MW;  541873E34DE72644 CRC64;
     MTTYLEFIQQ NEERDGVRFS WNVWPSSRLE ATRMVVPVAA LFTPLKERPD LPPIQYEPVL
     CSRTTCRAVL NPLCQVDYRA KLWACNFCYQ RNQFPPTYAG ISELNQPXXL LPQFSSIEYV
     VLRGPQMPLI FLYVVDTCME DEDLQALKES MQMSLSLLPP TALVGLITFG RMVQVHELGC
     EGISKSYVFR GTKDLSAKQL QEMLGLSKVP VTQATRGPQV QQPPPSNRFL QPVQKIDMNL
     TDLLGELQRD PWPVPQGXXX XXXXXXXXXX XXXGKRPLRS SGVALSIAVG LLECTFPNTG
     ARIMMFIGGP ATQGPGMVVG DELKTPIRSW HDIEKDNAKY VKKGTKHFEA LANRAATTGH
     VIDIYACALD QTGLLEMKCC PNLTGGYMVM GDSFNTSLFK QTFQRVFTKD MHGQFKMGFG
     GTLEIKTSRE IKISGAIGPC VSLNSKGPCV SENEIGTGGT CQWKICGLSP TTTLAIYFEV
     VNQHNAPIPQ GGRGAIQFVT QYQHSSGQRR IRVTTIARNW ADAQTQIQNI AASFDQEAAA
     ILMARLAIYR AETEEGPDVL RWLDRQLIRL CQKFGEYHKD DPSSFRFSET FSLYPQFMFH
     LRRSPFLQVF NNSPDESSYY RHHFMRQDLT QSLIMIQPIL YAYSFSGPPE PVLLDSSSIL
     ADRILLMDTF FQILIYHGET IAQWRKSGYQ DMPEYENFRH LLQAPVDDAQ EILHSRFPMP
     RYIDTEHGGS QARFLLSKVN PSQTHNNMYA WGQESGAPIL TDDVSLQVFM DHLKKLAVSS
     AA
//
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