ID B4KFK7_DROMO Unreviewed; 1247 AA.
AC B4KFK7;
DT 23-SEP-2008, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 2.
DT 24-JAN-2024, entry version 80.
DE RecName: Full=Protein transport protein Sec24C {ECO:0008006|Google:ProtNLM};
GN Name=Dmoj\GI18047 {ECO:0000313|EMBL:EDW13122.2};
GN ORFNames=Dmoj_GI18047 {ECO:0000313|EMBL:EDW13122.2};
OS Drosophila mojavensis (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila.
OX NCBI_TaxID=7230 {ECO:0000313|EMBL:EDW13122.2, ECO:0000313|Proteomes:UP000009192};
RN [1] {ECO:0000313|EMBL:EDW13122.2, ECO:0000313|Proteomes:UP000009192}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tucson 15081-1352.22 {ECO:0000313|Proteomes:UP000009192};
RX PubMed=17994087; DOI=10.1038/nature06341;
RG Drosophila 12 genomes consortium;
RA Clark A.G., Eisen M.B., Smith D.R., Bergman C.M., Oliver B., Markow T.A.,
RA Kaufman T.C., Kellis M., Gelbart W., Iyer V.N., Pollard D.A., Sackton T.B.,
RA Larracuente A.M., Singh N.D., Abad J.P., Abt D.N., Adryan B., Aguade M.,
RA Akashi H., Anderson W.W., Aquadro C.F., Ardell D.H., Arguello R.,
RA Artieri C.G., Barbash D.A., Barker D., Barsanti P., Batterham P.,
RA Batzoglou S., Begun D., Bhutkar A., Blanco E., Bosak S.A., Bradley R.K.,
RA Brand A.D., Brent M.R., Brooks A.N., Brown R.H., Butlin R.K., Caggese C.,
RA Calvi B.R., Bernardo de Carvalho A., Caspi A., Castrezana S.,
RA Celniker S.E., Chang J.L., Chapple C., Chatterji S., Chinwalla A.,
RA Civetta A., Clifton S.W., Comeron J.M., Costello J.C., Coyne J.A., Daub J.,
RA David R.G., Delcher A.L., Delehaunty K., Do C.B., Ebling H., Edwards K.,
RA Eickbush T., Evans J.D., Filipski A., Findeiss S., Freyhult E., Fulton L.,
RA Fulton R., Garcia A.C., Gardiner A., Garfield D.A., Garvin B.E., Gibson G.,
RA Gilbert D., Gnerre S., Godfrey J., Good R., Gotea V., Gravely B.,
RA Greenberg A.J., Griffiths-Jones S., Gross S., Guigo R., Gustafson E.A.,
RA Haerty W., Hahn M.W., Halligan D.L., Halpern A.L., Halter G.M., Han M.V.,
RA Heger A., Hillier L., Hinrichs A.S., Holmes I., Hoskins R.A., Hubisz M.J.,
RA Hultmark D., Huntley M.A., Jaffe D.B., Jagadeeshan S., Jeck W.R.,
RA Johnson J., Jones C.D., Jordan W.C., Karpen G.H., Kataoka E.,
RA Keightley P.D., Kheradpour P., Kirkness E.F., Koerich L.B., Kristiansen K.,
RA Kudrna D., Kulathinal R.J., Kumar S., Kwok R., Lander E., Langley C.H.,
RA Lapoint R., Lazzaro B.P., Lee S.J., Levesque L., Li R., Lin C.F., Lin M.F.,
RA Lindblad-Toh K., Llopart A., Long M., Low L., Lozovsky E., Lu J., Luo M.,
RA Machado C.A., Makalowski W., Marzo M., Matsuda M., Matzkin L.,
RA McAllister B., McBride C.S., McKernan B., McKernan K., Mendez-Lago M.,
RA Minx P., Mollenhauer M.U., Montooth K., Mount S.M., Mu X., Myers E.,
RA Negre B., Newfeld S., Nielsen R., Noor M.A., O'Grady P., Pachter L.,
RA Papaceit M., Parisi M.J., Parisi M., Parts L., Pedersen J.S., Pesole G.,
RA Phillippy A.M., Ponting C.P., Pop M., Porcelli D., Powell J.R.,
RA Prohaska S., Pruitt K., Puig M., Quesneville H., Ram K.R., Rand D.,
RA Rasmussen M.D., Reed L.K., Reenan R., Reily A., Remington K.A.,
RA Rieger T.T., Ritchie M.G., Robin C., Rogers Y.H., Rohde C., Rozas J.,
RA Rubenfield M.J., Ruiz A., Russo S., Salzberg S.L., Sanchez-Gracia A.,
RA Saranga D.J., Sato H., Schaeffer S.W., Schatz M.C., Schlenke T.,
RA Schwartz R., Segarra C., Singh R.S., Sirot L., Sirota M., Sisneros N.B.,
RA Smith C.D., Smith T.F., Spieth J., Stage D.E., Stark A., Stephan W.,
RA Strausberg R.L., Strempel S., Sturgill D., Sutton G., Sutton G.G., Tao W.,
RA Teichmann S., Tobari Y.N., Tomimura Y., Tsolas J.M., Valente V.L.,
RA Venter E., Venter J.C., Vicario S., Vieira F.G., Vilella A.J.,
RA Villasante A., Walenz B., Wang J., Wasserman M., Watts T., Wilson D.,
RA Wilson R.K., Wing R.A., Wolfner M.F., Wong A., Wong G.K., Wu C.I., Wu G.,
RA Yamamoto D., Yang H.P., Yang S.P., Yorke J.A., Yoshida K., Zdobnov E.,
RA Zhang P., Zhang Y., Zimin A.V., Baldwin J., Abdouelleil A., Abdulkadir J.,
RA Abebe A., Abera B., Abreu J., Acer S.C., Aftuck L., Alexander A., An P.,
RA Anderson E., Anderson S., Arachi H., Azer M., Bachantsang P., Barry A.,
RA Bayul T., Berlin A., Bessette D., Bloom T., Blye J., Boguslavskiy L.,
RA Bonnet C., Boukhgalter B., Bourzgui I., Brown A., Cahill P., Channer S.,
RA Cheshatsang Y., Chuda L., Citroen M., Collymore A., Cooke P., Costello M.,
RA D'Aco K., Daza R., De Haan G., DeGray S., DeMaso C., Dhargay N., Dooley K.,
RA Dooley E., Doricent M., Dorje P., Dorjee K., Dupes A., Elong R., Falk J.,
RA Farina A., Faro S., Ferguson D., Fisher S., Foley C.D., Franke A.,
RA Friedrich D., Gadbois L., Gearin G., Gearin C.R., Giannoukos G., Goode T.,
RA Graham J., Grandbois E., Grewal S., Gyaltsen K., Hafez N., Hagos B.,
RA Hall J., Henson C., Hollinger A., Honan T., Huard M.D., Hughes L.,
RA Hurhula B., Husby M.E., Kamat A., Kanga B., Kashin S., Khazanovich D.,
RA Kisner P., Lance K., Lara M., Lee W., Lennon N., Letendre F., LeVine R.,
RA Lipovsky A., Liu X., Liu J., Liu S., Lokyitsang T., Lokyitsang Y.,
RA Lubonja R., Lui A., MacDonald P., Magnisalis V., Maru K., Matthews C.,
RA McCusker W., McDonough S., Mehta T., Meldrim J., Meneus L., Mihai O.,
RA Mihalev A., Mihova T., Mittelman R., Mlenga V., Montmayeur A., Mulrain L.,
RA Navidi A., Naylor J., Negash T., Nguyen T., Nguyen N., Nicol R., Norbu C.,
RA Norbu N., Novod N., O'Neill B., Osman S., Markiewicz E., Oyono O.L.,
RA Patti C., Phunkhang P., Pierre F., Priest M., Raghuraman S., Rege F.,
RA Reyes R., Rise C., Rogov P., Ross K., Ryan E., Settipalli S., Shea T.,
RA Sherpa N., Shi L., Shih D., Sparrow T., Spaulding J., Stalker J.,
RA Stange-Thomann N., Stavropoulos S., Stone C., Strader C., Tesfaye S.,
RA Thomson T., Thoulutsang Y., Thoulutsang D., Topham K., Topping I.,
RA Tsamla T., Vassiliev H., Vo A., Wangchuk T., Wangdi T., Weiand M.,
RA Wilkinson J., Wilson A., Yadav S., Young G., Yu Q., Zembek L., Zhong D.,
RA Zimmer A., Zwirko Z., Jaffe D.B., Alvarez P., Brockman W., Butler J.,
RA Chin C., Gnerre S., Grabherr M., Kleber M., Mauceli E., MacCallum I.;
RT "Evolution of genes and genomes on the Drosophila phylogeny.";
RL Nature 450:203-218(2007).
CC -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle, COPII-coated vesicle
CC membrane {ECO:0000256|ARBA:ARBA00004299}; Peripheral membrane protein
CC {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; CH933807; EDW13122.2; -; Genomic_DNA.
DR RefSeq; XP_002003680.2; XM_002003644.2.
DR EnsemblMetazoa; FBtr0422953; FBpp0380941; FBgn0140787.
DR KEGG; dmo:Dmoj_GI18047; -.
DR eggNOG; KOG1984; Eukaryota.
DR HOGENOM; CLU_004589_1_1_1; -.
DR InParanoid; B4KFK7; -.
DR Proteomes; UP000009192; Unassembled WGS sequence.
DR GO; GO:0030127; C:COPII vesicle coat; IEA:InterPro.
DR GO; GO:0070971; C:endoplasmic reticulum exit site; IEA:EnsemblMetazoa.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0071711; P:basement membrane organization; IEA:EnsemblMetazoa.
DR GO; GO:0000902; P:cell morphogenesis; IEA:EnsemblMetazoa.
DR GO; GO:0040003; P:chitin-based cuticle development; IEA:EnsemblMetazoa.
DR GO; GO:0007029; P:endoplasmic reticulum organization; IEA:EnsemblMetazoa.
DR GO; GO:0006888; P:endoplasmic reticulum to Golgi vesicle-mediated transport; IEA:InterPro.
DR GO; GO:0007030; P:Golgi organization; IEA:EnsemblMetazoa.
DR GO; GO:0006886; P:intracellular protein transport; IEA:InterPro.
DR GO; GO:0035149; P:lumen formation, open tracheal system; IEA:EnsemblMetazoa.
DR GO; GO:0030011; P:maintenance of cell polarity; IEA:EnsemblMetazoa.
DR GO; GO:0016203; P:muscle attachment; IEA:EnsemblMetazoa.
DR GO; GO:0022409; P:positive regulation of cell-cell adhesion; IEA:EnsemblMetazoa.
DR GO; GO:0048081; P:positive regulation of cuticle pigmentation; IEA:EnsemblMetazoa.
DR GO; GO:0003331; P:positive regulation of extracellular matrix constituent secretion; IEA:EnsemblMetazoa.
DR GO; GO:0034394; P:protein localization to cell surface; IEA:EnsemblMetazoa.
DR GO; GO:0072659; P:protein localization to plasma membrane; IEA:EnsemblMetazoa.
DR GO; GO:0009306; P:protein secretion; IEA:EnsemblMetazoa.
DR GO; GO:0008360; P:regulation of cell shape; IEA:EnsemblMetazoa.
DR GO; GO:0035158; P:regulation of tube diameter, open tracheal system; IEA:EnsemblMetazoa.
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; SEC24-RELATED PROTEIN; 1.
DR PANTHER; PTHR13803:SF4; SECRETORY 24CD, ISOFORM C; 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 3: Inferred from homology;
KW Cytoplasmic vesicle {ECO:0000256|ARBA:ARBA00023329};
KW Protein transport {ECO:0000256|ARBA:ARBA00022927};
KW Reference proteome {ECO:0000313|Proteomes:UP000009192};
KW Transport {ECO:0000256|ARBA:ARBA00022448}.
FT DOMAIN 533..571
FT /note="Zinc finger Sec23/Sec24-type"
FT /evidence="ECO:0000259|Pfam:PF04810"
FT DOMAIN 610..854
FT /note="Sec23/Sec24 trunk"
FT /evidence="ECO:0000259|Pfam:PF04811"
FT DOMAIN 859..943
FT /note="Sec23/Sec24 beta-sandwich"
FT /evidence="ECO:0000259|Pfam:PF08033"
FT DOMAIN 954..1055
FT /note="Sec23/Sec24 helical"
FT /evidence="ECO:0000259|Pfam:PF04815"
FT DOMAIN 1074..1131
FT /note="Gelsolin-like"
FT /evidence="ECO:0000259|Pfam:PF00626"
FT REGION 1..439
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..25
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 26..45
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 54..82
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 122..146
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 147..171
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 172..207
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 220..234
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 320..338
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 350..415
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1247 AA; 135113 MW; C52F575F97C30AEE CRC64;
MNPNMYGPPP TQFQPQYPAG PPRGPTGWPS QQQQQQQQQQ PLQSQPPPQQ QQPHQQPYVN
GNYQQQLTTS MSGLSVSGNP LKPSQPPIGM PTGGGGAPVA APSGPFNQFN SNAPPTSQPM
PPASSGMNFN NNNNAYAAAY ANGSTGPSPS PAPPVSAAAA GPSPSPAPSM FPPTSAASNM
AQPTSAAATM PQNVPGGINQ MTLNSASLAG LPHMPPKSSA QQLPPTSTAP GQALPPVTQA
GGYGRPGQPQ MPPGAAAPAA FAQPGMPPQR PAAGGAPATA FAQPGMGTQP PAVGGPSSNS
YGVPPPGNFP GSYAGQPAPG PGTAPAPGAY PGAPPLPGQQ AGPQQFGAAP PPAVGYPPQP
GQQLQQPSMP GYPPQPMPGY PPQAGQQPQQ PMPGYPPQPG SYPGQPGPGR PGYNQPPMPG
AGSMYQQAPP RRLDPDQMPN PIQVMIENQQ AAGGIFVTNQ PGLLPPLVTT KFVVHDQGNS
SPRFIRSSLY CIPNTGDLLK TTALPLTLNI SPLARIGKGE MEPPIVNFGD MGPIRCNRCK
AYMSPNMQFV DAGRRFQCLM CKVTTEVHPD YYQHLDHTGQ RVDKHERPEL LLGTYEFLAT
KDYCRNNTAP EVPAFIFVID VSYNTIKSGL VHLLCSQIKN ILKHLPVDQG QDKSKVRVGF
ITYNSTVHFY NIKSNLAQPQ MMVVGDVQEM FMPLLDGFLC HPEESAAVID ALMEEIPRMF
VDTKETETIL YPAIQAGLEA LKASNASGKL LVFNSTLPIA EAPGKLKNRD DRKLLGTDKE
KTVLTPQTTV YNQLGQECVQ QGCSVDLFVF NNAYIDIATI GQVSRLTGGE VYKYTYFQAE
LDGKRLIEDI IKNVSRPIAF DAVMRVRTSA GIRPTEFFGH FYMSNTTDVE LASIDATKSV
SIEIKHDDKL APEENVYIQV ALLYTSCSGQ RRLRILNLAL RVTVTIADVF KSCDLDAMML
FFAKQACFKL MEHSPKQVKD NLIQRSAQIL ACYRKHCTSP TSAGQLILPE CLKLLPLYAS
CLLKNDAVSG GSDMTLDDRS YVIQFVLAMD LNMSVNYLYP RFIPIHNVDI DDTSLPTPVR
CTHEKITEDG AYILENGVHM FVWLGQSLSP SFVQSVFGVQ CTQQVNAERF AITADTPLAR
RITGIINQIM EERTRYMRVT CVRQNDKLES VFRHFLIEDR GTDGSASYVD FLCHMHKEIK
DLLSXHVGNS HKSPTASCYS TEERWSRSYS QNRARMRRLS FSSRRFK
//
