FSC1_SCHPO
ID FSC1_SCHPO Reviewed; 728 AA.
AC O94439;
DT 16-DEC-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 106.
DE RecName: Full=FAS1 domain-containing protein fsc1;
DE Flags: Precursor;
GN Name=fsc1; ORFNames=SPAC22H12.05c;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
RN [2]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=16823372; DOI=10.1038/nbt1222;
RA Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S.,
RA Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S.,
RA Yoshida M.;
RT "ORFeome cloning and global analysis of protein localization in the fission
RT yeast Schizosaccharomyces pombe.";
RL Nat. Biotechnol. 24:841-847(2006).
RN [3]
RP DISRUPTION PHENOTYPE, SUBCELLULAR LOCATION, AND FUNCTION.
RX PubMed=23950735; DOI=10.1371/journal.pgen.1003715;
RA Sun L.L., Li M., Suo F., Liu X.M., Shen E.Z., Yang B., Dong M.Q., He W.Z.,
RA Du L.L.;
RT "Global analysis of fission yeast mating genes reveals new autophagy
RT factors.";
RL PLoS Genet. 9:E1003715-E1003715(2013).
CC -!- FUNCTION: Required for the fusion of autophagosomes with the vacuole.
CC {ECO:0000269|PubMed:23950735}.
CC -!- SUBCELLULAR LOCATION: Vacuole membrane {ECO:0000269|PubMed:16823372,
CC ECO:0000269|PubMed:23950735}; Single-pass type I membrane protein
CC {ECO:0000269|PubMed:16823372, ECO:0000269|PubMed:23950735}.
CC -!- DISRUPTION PHENOTYPE: Impairs atg8-processing.
CC {ECO:0000269|PubMed:23950735}.
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DR EMBL; CU329670; CAA22557.1; -; Genomic_DNA.
DR PIR; T38220; T38220.
DR RefSeq; NP_593117.1; NM_001018514.2.
DR AlphaFoldDB; O94439; -.
DR SMR; O94439; -.
DR BioGRID; 278319; 22.
DR STRING; 4896.SPAC22H12.05c.1; -.
DR iPTMnet; O94439; -.
DR MaxQB; O94439; -.
DR PaxDb; O94439; -.
DR PRIDE; O94439; -.
DR EnsemblFungi; SPAC22H12.05c.1; SPAC22H12.05c.1:pep; SPAC22H12.05c.
DR GeneID; 2541828; -.
DR KEGG; spo:SPAC22H12.05c; -.
DR PomBase; SPAC22H12.05c; fsc1.
DR VEuPathDB; FungiDB:SPAC22H12.05c; -.
DR eggNOG; KOG1437; Eukaryota.
DR HOGENOM; CLU_386923_0_0_1; -.
DR InParanoid; O94439; -.
DR OMA; PPYPPWM; -.
DR PhylomeDB; O94439; -.
DR PRO; PR:O94439; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0000329; C:fungal-type vacuole membrane; IDA:PomBase.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016236; P:macroautophagy; IMP:PomBase.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR Gene3D; 2.30.180.10; -; 3.
DR InterPro; IPR036378; FAS1_dom_sf.
DR InterPro; IPR000782; FAS1_domain.
DR Pfam; PF02469; Fasciclin; 2.
DR SMART; SM00554; FAS1; 3.
DR SUPFAM; SSF82153; SSF82153; 3.
DR PROSITE; PS50213; FAS1; 2.
PE 3: Inferred from homology;
KW Autophagy; Glycoprotein; Membrane; Protein transport; Reference proteome;
KW Repeat; Signal; Transmembrane; Transmembrane helix; Transport; Vacuole.
FT SIGNAL 1..21
FT /evidence="ECO:0000255"
FT CHAIN 22..728
FT /note="FAS1 domain-containing protein fsc1"
FT /id="PRO_0000356245"
FT TOPO_DOM 22..670
FT /note="Vacuolar"
FT /evidence="ECO:0000255"
FT TRANSMEM 671..691
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 692..728
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 29..151
FT /note="FAS1 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00082"
FT DOMAIN 154..285
FT /note="FAS1 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00082"
FT CARBOHYD 89
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 404
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 501
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 728 AA; 82589 MW; ADF34622B35463C7 CRC64;
MNLQFRLYLL FILLFISFAN GKNEYEDKST SIIDLLSSKS QFSKLIRRLQ RNRLVPYLNR
NKGLTLFAPL NEAFPDDSIE PNLLYYIVNT TELDRSVLRT QLKSSDGQQI ALKIHYKAET
GRAYDKVNNA QIVQSNWRAD SGVVQVIDNI IDLPPPALEI LSSEKDFSIF HRLSVAWVGE
YSSVTMLVPD SSAFLNVYTN TELAYLYSMY AAEDVKTLIH QHILVNQRVY AEDVIEPKTF
HYKNGISISM KFDKDQKKLF INDVSTTKYD LLTFSGAIHT VSSLINPEII SFTPAKYLIG
IGAAWFSEKL SRERKSISVD KTSKRAILAP TNWAYREIID IDYHIIENFD LPAPNKYALY
VTNIKSGNSV GEDTNALVRI ATGSAGEMYV NVETRSIQSE NIGNVSLYVL DKDIEPPQPL
LSQLILVDEI SFSVRYLASL GLGDYTKVTW FLVKNSAWTQ LGLVHLVLQQ NLELLESVML
DYAFEGIAFY GSSDEAWASG NYTTLSNKEF LIEGVYEDSN SRNKRDLLRI NNEIYEVQTR
DLLVKDGVVH LVDKVKLPFS VSQKDMIIAG GRKEFLELLD KFEMLDMLDS GYPVVVPSLT
GSDVNTKDSS FAERHIIDPE KRNFVISGSR LSVDSSPWIS IQDYGYSELG NVYFVQNAIP
TKRQNRWRIT FISISGLLLS VGICVLCYKI YFKFFRNRFM NQGEREPLLA PADSDTMAGR
RNSSSLSV
