GenomeNet

Database: UniProt
Entry: Q6NXL1_MOUSE
LinkDB: Q6NXL1_MOUSE
Original site: Q6NXL1_MOUSE 
ID   Q6NXL1_MOUSE            Unreviewed;      1032 AA.
AC   Q6NXL1;
DT   05-JUL-2004, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2004, sequence version 1.
DT   27-MAR-2024, entry version 141.
DE   SubName: Full=Sec24 related gene family, member D (S. cerevisiae) {ECO:0000313|EMBL:AAH67020.1, ECO:0000313|Ensembl:ENSMUSP00000035823.8};
GN   Name=Sec24d {ECO:0000313|EMBL:AAH67020.1,
GN   ECO:0000313|Ensembl:ENSMUSP00000035823.8,
GN   ECO:0000313|MGI:MGI:1916858};
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:AAH67020.1};
RN   [1] {ECO:0000313|EMBL:AAH67020.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6 {ECO:0000313|EMBL:AAH67020.1};
RC   TISSUE=Brain {ECO:0000313|EMBL:AAH67020.1};
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:0000313|Ensembl:ENSMUSP00000035823.8, ECO:0000313|Proteomes:UP000000589}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J {ECO:0000313|Ensembl:ENSMUSP00000035823.8,
RC   ECO:0000313|Proteomes:UP000000589};
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   [3] {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   [4] {ECO:0000313|Ensembl:ENSMUSP00000035823.8}
RP   IDENTIFICATION.
RC   STRAIN=C57BL/6J {ECO:0000313|Ensembl:ENSMUSP00000035823.8};
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
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}. 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. SEC24 subfamily.
CC       {ECO:0000256|ARBA:ARBA00008334}.
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DR   EMBL; BC067020; AAH67020.1; -; mRNA.
DR   RefSeq; NP_081411.2; NM_027135.2.
DR   RefSeq; XP_006502101.1; XM_006502038.3.
DR   STRING; 10090.ENSMUSP00000035823; -.
DR   PaxDb; 10090-ENSMUSP00000035823; -.
DR   ProteomicsDB; 339185; -.
DR   Antibodypedia; 26618; 128 antibodies from 25 providers.
DR   DNASU; 69608; -.
DR   Ensembl; ENSMUST00000047923.12; ENSMUSP00000035823.8; ENSMUSG00000039234.12.
DR   GeneID; 69608; -.
DR   KEGG; mmu:69608; -.
DR   UCSC; uc008rfh.1; mouse.
DR   AGR; MGI:1916858; -.
DR   CTD; 9871; -.
DR   MGI; MGI:1916858; Sec24d.
DR   VEuPathDB; HostDB:ENSMUSG00000039234; -.
DR   eggNOG; KOG1984; Eukaryota.
DR   GeneTree; ENSGT00950000182924; -.
DR   HOGENOM; CLU_004589_1_1_1; -.
DR   OMA; QNGAHAS; -.
DR   OrthoDB; 977017at2759; -.
DR   TreeFam; TF300464; -.
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; 69608; 2 hits in 77 CRISPR screens.
DR   ChiTaRS; Sec24d; mouse.
DR   Proteomes; UP000000589; Chromosome 3.
DR   Bgee; ENSMUSG00000039234; Expressed in humerus cartilage element and 214 other cell types or tissues.
DR   GO; GO:0030127; C:COPII vesicle coat; ISO:MGI.
DR   GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
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:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
DR   GO; GO:0000149; F:SNARE binding; ISO:MGI.
DR   GO; GO:0008270; F:zinc ion binding; ISO:MGI.
DR   GO; GO:0090110; P:COPII-coated vesicle cargo loading; ISO:MGI.
DR   GO; GO:0006888; P:endoplasmic reticulum to Golgi vesicle-mediated transport; ISO:MGI.
DR   GO; GO:0001701; P:in utero embryonic development; IMP:MGI.
DR   GO; GO:0006886; P:intracellular protein transport; IEA:InterPro.
DR   CDD; cd01479; Sec24-like; 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; 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; IPR041742; Sec24-like_trunk_dom.
DR   InterPro; IPR036465; vWFA_dom_sf.
DR   InterPro; IPR006895; Znf_Sec23_Sec24.
DR   PANTHER; PTHR13803:SF6; PROTEIN TRANSPORT PROTEIN SEC24D; 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; 2.
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.
PE   1: Evidence at protein level;
KW   Cytoplasmic vesicle {ECO:0000256|ARBA:ARBA00023329};
KW   Protein transport {ECO:0000256|ARBA:ARBA00022927};
KW   Proteomics identification {ECO:0007829|EPD:Q6NXL1,
KW   ECO:0007829|MaxQB:Q6NXL1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000589};
KW   Transport {ECO:0000256|ARBA:ARBA00022448}.
FT   DOMAIN          360..398
FT                   /note="Zinc finger Sec23/Sec24-type"
FT                   /evidence="ECO:0000259|Pfam:PF04810"
FT   DOMAIN          437..680
FT                   /note="Sec23/Sec24 trunk"
FT                   /evidence="ECO:0000259|Pfam:PF04811"
FT   DOMAIN          686..770
FT                   /note="Sec23/Sec24 beta-sandwich"
FT                   /evidence="ECO:0000259|Pfam:PF08033"
FT   DOMAIN          782..881
FT                   /note="Sec23/Sec24 helical"
FT                   /evidence="ECO:0000259|Pfam:PF04815"
FT   DOMAIN          902..974
FT                   /note="Gelsolin-like"
FT                   /evidence="ECO:0000259|Pfam:PF00626"
FT   REGION          1..263
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..20
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        50..90
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        92..145
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        157..180
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        200..216
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        217..231
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1032 AA;  112676 MW;  35334F5F589325B0 CRC64;
     MSQQGYVATP PYSQSQPGMG ISPPHYGHYG DPSHASSPPG VMKPLGPSAA PSGMLPPGPL
     PPGPPQFGPN GAHTPGHPPQ RFPGPPPVNS VAPSYASGQT LPQSSYPGPG STSSVTQLGS
     QFSSMQINSY GVGATPQSQG PPGPQSAGAF QGPPQPAQPS ILQPGHQVPP PPPTALNGPG
     ASPMSPPTHR QDGLPGPAPL NAQYQPPPPP GQTLGPGYPP QQATNYGPQM GGAQMSYPGG
     FPGGPAQMAG PAPQLQRKLD PDSIPSPIQV IENDRATRGG QVYTTNTRGQ VPPLVTTECV
     IQDQGHSSPR YIRCTTYCFP CTSDMAKQAQ IPLAAVIKPF ADIPPNETPL YLVNHGESGP
     VRCNRCKAYM CPFMQFIEGG RRYQCGFCSC VNEVPPFYFQ HLDHIGRRLD HYEKPELSLG
     SYEYVATLDY CRKNKPPSPP AFIFMIDVSY SNIKNGLVKL ICEELKTALK RLPKEEHEET
     SAIRVGFITY NKVLHFFNVK SNLAQPQMMV VTDVGEVFVP LLDGFLVNYE ESQSVIHNLL
     DQIPEMFADS NENETVFAPV IQAGMEALKA AECPGKLFIF HSSLPTAEAP GKLKNRDDKK
     LVNTDKEKIL FQPQTAVYES LAKDCVANSC SVTLFLFPSQ FVDVASLGLV PLLTGGTLYK
     YNVFQIHSDS QRFLTDLRND IEKKIGFDAI MRVRTSTGFR ATDFFGGIFM NNTTDVEMAA
     IDCDKAVTVE FKHDDKLSED VGALIQCAVL YTTISGQRRL RIHNLALNCS TQLADLYKSC
     ETDALINFFA KSAFKAVLNQ PLKAIREILV NQTAHMLACY RKHCASPSAA SQLILPDSMK
     VLPVYMNSLL KNCVLLSRSE ISPDERAYQR QLVMTMGVAD SQLFFYPLLL PIHTLDVKSA
     ALPPAVRCSE SRLSEEGIFL LANGLNMFLW FGVGSPPELI QGIFNVPSFA HINTDMTSLP
     EVGSPHSQQL RMIMNNIQQK KPYSMKLIVV KQREQREMAF RQFLVEDKGL YGGSSYVDFL
     CCVHKEICQL LN
//
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