CSF1_ASHGO
ID CSF1_ASHGO Reviewed; 2887 AA.
AC Q74ZX0;
DT 21-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 25-MAY-2022, entry version 79.
DE RecName: Full=Protein CSF1;
GN Name=CSF1; OrderedLocusNames=AGR088W;
OS Ashbya gossypii (strain ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056)
OS (Yeast) (Eremothecium gossypii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Eremothecium.
OX NCBI_TaxID=284811;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX PubMed=15001715; DOI=10.1126/science.1095781;
RA Dietrich F.S., Voegeli S., Brachat S., Lerch A., Gates K., Steiner S.,
RA Mohr C., Poehlmann R., Luedi P., Choi S., Wing R.A., Flavier A.,
RA Gaffney T.D., Philippsen P.;
RT "The Ashbya gossypii genome as a tool for mapping the ancient Saccharomyces
RT cerevisiae genome.";
RL Science 304:304-307(2004).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX PubMed=23749448; DOI=10.1534/g3.112.002881;
RA Dietrich F.S., Voegeli S., Kuo S., Philippsen P.;
RT "Genomes of Ashbya fungi isolated from insects reveal four mating-type
RT loci, numerous translocations, lack of transposons, and distinct gene
RT duplications.";
RL G3 (Bethesda) 3:1225-1239(2013).
CC -!- FUNCTION: Required for the glucose and other nutrients uptake at low
CC temperature. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type II
CC membrane protein {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the CSF1 family. {ECO:0000305}.
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DR EMBL; AE016820; AAS54577.1; -; Genomic_DNA.
DR RefSeq; NP_986753.1; NM_211815.2.
DR STRING; 33169.AAS54577; -.
DR PRIDE; Q74ZX0; -.
DR EnsemblFungi; AAS54577; AAS54577; AGOS_AGR088W.
DR GeneID; 4623055; -.
DR KEGG; ago:AGOS_AGR088W; -.
DR eggNOG; KOG3596; Eukaryota.
DR HOGENOM; CLU_000126_1_0_1; -.
DR InParanoid; Q74ZX0; -.
DR OMA; YTWHYYR; -.
DR Proteomes; UP000000591; Chromosome VII.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0006113; P:fermentation; IEA:InterPro.
DR InterPro; IPR029636; Csf1.
DR PANTHER; PTHR32085; PTHR32085; 1.
PE 3: Inferred from homology;
KW Glycoprotein; Membrane; Reference proteome; Signal-anchor; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..2887
FT /note="Protein CSF1"
FT /id="PRO_0000228142"
FT TOPO_DOM 1
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 2..22
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 23..2887
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT CARBOHYD 51
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 205
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 213
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 349
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 443
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 929
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1104
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1196
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1364
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1553
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1559
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1584
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1712
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1827
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1848
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1984
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1985
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2021
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2075
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2255
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2273
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2462
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2592
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2702
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2739
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2852
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 2887 AA; 327181 MW; FA7B48B618E16642 CRC64;
MVIFAIFYVG RVLGYIVSKA ANLVLWKQYR VTVSIQSLVF SPLAGKVHFK NVSVTSQDQL
ISVLKGTITW RYWLIGRYRR SGTADGARRC RFALKFEGFE YFVYNRNGVY DRIARELDGE
DTSAEPTVSV PSVEEVIAEL QDDPLIRRFL PVEFLHNKGA IVLGNKQTHS VAIMNYEKLA
GTVSIEVPDD TRAPSSFRTE AKISNCTVAI KPNISYEVDN PVKIYVEPKR TARLWKKYKT
LLGTVLEATL HAKRKKEQHQ TPKWYDNWRG LSMYDVNLDE ELDEEVKFDI EHHEYAKCTT
VLKADQMDVT YSYGMPGTAR VTDSDNAENP LLERPELDHS VDILVYDANC TYGPWANRQV
QQCLRVFSPT VCRNFKLRTP EEIAQQTEPA AFKLSVTIME DSVLRVPMKE SSKDAAFLEK
YKQTRDETRP FGWIDIRIAK ESNITVRMAA YPTENGFENI LHANLVDTTI STSVNHDTLL
KAKSHDITVD FSYPYGWQDK AEWNFNVCST QAELFVLRDH VYLISDLVTD FSGGEEVLYE
QFRPFDYRFR WDIRGYSAYL NVNDANIINN PIDFGENCYL SVHGDDAEIT FSLPITSIIQ
KYVTVDFNIF TPHFSLFLNA PPWHTFSELL HYKEIGRSKN FNIKGSYTSY SEVDVDNVDA
LNIACETDYI VVLCYGVILK CMLNVKVNYF GEMVHFRTTE EYVEELQRRN KQNPSTCRPF
NSDGNVHDSD VVATESNEII DASFDAFGGP PTIKKSALKR SINELDVWFT FISKGGCFFF
PENIYKFDAC LGFYFDNLEA SLRFLNYYVD AAVSLDSIYF KRHTDIDART LFKVIEDIGI
PIDASDAYLS QFSFRLHKML GIMPSEESYA CEFDVRVDTL DVHCDLAVLK AFVNTLRNLA
FGFKDVENSL QYEREQVFDL NKISCVIENV TVKLQNVDKD EDIWLSLNLP VTTLTSFDLA
NERYSRRSDL SIPELLFGIY RGDSESTCLG AFSTGVTVTL FERFEQFARC RVLQRKHILV
NDAPFHRCSF MLPPEYKKMP IYRSLYGCIP PSSSLPLFPE PISADNFEVI FEKLLGEIYQ
EYASDSSYQI TDDSISSTEH DYHNQTVNAA IGTSSSLFIR SQNHQQTLSS FIVEFDPIDG
YLDLSATEFM LEIYKYLTEV SLDEAIDSLE IGIINQFIQT FGEDNGISEV RVLCPNISLS
ATNKQSKFSM FKLSSKIKNL DITSRIKSSD PNLKPDPEKT TLCYKIDYIR ANIVQDGIVV
PPKQPSQLFS CSIELLEGYL SYDKLSLLDN NVQSCSVTLS PGTDKLLFEF LNPFISTFDL
LQRELSSFED TLLASKREFL LNILRGGRDY EIQHDPPVIT KPANITRFSN RHIRSAESWR
IIMRLRHILN YLPQEWHQSF TRHLGTQDFT SPEEAGKEFL SIFSDWRSWE PTDVQGSFVH
EKVFTKKRSR PFAALQGFTF SSDDIRLNMK DDARVPITVK GVTLGIRNNG LAPEQVDGRT
EGSMPDPDYI SFCTTDEVVM RVDRSFVKTL KEFRDLIHRF KIGGPVGTAK HDNVSLFSNI
TFQFGKLYVV AKLAGVYLRI CLDNLSALML TSQSSVESKV ISSSTLSFDH MQAILGYRSF
RFMTIDIDMF SVLLHYLPGQ GCYSIDWKAR KFHIDSSSAT TKDLTESLPY VRDEIKYLVE
ALVPELFAEP PIERESSGNK IHAVLFQGQV ANITLKLQIL SPFIILYCAE NFELQAESTD
SVIFDLNSGE SYMEISSAKQ KLDYFKYTHT CLKLSGTSSS ARLFEHISCD IGILKLSVFD
LKTRITDLLQ DIKAALFSMK SLSDILNISQ SSPTASAFGS WFSILPDNLS LQATYAGLLL
GFGHTLYILE FNNFEAKHTR DGLPDAITPR PCFKVDHSIE SASFLIKDRR IDDRLAKVVD
FAVNFNMVHD TDLCIQSVQI ESTHLKITLA PMTVVRLLSL INEFGIIRKQ FTEESIYTPS
SAHNNSTATE CLEPSVWRLI IKSGHILSHD FSIVWLFDIP NSSADGLICG YDRLFSVYEK
PYGKLTLLNA YFSAAKILAS EADFYSSVVR KQRINTSYLS DMQLRYWFTE DSENTDLFIR
IHGAKLAVDI SAEIVTLLEE TIQSIQTFNN LKKALVDPFR TKKQDSDISK EPYNWNNQLA
TGVRSLNCII NYAGVTLKLH SHDGRGDASP LELTSPSYKV AIDYKYFPNL EKTHRFRTLI
TATPTHNTFY STSAFLIHDL CYRFSKLLKT SSTENKSSSA STSSSIKVEG SDNSTLLGSI
DLVIILNVGK QEVTFSCEPK AKVQATVGFE KFDIKIFNNN INDEESLCLA IEIENLMTNS
RHIYSREVCA SLKLRHISMV FDIMGSQVRR IYGSTLISSP LFYFNMKQLQ DLKLFIDQWF
PQKTPMNTGS YPEGVLVDDI SRSIGSKFYK GSSSSSFTWG YSVIVAGSCA EIELGPSLGV
LNVTSEDVWA ISKQQVDWSQ QLDLNMGKLD VTSSGRLGGN FLVRNAHLSL ELKWPNPKDF
FQVPLVCVKL GSDTVDTKLS FDYHTFFISS LKQGYASLFN ERDEDGSLAD LLSVTVSFES
VNIFLTALAA ANISDIKNSI TRLKKDNELS YLSSFLASDQ PSDEPEEDGG IFDTLSLLRT
QLSLNLGVFR LQISPTSLFD SDVLILTATK MMANTGIQAD IKIKTDLHWQ LDDVSLALLP
FNNSLDESYL ATMEVGKYIE LSSTIQGGAI FSAPSIVVNM TTWQEPQSNV IELLYSTSFG
GTVKIRWNLG PISFIKDMWQ AHMNAMQLRE GYYHGLAESG VAVTPLNSKA VPLEMHLGSD
YQYLPLQEPD IEMPRIKDLG DATPPIEWFG VNRTKFPGFT HQFVIVPLQK LARTAEKEYE
KILGRAL
