ID   Q80ZX0_MOUSE            Unreviewed;      1251 AA.
AC   Q80ZX0;
DT   01-JUN-2003, integrated into UniProtKB/TrEMBL.
DT   01-JUN-2003, sequence version 1.
DT   02-SEP-2026, entry version 153.
DE   SubName: Full=Sec24 related gene family, member B (S. cerevisiae) {ECO:0000313|EMBL:AAH46776.1};
GN   Name=Sec24b {ECO:0000313|EMBL:AAH46776.1,
GN   ECO:0000313|MGI:MGI:2139764};
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 {ECO:0000313|EMBL:AAH46776.1};
RN   [1] {ECO:0000313|EMBL:AAH46776.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6 {ECO:0000313|EMBL:AAH46776.1};
RC   TISSUE=Brain {ECO:0000313|EMBL:AAH46776.1};
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RA   Gerhard D.S., Wagner L., Feingold E.A., Shenmen C.M., Grouse L.H.,
RA   Schuler G., Klein S.L., Old S., Rasooly R., Good P., Guyer M., Peck A.M.,
RA   Derge J.G., Lipman D., Collins F.S., Jang W., Sherry S., Feolo M.,
RA   Misquitta L., Lee E., Rotmistrovsky K., Greenhut S.F., Schaefer C.F.,
RA   Buetow K., Bonner T.I., Haussler D., Kent J., Kiekhaus M., Furey T.,
RA   Brent M., Prange C., Schreiber K., Shapiro N., Bhat N.K., Hopkins R.F.,
RA   Hsie F., Driscoll T., Soares M.B., Casavant T.L., Scheetz T.E.,
RA   Brown-stein M.J., Usdin T.B., Toshiyuki S., Carninci P., Piao Y.,
RA   Dudekula D.B., Ko M.S., Kawakami K., Suzuki Y., Sugano S., Gruber C.E.,
RA   Smith M.R., Simmons B., Moore T., Waterman R., Johnson S.L., Ruan Y.,
RA   Wei C.L., Mathavan S., Gunaratne P.H., Wu J., Garcia A.M., Hulyk S.W.,
RA   Fuh E., Yuan Y., Sneed A., Kowis C., Hodgson A., Muzny D.M., McPherson J.,
RA   Gibbs R.A., Fahey J., Helton E., Ketteman M., Madan A., Rodrigues S.,
RA   Sanchez A., Whiting M., Madari A., Young A.C., Wetherby K.D., Granite S.J.,
RA   Kwong P.N., Brinkley C.P., Pearson R.L., Bouffard G.G., Blakesly R.W.,
RA   Green E.D., Dickson M.C., Rodriguez A.C., Grimwood J., Schmutz J.,
RA   Myers R.M., Butterfield Y.S., Griffith M., Griffith O.L., Krzywinski M.I.,
RA   Liao N., Morin R., Morrin R., Palmquist D., Petrescu A.S., Skalska U.,
RA   Smailus D.E., Stott J.M., Schnerch A., Schein J.E., Jones S.J., Holt R.A.,
RA   Baross A., Marra M.A., Clifton S., Makowski K.A., Bosak S., Malek J.;
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   [2] {ECO:0007829|PubMed:21183079}
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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   [3] {ECO:0007829|PubMed:23806337}
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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   -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
CC       {ECO:0000256|ARBA:ARBA00004514}. Cytoplasmic vesicle, COPII-coated
CC       vesicle membrane {ECO:0000256|ARBA:ARBA00004299}; Peripheral membrane
CC       protein {ECO:0000256|ARBA:ARBA00004299}; Cytoplasmic side
CC       {ECO:0000256|ARBA:ARBA00004299}. Endoplasmic reticulum membrane
CC       {ECO:0000256|ARBA:ARBA00004397}; Peripheral membrane protein
CC       {ECO:0000256|ARBA:ARBA00004397}; Cytoplasmic side
CC       {ECO:0000256|ARBA:ARBA00004397}.
CC   -!- SIMILARITY: Belongs to the SEC23/SEC24 family. SEC24 subfamily.
CC       {ECO:0000256|ARBA:ARBA00008334}.
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DR   EMBL; BC046776; AAH46776.1; -; mRNA.
DR   RefSeq; NP_997092.1; NM_207209.4.
DR   AlphaFoldDB; Q80ZX0; -.
DR   SMR; Q80ZX0; -.
DR   IntAct; Q80ZX0; 2.
DR   STRING; 10090.ENSMUSP00000001079; -.
DR   GlyGen; Q80ZX0; 4 sites, 1 O-linked glycan (3 sites).
DR   jPOST; Q80ZX0; -.
DR   PaxDb; 10090-ENSMUSP00000001079; -.
DR   PeptideAtlas; Q80ZX0; -.
DR   ProteomicsDB; 332317; -.
DR   Antibodypedia; 48510; 33 antibodies from 12 providers.
DR   GeneID; 99683; -.
DR   UCSC; uc008rit.1; mouse.
DR   AGR; MGI:2139764; -.
DR   CTD; 10427; -.
DR   MGI; MGI:2139764; Sec24b.
DR   VEuPathDB; HostDB:ENSMUSG00000001052; -.
DR   eggNOG; KOG1985; Eukaryota.
DR   GeneTree; ENSGT00950000182924; -.
DR   OMA; QPPPFQM; -.
DR   OrthoDB; 49016at2759; -.
DR   Reactome; R-MMU-204005; COPII-mediated vesicle transport.
DR   Reactome; R-MMU-2132295; MHC class II antigen presentation.
DR   Reactome; R-MMU-5694530; Cargo concentration in the ER.
DR   Reactome; R-MMU-983170; Antigen Presentation: Folding, assembly and peptide loading of class I MHC.
DR   BioGRID-ORCS; 99683; 1 hit in 78 CRISPR screens.
DR   Bgee; ENSMUSG00000001052; Expressed in undifferentiated genital tubercle and 262 other cell types or tissues.
DR   GO; GO:0030127; C:COPII vesicle coat; IDA:MGI.
DR   GO; GO:0030134; C:COPII-coated ER to Golgi transport vesicle; ISO:MGI.
DR   GO; GO:0005829; C:cytosol; ISO:GO_Central.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; ISO:GO_Central.
DR   GO; GO:0000149; F:SNARE binding; IBA:GO_Central.
DR   GO; GO:0008270; F:zinc ion binding; ISO:GO_Central.
DR   GO; GO:0035909; P:aorta morphogenesis; IMP:MGI.
DR   GO; GO:0002093; P:auditory receptor cell morphogenesis; IMP:MGI.
DR   GO; GO:0060088; P:auditory receptor cell stereocilium organization; IMP:MGI.
DR   GO; GO:0072359; P:circulatory system development; IMP:MGI.
DR   GO; GO:0021747; P:cochlear nucleus development; IMP:MGI.
DR   GO; GO:0090110; P:COPII-coated vesicle cargo loading; ISO:GO_Central.
DR   GO; GO:0060982; P:coronary artery morphogenesis; IMP:MGI.
DR   GO; GO:0006888; P:endoplasmic reticulum to Golgi vesicle-mediated transport; ISO:GO_Central.
DR   GO; GO:0006886; P:intracellular protein transport; IEA:InterPro.
DR   GO; GO:0060463; P:lung lobe morphogenesis; IMP:MGI.
DR   GO; GO:0060425; P:lung morphogenesis; IMP:MGI.
DR   GO; GO:0001843; P:neural tube closure; IMP:MGI.
DR   GO; GO:0003151; P:outflow tract morphogenesis; IMP:MGI.
DR   GO; GO:0061156; P:pulmonary artery morphogenesis; IMP:MGI.
DR   GO; GO:1901301; P:regulation of cargo loading into COPII-coated vesicle; IMP:MGI.
DR   GO; GO:0090178; P:regulation of establishment of planar polarity involved in neural tube closure; IMP:MGI.
DR   CDD; cd01479; Sec24-like; 1.
DR   FunFam; 2.30.30.380:FF:000004; SEC24 homolog B, COPII coat complex component; 1.
DR   FunFam; 3.40.50.410:FF:000019; SEC24 homolog B, COPII coat complex component; 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; IPR012990; Beta-sandwich_Sec23_24.
DR   InterPro; IPR007123; Gelsolin-like_dom.
DR   InterPro; IPR036180; Gelsolin-like_dom_sf.
DR   InterPro; IPR006900; Sec23/24_helical_dom.
DR   InterPro; IPR036175; Sec23/24_helical_dom_sf.
DR   InterPro; IPR006896; Sec23/24_trunk_dom.
DR   InterPro; IPR050550; SEC23_SEC24_subfamily.
DR   InterPro; IPR041742; Sec24-like_trunk_dom.
DR   InterPro; IPR036465; vWFA_dom_sf.
DR   InterPro; IPR006895; Znf_Sec23_Sec24.
DR   InterPro; IPR036174; Znf_Sec23_Sec24_sf.
DR   PANTHER; PTHR13803:SF42; PROTEIN TRANSPORT PROTEIN SEC24B; 1.
DR   PANTHER; PTHR13803; SEC24-RELATED PROTEIN; 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   1: Evidence at protein level;
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW   Cytoplasmic vesicle {ECO:0000256|ARBA:ARBA00023329};
KW   Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00022824};
KW   ER-Golgi transport {ECO:0000256|ARBA:ARBA00022892};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Protein transport {ECO:0000256|ARBA:ARBA00022927};
KW   Transport {ECO:0000256|ARBA:ARBA00022448};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT   DOMAIN          585..621
FT                   /note="Zinc finger Sec23/Sec24-type"
FT                   /evidence="ECO:0000259|Pfam:PF04810"
FT   DOMAIN          658..897
FT                   /note="Sec23/Sec24 trunk"
FT                   /evidence="ECO:0000259|Pfam:PF04811"
FT   DOMAIN          902..986
FT                   /note="Sec23/Sec24 beta-sandwich"
FT                   /evidence="ECO:0000259|Pfam:PF08033"
FT   DOMAIN          997..1097
FT                   /note="Sec23/Sec24 helical"
FT                   /evidence="ECO:0000259|Pfam:PF04815"
FT   DOMAIN          1124..1196
FT                   /note="Gelsolin-like"
FT                   /evidence="ECO:0000259|Pfam:PF00626"
FT   REGION          1..165
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          183..419
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..14
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        30..41
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        86..102
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        127..143
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        144..165
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        235..254
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        273..314
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        316..334
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        351..361
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        362..375
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1251 AA;  135551 MW;  4E36C4C0C0F79D25 CRC64;
     MSAPAGSPHP AAGARMPPKL GGAVSGLAPP QQNGPAQSPM QVPSGYGLPH QNYMVPSGHY
     SQGPGKMTSL PLDSQCDSYY SRPYTVPTQN SGTPSSANQP GAQQMYGRGP SAPHMGGSMP
     GSFQGIPASA SHSYSSASQP YSSLGNRYSS PTTYSANASV ASQGYPSTCS HYPISTVSNV
     VYPNVSYPSL PASEPYGQMF TSQSAPPPAR PVKESYSGPS TALTYPSRPP PPPSQHQQQQ
     QQQQQQQQQQ QSHSGYSSLP WSGPALPPAQ DSLIRNQMGS LATANSHPTN NENVQPPKSS
     SVVSTVLPGP SSTRMPPAPS HPVGPVPSAP PPPEQMQTKG MQYGDYGNNQ ASSTATPLSS
     ASDDEEEQEE DEEAGVDSSS TTSSASPLPN SYDALEGGSY PDMHSSSASS PVPDHALEPS
     PTLAQALSAA PTPPAAQPAK VAKPFGYGYP ALQPAYQNAA PPPMPAAHPS GPAYTGYPQH
     YPGVNQLSSG LGGLSLQSSP QPESLRPVNL TQEKNILPPT PIWAPVPNLS AELSKLNCSP
     DSFRCTLTSI PQTQALLNKA KLPLGLLLHP FRDLTQLPVI TSNTIVRCRS CRTYINPFVS
     FIDQRRWKCN LCYRVNDVPE EFLYNPLTRS YGEPHKRPEV QNSTVEFIAS SDYMLRPPQP
     AVYLFVLDVS HNAVEAGYLT VLCQSLLENL DKLPGDSRTR IGFMTFDSTI HFYNLQEGLS
     QPQMLIVSDI DDVFLPTPDS LLVNLYESKE LIKDLLNALP SMFINTRETH SALGPALQAA
     FKLMSPTGGR VSVFQTQLPS LGAGLLQSRE DPNQRSSTKV VHHLGPATDF YKKLALDCSG
     QQTAVDLFLL SSQYSDLASL ACMSKYSAGC IFYYPSFHST HNPSQAEKLQ KDLKRYLTRK
     IGFEAVMRIR CTKGLSMHTF HGNFFVRSTD LLSLANINPD AGFAVQLSIE ESLTDTALVC
     FQTALLYTSS KGERRIRVHT LCLPVVSSLA DVYAGVDVQA AVCLLANMAV DRSVSSSLSD
     ARDALVNAVV DPLSAYSSAV ASVPRSTLTA PSSLKLLPLY VLALLKQKAF RTGTSTRLDD
     RVYAMCQMKS QPLVHLMKMI HPNLYRIDRL TDEGAIHVND RVVPQPPLQK LSAEKLTREG
     AFLMDCGSVF YIWVGKGCDS NFIENVLGYP DFASIPQKMT HLPELDTLPS ERTRSFVTWL
     RDSRPLSPVL HLVKDESPAK TDFFQHLLED RTEAALSYYE FLIHIQQQVC K
//