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   24-JAN-2024, entry version 160.
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,
RC   Pancreas, 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   GlyGen; Q9D662; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; Q9D662; -.
DR   PhosphoSitePlus; Q9D662; -.
DR   SwissPalm; Q9D662; -.
DR   EPD; Q9D662; -.
DR   jPOST; Q9D662; -.
DR   MaxQB; Q9D662; -.
DR   PaxDb; 10090-ENSMUSP00000028916; -.
DR   ProteomicsDB; 255465; -.
DR   Pumba; Q9D662; -.
DR   Antibodypedia; 1407; 236 antibodies from 24 providers.
DR   DNASU; 27054; -.
DR   Ensembl; ENSMUST00000028916.15; ENSMUSP00000028916.9; ENSMUSG00000027429.17.
DR   GeneID; 27054; -.
DR   KEGG; mmu:27054; -.
DR   UCSC; uc008mrj.2; mouse.
DR   AGR; MGI:1350925; -.
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; 5474700at2759; -.
DR   PhylomeDB; Q9D662; -.
DR   TreeFam; TF300693; -.
DR   BioGRID-ORCS; 27054; 11 hits in 80 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 253 other cell types or tissues.
DR   ExpressionAtlas; Q9D662; baseline and differential.
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; 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:SF10; PROTEIN TRANSPORT PROTEIN SEC23B; 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.
DR   Genevisible; Q9D662; MM.
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
//