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Database: UniProt
Entry: A1CP38_ASPCL
LinkDB: A1CP38_ASPCL
Original site: A1CP38_ASPCL 
ID   A1CP38_ASPCL            Unreviewed;       770 AA.
AC   A1CP38;
DT   23-JAN-2007, integrated into UniProtKB/TrEMBL.
DT   23-JAN-2007, sequence version 1.
DT   27-MAR-2024, entry version 56.
DE   RecName: Full=Protein CASP {ECO:0000256|ARBA:ARBA00018691};
GN   ORFNames=ACLA_021170 {ECO:0000313|EMBL:EAW07409.1};
OS   Aspergillus clavatus (strain ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 /
OS   NRRL 1 / QM 1276 / 107).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Fumigati.
OX   NCBI_TaxID=344612 {ECO:0000313|EMBL:EAW07409.1, ECO:0000313|Proteomes:UP000006701};
RN   [1] {ECO:0000313|EMBL:EAW07409.1, ECO:0000313|Proteomes:UP000006701}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 / NRRL 1
RC   {ECO:0000313|Proteomes:UP000006701};
RX   PubMed=18404212; DOI=10.1371/journal.pgen.1000046;
RA   Fedorova N.D., Khaldi N., Joardar V.S., Maiti R., Amedeo P., Anderson M.J.,
RA   Crabtree J., Silva J.C., Badger J.H., Albarraq A., Angiuoli S., Bussey H.,
RA   Bowyer P., Cotty P.J., Dyer P.S., Egan A., Galens K., Fraser-Liggett C.M.,
RA   Haas B.J., Inman J.M., Kent R., Lemieux S., Malavazi I., Orvis J.,
RA   Roemer T., Ronning C.M., Sundaram J.P., Sutton G., Turner G., Venter J.C.,
RA   White O.R., Whitty B.R., Youngman P., Wolfe K.H., Goldman G.H.,
RA   Wortman J.R., Jiang B., Denning D.W., Nierman W.C.;
RT   "Genomic islands in the pathogenic filamentous fungus Aspergillus
RT   fumigatus.";
RL   PLoS Genet. 4:E1000046-E1000046(2008).
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004211}; Single-
CC       pass type IV membrane protein {ECO:0000256|ARBA:ARBA00004211}.
CC   -!- SIMILARITY: Belongs to the CASP family.
CC       {ECO:0000256|ARBA:ARBA00006415}.
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DR   EMBL; DS027059; EAW07409.1; -; Genomic_DNA.
DR   RefSeq; XP_001268835.1; XM_001268834.1.
DR   AlphaFoldDB; A1CP38; -.
DR   STRING; 344612.A1CP38; -.
DR   EnsemblFungi; EAW07409; EAW07409; ACLA_021170.
DR   GeneID; 4701611; -.
DR   KEGG; act:ACLA_021170; -.
DR   VEuPathDB; FungiDB:ACLA_021170; -.
DR   eggNOG; KOG0963; Eukaryota.
DR   HOGENOM; CLU_016758_0_0_1; -.
DR   OMA; FAGYCFA; -.
DR   OrthoDB; 1643779at2759; -.
DR   Proteomes; UP000006701; Unassembled WGS sequence.
DR   GO; GO:0000139; C:Golgi membrane; IEA:InterPro.
DR   GO; GO:0006891; P:intra-Golgi vesicle-mediated transport; IEA:InterPro.
DR   InterPro; IPR012955; CASP_C.
DR   PANTHER; PTHR14043; CCAAT DISPLACEMENT PROTEIN-RELATED; 1.
DR   PANTHER; PTHR14043:SF2; HOMEOBOX PROTEIN CUT; 1.
DR   Pfam; PF08172; CASP_C; 1.
PE   3: Inferred from homology;
KW   Coiled coil {ECO:0000256|ARBA:ARBA00023054, ECO:0000256|SAM:Coils};
KW   Golgi apparatus {ECO:0000256|ARBA:ARBA00023034};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006701};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}; Transport {ECO:0000256|ARBA:ARBA00022448}.
FT   TRANSMEM        698..716
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          460..719
FT                   /note="CASP C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF08172"
FT   REGION          1..32
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          169..192
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          406..426
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          266..300
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          450..491
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          556..604
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        9..32
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        172..192
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   770 AA;  84589 MW;  65F2021ED004DA06 CRC64;
     MDTFAITEGI VPESNNQDGH ESENATSEQH LEGANKFQRA IAAWRSIDLN TTVAKLDSTA
     SDIVAQQRDA LVQRKDLAQK TKDFRKLDDS SKLAEYKSLL KSYQSFIDLL TNQGKASSSA
     FLQLYSSLSE APDPYPLLEA SVDSLVLSEQ TVPKLTSEKE QLQASVNRLT SQLDDTEKRL
     QEERSARKNL EDNQEAKIKE IESSWSAVLA EKTNNWAAKE KTLEEKVENQ ERLLKEVKAS
     YEVSQRLGQE DDGGDSSHHG AAAAELELVS ADLEKTSLRL AEVEARNEQL RLELAQAVSH
     SSQTAQATSV EDDPAYLRLQ SENSSLLRKL DAARYDRDSV RHTWESKISQ LERQGSKVAA
     ERDELRSRLE KTADYEDIRR ELEMIKSIEF SVGDGDDDEV AELVNNDAGT TANGSSSRSR
     DGSKNTSLEQ LLLARNKKLT DELTVLRVSH RDLQGQLELL REDLTSTKQE LEKSQQLSTT
     LENDLLRVQQ EAANAFPSSA MSVAGTYSSR YPHSSRRGAV SPTSSIISGF DQAAASANTM
     ESIRAGEPVG GGSGLLPMIQ AQRDRFKTKN AELEEELSKL YSTVKSLRQE VASLQKDNLN
     LYEKTRYVST YSRGHGAASS ASAYANKPSS SSVHFSADTP SGLSLDRYQT AYEANLSPFA
     AFRGRESVRA YKRMSLPERV VFSLTRIILA NRTSRNLFAG YCFALHVLLF LVLYMMSSTE
     IERNSGASLG AAAAAAMAGA GGSGSSSGYG GSGGKLHGDN WQAEGFNQVT
//
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