ID A0A0R4IMX2_DANRE Unreviewed; 1248 AA. AC A0A0R4IMX2; A0A8M1NZ87; DT 20-JAN-2016, integrated into UniProtKB/TrEMBL. DT 20-JAN-2016, sequence version 1. DT 28-JUN-2023, entry version 41. DE SubName: Full=Protein transport protein Sec24C {ECO:0000313|RefSeq:NP_001232897.3}; DE SubName: Full=SEC24 homolog C, COPII coat complex component {ECO:0000313|Ensembl:ENSDARP00000135644}; GN Name=im:7145364 {ECO:0000313|RefSeq:NP_001232897.3}; GN Synonyms=wu:fd10d12 {ECO:0000313|RefSeq:NP_001232897.3}; GN OrderedLocusNames=sec24c {ECO:0000313|Ensembl:ENSDARP00000135644, GN ECO:0000313|RefSeq:NP_001232897.3, GN ECO:0000313|ZFIN:ZDB-GENE-030131-4487}; OS Danio rerio (Zebrafish) (Brachydanio rerio). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes; OC Danionidae; Danioninae; Danio. OX NCBI_TaxID=7955 {ECO:0000313|Ensembl:ENSDARP00000135644}; RN [1] {ECO:0000313|RefSeq:NP_001232897.3} RP NUCLEOTIDE SEQUENCE. RC STRAIN=Tuebingen {ECO:0000313|RefSeq:NP_001232897.3}; RX PubMed=20442775; RA Sarmah S., Barrallo-Gimeno A., Melville D.B., Topczewski J., RA Solnica-Krezel L., Knapik E.W.; RT "Sec24D-dependent transport of extracellular matrix proteins is required RT for zebrafish skeletal morphogenesis."; RL PLoS ONE 5:E10367-E10367(2010). RN [2] {ECO:0000313|RefSeq:NP_001232897.3} RP NUCLEOTIDE SEQUENCE. RC STRAIN=Tuebingen {ECO:0000313|RefSeq:NP_001232897.3}; RX PubMed=21729877; RA Melville D.B., Montero-Balaguer M., Levic D.S., Bradley K., Smith J.R., RA Hatzopoulos A.K., Knapik E.W.; RT "The feelgood mutation in zebrafish dysregulates COPII-dependent secretion RT of select extracellular matrix proteins in skeletal morphogenesis."; RL Dis. Model. Mech. 4:763-776(2011). RN [3] {ECO:0000313|Ensembl:ENSDARP00000135644} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Tuebingen {ECO:0000313|Ensembl:ENSDARP00000135644}; RX PubMed=23594743; DOI=10.1038/nature12111; RA Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C., Muffato M., RA Collins J.E., Humphray S., McLaren K., Matthews L., McLaren S., Sealy I., RA Caccamo M., Churcher C., Scott C., Barrett J.C., Koch R., Rauch G.J., RA White S., Chow W., Kilian B., Quintais L.T., Guerra-Assuncao J.A., Zhou Y., RA Gu Y., Yen J., Vogel J.H., Eyre T., Redmond S., Banerjee R., Chi J., Fu B., RA Langley E., Maguire S.F., Laird G.K., Lloyd D., Kenyon E., Donaldson S., RA Sehra H., Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M., RA Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J., RA Clee C., Oliver K., Clark R., Riddle C., Elliot D., Threadgold G., RA Harden G., Ware D., Begum S., Mortimore B., Kerry G., Heath P., RA Phillimore B., Tracey A., Corby N., Dunn M., Johnson C., Wood J., Clark S., RA Pelan S., Griffiths G., Smith M., Glithero R., Howden P., Barker N., RA Lloyd C., Stevens C., Harley J., Holt K., Panagiotidis G., Lovell J., RA Beasley H., Henderson C., Gordon D., Auger K., Wright D., Collins J., RA Raisen C., Dyer L., Leung K., Robertson L., Ambridge K., Leongamornlert D., RA McGuire S., Gilderthorp R., Griffiths C., Manthravadi D., Nichol S., RA Barker G., Whitehead S., Kay M., Brown J., Murnane C., Gray E., RA Humphries M., Sycamore N., Barker D., Saunders D., Wallis J., Babbage A., RA Hammond S., Mashreghi-Mohammadi M., Barr L., Martin S., Wray P., RA Ellington A., Matthews N., Ellwood M., Woodmansey R., Clark G., Cooper J., RA Tromans A., Grafham D., Skuce C., Pandian R., Andrews R., Harrison E., RA Kimberley A., Garnett J., Fosker N., Hall R., Garner P., Kelly D., Bird C., RA Palmer S., Gehring I., Berger A., Dooley C.M., Ersan-Urun Z., Eser C., RA Geiger H., Geisler M., Karotki L., Kirn A., Konantz J., Konantz M., RA Oberlander M., Rudolph-Geiger S., Teucke M., Lanz C., Raddatz G., RA Osoegawa K., Zhu B., Rapp A., Widaa S., Langford C., Yang F., RA Schuster S.C., Carter N.P., Harrow J., Ning Z., Herrero J., Searle S.M., RA Enright A., Geisler R., Plasterk R.H., Lee C., Westerfield M., RA de Jong P.J., Zon L.I., Postlethwait J.H., Nusslein-Volhard C., RA Hubbard T.J., Roest Crollius H., Rogers J., Stemple D.L.; RT "The zebrafish reference genome sequence and its relationship to the human RT genome."; RL Nature 496:498-503(2013). RN [4] {ECO:0000313|RefSeq:NP_001232897.3} RP NUCLEOTIDE SEQUENCE. RC STRAIN=Tuebingen {ECO:0000313|RefSeq:NP_001232897.3}; RX PubMed=24627348; RA Le Corre S., Eyre D., Drummond I.A.; RT "Modulation of the secretory pathway rescues zebrafish polycystic kidney RT disease pathology."; RL J. Am. Soc. Nephrol. 25:1749-1759(2014). RN [5] {ECO:0000313|Ensembl:ENSDARP00000135644} RP IDENTIFICATION. RC STRAIN=Tuebingen {ECO:0000313|Ensembl:ENSDARP00000135644}; RG Ensembl; RL Submitted (NOV-2015) to UniProtKB. RN [6] {ECO:0000313|RefSeq:NP_001232897.3} RP IDENTIFICATION. RC STRAIN=Tuebingen {ECO:0000313|RefSeq:NP_001232897.3}; RG RefSeq; RL Submitted (MAR-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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; CU469520; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CU694198; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR RefSeq; NP_001232897.3; NM_001245968.3. DR AlphaFoldDB; A0A0R4IMX2; -. DR STRING; 7955.ENSDARP00000127272; -. DR Ensembl; ENSDART00000162175.2; ENSDARP00000135644.1; ENSDARG00000103516.2. DR GeneID; 571870; -. DR KEGG; dre:571870; -. DR CTD; 9632; -. DR ZFIN; ZDB-GENE-030131-4487; sec24c. DR OrthoDB; 977017at2759; -. DR Proteomes; UP000000437; Chromosome 12. DR Bgee; ENSDARG00000103516; Expressed in early embryo and 27 other tissues. DR ExpressionAtlas; A0A0R4IMX2; 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:0070971; C:endoplasmic reticulum exit site; IBA:GO_Central. DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell. DR GO; GO:0000149; F:SNARE binding; IBA:GO_Central. DR GO; GO:0008270; F:zinc ion binding; IBA:GO_Central. 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; 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 InterPro; IPR036174; Znf_Sec23_Sec24_sf. DR PANTHER; PTHR13803:SF5; PROTEIN TRANSPORT PROTEIN SEC24C; 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 Cytoplasmic vesicle {ECO:0000256|ARBA:ARBA00023329}; KW Protein transport {ECO:0000256|ARBA:ARBA00022927}; KW Proteomics identification {ECO:0007829|PeptideAtlas:A0A0R4IMX2}; KW Reference proteome {ECO:0000313|Proteomes:UP000000437}; KW Transport {ECO:0000256|ARBA:ARBA00022448}. FT DOMAIN 576..614 FT /note="Zinc finger Sec23/Sec24-type" FT /evidence="ECO:0000259|Pfam:PF04810" FT DOMAIN 653..897 FT /note="Sec23/Sec24 trunk" FT /evidence="ECO:0000259|Pfam:PF04811" FT DOMAIN 902..985 FT /note="Sec23/Sec24 beta-sandwich" FT /evidence="ECO:0000259|Pfam:PF08033" FT DOMAIN 998..1098 FT /note="Sec23/Sec24 helical" FT /evidence="ECO:0000259|Pfam:PF04815" FT DOMAIN 1118..1188 FT /note="Gelsolin-like" FT /evidence="ECO:0000259|Pfam:PF00626" FT REGION 1..484 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 83..101 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 114..135 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 141..162 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 186..227 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 228..260 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 261..288 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 297..355 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 383..401 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 403..428 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 455..476 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" SQ SEQUENCE 1248 AA; 134951 MW; 994A54D3BFB96EBC CRC64; MNVNQQPHMA SPYGQPQPGY QRYPQPGYQR YPQPGYQRYP QPGYGGGHVP SGYPAQYAPD NGPGSGYQQG PPQGMREPPT SGTPPVSGAQ SYSQFGQGET QNGPPPMVAP PQGTLVSQPH TPNAVSLSGP TQPPYGQQFG SPPIGMQQMT NQMASMQVGS TAPSPAGPGY APPSTAQAPI SAAYTPSAPP TFPPTSSAPS QPPPTEAVAQ PPPLPYYGAP PPAQQPFPNA VSTFSSAGPT QPQAPPSVSQ QSFPQAPAVS QPPFSTAPPP GPSQSYGGPL PPTQPSFQRA PLPTSQPGVF PGGPPPTSTH SQLPGPMPPQ PPVSQPSPYY SEPPPTTASF PPQVGAPPRP PLAGMQGPPM ASQGPLMASH GPPGASQEPP LQLQGPPMGS QGPTMAQVNH VPPSQPGMPP GPINASLSGP PPQPGMQGYP PQQNGAFGQV RGPQPGYAAP PYSGQPNYGA PPAAPAPAPA APKRLDPDSI PSPIQVIEDD KANKGSQPFT TGVRGQAPPL VTTRFQVKDQ GNASPRYIRC TAYNMPCNSD MAKQSQVPLA AVIKPLATLP PDESPPYLVD HGESGPIRCN RCKAYMCPFM QFIEGGRRFQ CGFCSCVTEV PPHYFQHLDH TGKRVDCYER PELSMGSYEF MATVDYCKNN KFPQPPAFIF LIDVSYNAVK NGMVGMVCQE LKTLMDYLPR ENPDVESNVR VGFVTYNKVL HFYNVKASLA QPQMLVVSDV ADMFVPLLDG FLVNVSESRV VIESLLDQIP EMFADTRETE TVFGPVIQAG LEALKAADCA GKLFIFHSSL PIAEAPGKLK NREDKKLVGT DKEKSLFQPQ VSFYNTLAKD CVAQGCCVDL FLFPNQYVDV ATLGVVPTST GGSIYKYTYF QASSDQERFL NDLRRDVQKQ MGFDAVMRVR TSTGIRATDF FGSFYMSNTT DVELAGLDCD KTVTVEFRHD DKLSEETGAL MQCAVLYTSC SGQRRLRVHN MAVNCCSQLA DLYRNCETDT IINFFVKYAY RSVLSSPTKN VRDSLVNQCA QILACYRKNC ASPSSAGQLI LPECMKLLPV YLNCVLKSDV LQPGADVSLD DRAYLRQLVS AMDVAESHVF FYPRLLPLQK LDAESTSLPL AVRDSEERLS RGGVYLLENG LNIFIWVGVN AQQELLQNIF GTPAFSQIDP SMTSLPALDN PFSKRLKEII ESIRAQRSRY MKLMVVKQED KLELIFKHFL VEDKSNNGGA SYVDFLCHMH KEIRQLLS //