SC23B_BOVIN
ID SC23B_BOVIN Reviewed; 767 AA.
AC Q3SZN2;
DT 11-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2005, sequence version 1.
DT 03-AUG-2022, entry version 103.
DE RecName: Full=Protein transport protein Sec23B {ECO:0000305};
DE AltName: Full=SEC23-related protein B;
GN Name=SEC23B {ECO:0000250|UniProtKB:Q15437};
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Crossbred X Angus; TISSUE=Ileum;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (AUG-2005) 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 for their transport to the Golgi complex.
CC {ECO:0000250|UniProtKB:Q15436}.
CC -!- SUBUNIT: COPII is composed of at least five proteins: the Sec23/24
CC complex, the Sec13/31 complex and Sar1 (By similarity). Interacts with
CC SAR1A (By similarity). {ECO:0000250|UniProtKB:Q15436,
CC ECO:0000250|UniProtKB:Q15437}.
CC -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle, COPII-coated vesicle
CC membrane {ECO:0000250|UniProtKB:Q15436}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:Q15436}; Cytoplasmic side
CC {ECO:0000250|UniProtKB:Q15436}. Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:Q15437}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:Q15436}; Cytoplasmic side
CC {ECO:0000250|UniProtKB:Q15436}. Cytoplasm, cytosol
CC {ECO:0000250|UniProtKB:Q15436}.
CC -!- SIMILARITY: Belongs to the SEC23/SEC24 family. SEC23 subfamily.
CC {ECO:0000305}.
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DR EMBL; BC102775; AAI02776.1; -; mRNA.
DR RefSeq; NP_001029798.1; NM_001034626.2.
DR RefSeq; XP_005214413.1; XM_005214356.3.
DR RefSeq; XP_005214414.1; XM_005214357.3.
DR RefSeq; XP_005214415.1; XM_005214358.3.
DR RefSeq; XP_005214417.1; XM_005214360.3.
DR RefSeq; XP_005214418.1; XM_005214361.3.
DR RefSeq; XP_005214419.1; XM_005214362.3.
DR RefSeq; XP_005214420.1; XM_005214363.3.
DR RefSeq; XP_015329520.1; XM_015474034.1.
DR AlphaFoldDB; Q3SZN2; -.
DR SMR; Q3SZN2; -.
DR STRING; 9913.ENSBTAP00000024348; -.
DR PaxDb; Q3SZN2; -.
DR PeptideAtlas; Q3SZN2; -.
DR PRIDE; Q3SZN2; -.
DR Ensembl; ENSBTAT00000070497; ENSBTAP00000067465; ENSBTAG00000018295.
DR Ensembl; ENSBTAT00000075453; ENSBTAP00000065606; ENSBTAG00000018295.
DR Ensembl; ENSBTAT00000080168; ENSBTAP00000071054; ENSBTAG00000018295.
DR GeneID; 535071; -.
DR KEGG; bta:535071; -.
DR CTD; 10483; -.
DR VEuPathDB; HostDB:ENSBTAG00000018295; -.
DR VGNC; VGNC:34411; SEC23B.
DR eggNOG; KOG1986; Eukaryota.
DR GeneTree; ENSGT00390000006916; -.
DR HOGENOM; CLU_008658_3_0_1; -.
DR InParanoid; Q3SZN2; -.
DR OMA; PWNIIPV; -.
DR OrthoDB; 270617at2759; -.
DR TreeFam; TF300693; -.
DR Proteomes; UP000009136; Chromosome 13.
DR Bgee; ENSBTAG00000018295; Expressed in saliva-secreting gland and 107 other tissues.
DR ExpressionAtlas; Q3SZN2; baseline.
DR GO; GO:0030127; C:COPII vesicle coat; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR GO; GO:0005783; C:endoplasmic reticulum; ISS:UniProtKB.
DR GO; GO:0070971; C:endoplasmic reticulum exit site; IBA:GO_Central.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005096; F:GTPase activator activity; IBA:GO_Central.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0090110; P:COPII-coated vesicle cargo loading; IBA:GO_Central.
DR GO; GO:0006886; P:intracellular protein transport; IEA:InterPro.
DR CDD; cd11287; Sec23_C; 1.
DR Gene3D; 3.40.20.10; -; 1.
DR Gene3D; 3.40.50.410; -; 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; PTHR11141; 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; SSF53300; SSF53300; 1.
DR SUPFAM; SSF81811; SSF81811; 1.
DR SUPFAM; SSF82754; SSF82754; 1.
DR SUPFAM; SSF82919; SSF82919; 1.
PE 2: Evidence at transcript level;
KW Acetylation; Cytoplasm; Cytoplasmic vesicle; Endoplasmic reticulum;
KW ER-Golgi transport; Membrane; Metal-binding; Protein transport;
KW Reference proteome; Transport; Zinc.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q15437"
FT CHAIN 2..767
FT /note="Protein transport protein Sec23B"
FT /id="PRO_0000245344"
FT REPEAT 634..720
FT /note="Gelsolin-like"
FT /evidence="ECO:0000255"
FT BINDING 61
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q15436"
FT BINDING 66
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q15436"
FT BINDING 85
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q15436"
FT BINDING 88
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q15436"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:Q15437"
FT MOD_RES 564
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9D662"
SQ SEQUENCE 767 AA; 86462 MW; 0436D64B2F8840F3 CRC64;
MATYLEFIQQ NEERDGVRFS WNVWPSSRLE ATRMVVPLAC LLTPLKERPD LPPVQYEPVL
CSRPTCKAIL NPLCQVDYRA KLWACNFCFQ RNQFPPAYAG ISEVNQPAEL MPQFSTIEYV
IQRGAPSPLI FLYVVDTCLE DDDLQALKES LQMSLSLLPP DALVGLITFG RMVQVHELSC
EGISKSYVFR GTKDLTAKQI QDMLGLTKPA MPVQPMRPAQ PQERPSVSSR FLQPIHKIDM
NLTDLLGELQ RDPWPVPQGK RPLRSTGVAL SIAVGLLEGT FPNTGARIML FTGGPPTQGP
GMVVGDELKV PIRSWHDIEK DNARFMKKAT KHYEMLANRT AANGHCIDIY ACALDQTGLL
EMKCCPNLTG GYMVMGDSFN TSLFKQTFQR IFSKDFNGNF RMAFGATLEV KTSRELKVAG
AIGPCVSLNV KGPCVSENEL GVGGTSQWKI CGLDPTTTLG IYFEVVNQHN APIPQGGRGA
IQFVTHYQHS STQRRIRVTT VARNWADVQS QLKHIEAAFD QEAAAVLMAR LGVFRAETEE
GPDVLRWLDR QLIRLCQKFG QYNKEDPMSF RLSDSFSLYP QFMFHLRRSP FLQVFNNSPD
ESSYYRHHFA RQDLTQSLIM IQPILYSYSF HGPPEPVLLD SSSILADRIL LMDTFFQIVI
YLGETIAQWR KAGYQDMPEY ENFKHLLQAP LDDAQEILQA RFPMPRYIHT EHGGSQARFL
LSKVNPSQTH NNLYAWGQET GAPILTDDVS LQVFMDHLKK LAVSSAC
