SC23B_MOUSE
ID SC23B_MOUSE Reviewed; 767 AA.
AC Q9D662; A2ANA1; Q3U6B3; Q99K49; Q9QZ68;
DT 31-JAN-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 152.
DE RecName: Full=Protein transport protein Sec23B {ECO:0000305};
DE AltName: Full=SEC23-related protein B;
GN Name=Sec23b {ECO:0000312|MGI:MGI:1350925};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Low D.Y.H., Tang B.L., Hong W.J.;
RL Submitted (OCT-1999) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Bone marrow, Mammary gland, and Skin;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Mammary tumor;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [6]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-564, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y.,
RA Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic
RT pathways.";
RL Mol. Cell 50:919-930(2013).
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; AK014597; BAB29452.1; -; mRNA.
DR EMBL; AK149693; BAE29030.1; -; mRNA.
DR EMBL; AK153214; BAE31812.1; -; mRNA.
DR EMBL; AK166330; BAE38710.1; -; mRNA.
DR EMBL; AF200326; AAF08301.1; -; mRNA.
DR EMBL; AL808119; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC005464; AAH05464.1; -; mRNA.
DR EMBL; BC011160; AAH11160.1; -; mRNA.
DR CCDS; CCDS16822.1; -.
DR RefSeq; NP_001239472.1; NM_001252543.1.
DR RefSeq; NP_001239473.1; NM_001252544.1.
DR RefSeq; NP_001239474.1; NM_001252545.1.
DR RefSeq; NP_062761.2; NM_019787.4.
DR RefSeq; XP_017174388.1; XM_017318899.1.
DR AlphaFoldDB; Q9D662; -.
DR SMR; Q9D662; -.
DR BioGRID; 205109; 10.
DR STRING; 10090.ENSMUSP00000028916; -.
DR iPTMnet; Q9D662; -.
DR PhosphoSitePlus; Q9D662; -.
DR SwissPalm; Q9D662; -.
DR EPD; Q9D662; -.
DR jPOST; Q9D662; -.
DR MaxQB; Q9D662; -.
DR PaxDb; Q9D662; -.
DR PRIDE; Q9D662; -.
DR ProteomicsDB; 255465; -.
DR Antibodypedia; 1407; 197 antibodies from 23 providers.
DR DNASU; 27054; -.
DR Ensembl; ENSMUST00000028916; ENSMUSP00000028916; ENSMUSG00000027429.
DR GeneID; 27054; -.
DR KEGG; mmu:27054; -.
DR UCSC; uc008mrj.2; mouse.
DR CTD; 10483; -.
DR MGI; MGI:1350925; Sec23b.
DR VEuPathDB; HostDB:ENSMUSG00000027429; -.
DR eggNOG; KOG1986; Eukaryota.
DR GeneTree; ENSGT00390000006916; -.
DR HOGENOM; CLU_008658_3_0_1; -.
DR InParanoid; Q9D662; -.
DR OMA; PWNIIPV; -.
DR OrthoDB; 270617at2759; -.
DR PhylomeDB; Q9D662; -.
DR TreeFam; TF300693; -.
DR BioGRID-ORCS; 27054; 11 hits in 75 CRISPR screens.
DR ChiTaRS; Sec23b; mouse.
DR PRO; PR:Q9D662; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; Q9D662; protein.
DR Bgee; ENSMUSG00000027429; Expressed in submandibular gland and 249 other tissues.
DR ExpressionAtlas; Q9D662; baseline and differential.
DR Genevisible; Q9D662; MM.
DR GO; GO:0030127; C:COPII vesicle coat; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR GO; GO:0012505; C:endomembrane system; ISO:MGI.
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:0048471; C:perinuclear region of cytoplasm; IDA:MGI.
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 1: Evidence at protein 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_0000205149"
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:0007744|PubMed:23806337"
FT CONFLICT 314
FT /note="S -> W (in Ref. 1; AAF08301)"
FT /evidence="ECO:0000305"
FT CONFLICT 382..383
FT /note="SL -> CV (in Ref. 1; AAF08301)"
FT /evidence="ECO:0000305"
FT CONFLICT 536
FT /note="A -> T (in Ref. 4; AAH05464)"
FT /evidence="ECO:0000305"
FT CONFLICT 702
FT /note="F -> L (in Ref. 1; AAF08301)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 767 AA; 86437 MW; 1CB8EAA252A93A97 CRC64;
MATYLEFIQQ NEERDGVRFS WNVWPSSRLE ATRMVVPLAC LLTPLKERPD LPPVQYEPVL
CSRPTCKAIL NPLCQVDYRA KLWACNFCFQ RNQFPPAYAG ISEVNQPAEL MPQFSTIEYM
IQRGARSPLI FLYVVDTCLE EDDLQALKES LQMSLSLLPP DALVGLITFG RMVQVHELSC
EGISKSYVFR GTKDLTAKQI QEMLGLTKSA MPVQQARPAQ PQEQPFVSSR FLQPIHKIDM
NLTDLLGELQ RDPWPVTQGK RPLRSTGVAL SIAVGLLEGT FPNTGARIML FTGGPPTQGP
GMVVGDELKT PIRSWHDIEK DNARFMKKAT KHYEMLANRT ATNGHCIDIY ACALDQTGLL
EMKCCPNLTG GHMVMGDSFN TSLFKQTFQR IFSKDFNGDF RMAFGATLDV KTSRELKIAG
AIGPCVSLNV KGPCVSENEL GVGGTSQWKI CGLDPSSTLG IYFEVVNQHN APVPQGGRGA
IQFVTQYQHS STQKRIRVTT IARNWADAQS QLRHIEAAFD QEAAAVLMAR LGVFRAESEE
GPDVLRWLDR QLIRLCQKFG QYNKEDPTSF RLSDSFSLYP QFMFHLRRSP FLQVFNNSPD
ESSYYRHHFA RQDLTQSLIM IQPILYSYSF HGPPEPVLLD SSSILADRIL LMDTFFQIVI
YLGETIAQWR KAGYQDMPEY ENFKHLLQAP LDDAQEILQA RFPMPRYINT EHGGSQARFL
LSKVNPSQTH NNLYAWGQET GAPILTDDVS LQVFMDHLKK LAVSSAS
