APSA_EMENI
ID APSA_EMENI Reviewed; 1676 AA.
AC Q00083; C8VDM5; Q5AVC3;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2007, sequence version 2.
DT 25-MAY-2022, entry version 110.
DE RecName: Full=Anucleate primary sterigmata protein A;
GN Name=apsA; ORFNames=AN7757;
OS Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 /
OS M139) (Aspergillus nidulans).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Nidulantes.
OX NCBI_TaxID=227321;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX PubMed=7860626; DOI=10.1083/jcb.128.4.485;
RA Fischer R., Timberlake W.E.;
RT "Aspergillus nidulans apsA (anucleate primary sterigmata) encodes a coiled-
RT coil protein required for nuclear positioning and completion of asexual
RT development.";
RL J. Cell Biol. 128:485-498(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX PubMed=16372000; DOI=10.1038/nature04341;
RA Galagan J.E., Calvo S.E., Cuomo C., Ma L.-J., Wortman J.R., Batzoglou S.,
RA Lee S.-I., Bastuerkmen M., Spevak C.C., Clutterbuck J., Kapitonov V.,
RA Jurka J., Scazzocchio C., Farman M.L., Butler J., Purcell S., Harris S.,
RA Braus G.H., Draht O., Busch S., D'Enfert C., Bouchier C., Goldman G.H.,
RA Bell-Pedersen D., Griffiths-Jones S., Doonan J.H., Yu J., Vienken K.,
RA Pain A., Freitag M., Selker E.U., Archer D.B., Penalva M.A., Oakley B.R.,
RA Momany M., Tanaka T., Kumagai T., Asai K., Machida M., Nierman W.C.,
RA Denning D.W., Caddick M.X., Hynes M., Paoletti M., Fischer R., Miller B.L.,
RA Dyer P.S., Sachs M.S., Osmani S.A., Birren B.W.;
RT "Sequencing of Aspergillus nidulans and comparative analysis with A.
RT fumigatus and A. oryzae.";
RL Nature 438:1105-1115(2005).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX PubMed=19146970; DOI=10.1016/j.fgb.2008.12.003;
RA Wortman J.R., Gilsenan J.M., Joardar V., Deegan J., Clutterbuck J.,
RA Andersen M.R., Archer D., Bencina M., Braus G., Coutinho P., von Dohren H.,
RA Doonan J., Driessen A.J., Durek P., Espeso E., Fekete E., Flipphi M.,
RA Estrada C.G., Geysens S., Goldman G., de Groot P.W., Hansen K.,
RA Harris S.D., Heinekamp T., Helmstaedt K., Henrissat B., Hofmann G.,
RA Homan T., Horio T., Horiuchi H., James S., Jones M., Karaffa L.,
RA Karanyi Z., Kato M., Keller N., Kelly D.E., Kiel J.A., Kim J.M.,
RA van der Klei I.J., Klis F.M., Kovalchuk A., Krasevec N., Kubicek C.P.,
RA Liu B., Maccabe A., Meyer V., Mirabito P., Miskei M., Mos M., Mullins J.,
RA Nelson D.R., Nielsen J., Oakley B.R., Osmani S.A., Pakula T., Paszewski A.,
RA Paulsen I., Pilsyk S., Pocsi I., Punt P.J., Ram A.F., Ren Q., Robellet X.,
RA Robson G., Seiboth B., van Solingen P., Specht T., Sun J.,
RA Taheri-Talesh N., Takeshita N., Ussery D., vanKuyk P.A., Visser H.,
RA van de Vondervoort P.J., de Vries R.P., Walton J., Xiang X., Xiong Y.,
RA Zeng A.P., Brandt B.W., Cornell M.J., van den Hondel C.A., Visser J.,
RA Oliver S.G., Turner G.;
RT "The 2008 update of the Aspergillus nidulans genome annotation: a community
RT effort.";
RL Fungal Genet. Biol. 46:S2-13(2009).
RN [4]
RP CHARACTERIZATION.
RX PubMed=9379904; DOI=10.1046/j.1365-2958.1997.5131873.x;
RA Suelmann R., Sievers N., Fischer R.;
RT "Nuclear traffic in fungal hyphae: in vivo study of nuclear migration and
RT positioning in Aspergillus nidulans.";
RL Mol. Microbiol. 25:757-769(1997).
CC -!- FUNCTION: Required for nuclear positioning and completion of asexual
CC development.
CC -!- SUBCELLULAR LOCATION: Membrane; Peripheral membrane protein.
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DR EMBL; X82289; CAA57733.1; -; Genomic_DNA.
DR EMBL; AACD01000132; EAA61545.1; -; Genomic_DNA.
DR EMBL; BN001304; CBF80046.1; -; Genomic_DNA.
DR PIR; A56508; A56508.
DR RefSeq; XP_681026.1; XM_675934.1.
DR AlphaFoldDB; Q00083; -.
DR SMR; Q00083; -.
DR STRING; 162425.CADANIAP00000894; -.
DR PRIDE; Q00083; -.
DR EnsemblFungi; CBF80046; CBF80046; ANIA_07757.
DR EnsemblFungi; EAA61545; EAA61545; AN7757.2.
DR GeneID; 2869470; -.
DR KEGG; ani:AN7757.2; -.
DR VEuPathDB; FungiDB:AN7757; -.
DR eggNOG; ENOG502QWQU; Eukaryota.
DR HOGENOM; CLU_001023_0_0_1; -.
DR InParanoid; Q00083; -.
DR OMA; NIHREKT; -.
DR OrthoDB; 57988at2759; -.
DR Proteomes; UP000000560; Chromosome IV.
DR Proteomes; UP000005890; Unassembled WGS sequence.
DR GO; GO:0005938; C:cell cortex; ISS:AspGD.
DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IDA:AspGD.
DR GO; GO:0005543; F:phospholipid binding; IEA:InterPro.
DR GO; GO:0015631; F:tubulin binding; IBA:GO_Central.
DR GO; GO:0048315; P:conidium formation; IMP:AspGD.
DR GO; GO:0030989; P:dynein-driven meiotic oscillatory nuclear movement; IBA:GO_Central.
DR GO; GO:0051654; P:establishment of mitochondrion localization; IBA:GO_Central.
DR GO; GO:0032065; P:maintenance of protein location in cell cortex; IEA:InterPro.
DR GO; GO:0000226; P:microtubule cytoskeleton organization; IMP:AspGD.
DR GO; GO:0007097; P:nuclear migration; IMP:AspGD.
DR GO; GO:0051647; P:nucleus localization; IMP:AspGD.
DR InterPro; IPR024774; PH_dom-Mcp5-type.
DR InterPro; IPR001849; PH_domain.
DR Pfam; PF12814; Mcp5_PH; 1.
DR SMART; SM00233; PH; 1.
DR PROSITE; PS50003; PH_DOMAIN; 1.
PE 1: Evidence at protein level;
KW Coiled coil; Membrane; Reference proteome.
FT CHAIN 1..1676
FT /note="Anucleate primary sterigmata protein A"
FT /id="PRO_0000064645"
FT DOMAIN 1393..1504
FT /note="PH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT REGION 1..35
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 160..180
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 353..394
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 439..712
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1027..1050
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1176..1201
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1220..1270
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1297..1354
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1511..1589
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1654..1676
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 51..127
FT /evidence="ECO:0000255"
FT COILED 193..359
FT /evidence="ECO:0000255"
FT COILED 408..453
FT /evidence="ECO:0000255"
FT COMPBIAS 160..176
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 357..376
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 459..491
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 502..541
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 542..559
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 586..621
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 644..668
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1027..1045
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1187..1201
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1229..1270
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1312..1340
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1529..1566
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 593
FT /note="S -> T (in Ref. 1; CAA57733)"
FT /evidence="ECO:0000305"
FT CONFLICT 943..944
FT /note="EL -> DV (in Ref. 1; CAA57733)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1676 AA; 183686 MW; CE2EE5DF7D4B0049 CRC64;
MEDSQRGNAS MMSMMDDPFV VSPEGARDPP STNQYSTFDA QLFNLDASTP AQAKRALEAH
LAETERRLEE ASKLGTALVE QRKDLEDKLR EVEQQQEEGQ IGEELRRKLA DLEREYNEIG
QETARAFLAP KRLAGGDDGH LGTPSMDQKS PLHSALFAGQ ATNSPSKVSV PSRKSRNQSN
RVHDIEFATE ISTSLLAQVR QLQSLLAERE ETLKTVNLEK SRLELEAEGY AQRIRALDES
EERYKDENWA LETKIHELMA AVKDVTDRET KLTSSLGAAT AEKSAMEREL EDLKQANAKL
IEDHTAAQKA NDAEINTLRR NLSAGDAERL TLQRKLEDMN TQNQELAKAV AMRLRQQEAE
STREVVRPHD SEDEEQATPE NSPPPSPNKF TPRHNHLETE TLRSSLGHAH RMIQNLRSTI
HREKTEKIEL KRMLQEARDE VEQRRRDSVA ANGPTNKRQK TKAETRKPAR PDLLGAGRKK
AEVEIHDSDW ESNAGDISPT HKASNDSRDR RGDQPIDDRS DAYHTATEAD DPFETANERE
TTTESEAFQT GVESMAGDST DSDELTETED RVQRTPRGRV SSMTLAKARD RTSYYSTAST
SADEGDSTDP GTPSISQFST PRYRLRKKRS VLRKIRPSGE APMAFNSRPS SARESPSTSF
TRDTSAAPEG QSLFAELAEV DGDEDDFGPP MQFEAASPST PRMLPGFDSR RPSAVTVELP
SKPDMVDSGV MTDPWEPNLH LASQTDDETV ISVPVTPDKP TMSDASTGMD VVESPSLVHS
STQWTPLKPN AETSDDHVLS VPTPPKMAWD GQTLNEERKV DIPDSPTTQR ELNISSVSFE
ETEPVAPSFP ELRTAFFVGS TTEPVAAPVP VPPEVALSPI SSQTTQPTEP VIPAPPEPEP
IYVPEMAFSQ ILVEDTLPIL AKLPEPAPER VFAEQGTSTD IAELSVSAIS SEQTEPVEPV
YEPKQDVAIV AEAVPEGPLS FVEQGTNTDD VEISFPAISS VETEPVAPVR ETKDDVPEPV
LSLTEQGTST DTVEFSVSSI SSEETEPVEP IREAKEEAAA VDDVASESTH PVLSIFLTPP
AYTEPTAPKL QEAVIPPAPQ LALSTVSSVE TPPVQYTPDV LILPTPPALD ENTPPSVMAS
TAKATKSAPP LVVVDDNTDK GTADGLVTQQ NGVTLPLGAI SGNAAPRRAR SGSSNQADQG
AQTILSSKQI DQLLIDRASV RPLSPPDSDK LNEMSNSPFA TPKARSRPVP QASNASLHKR
PGSAASQASS VQIHPPLPAD HKEAIMAAEK KSIDQRPASA GLMGPPLAPA SAVRASSQQR
PRTPNESALQ VGSAKTTTSR ASVRRDSHMS RRSSVSSFAS ELEERFNMQP NPPFAPQGYS
TGTDPRMIQA ITQTMIGEFL WKYTRRAVSG EISNTRHRRY FWVHPYTRTL YWSEHDPQSA
GKSEGRTKSV SIEAVRVVAD DNPYPPGLHC KSLEVVSPGR RIRFTATTSQ RHETWFNALS
YLLVRNGPED EEAENGVTLD DIDEFNPGFR SRSRQTARMS VSSSQSRGTR GLPKQRSGSA
MSLRPSVTPG RASPYPPSHY SDQARQASSS RLSTIFNSTI KGSFGRKGPY AASSLNEDSI
HNHDDSVEDL RHMMDRGDDV DRLENVRACC DGKHDVSSLS RTSRYSPRAN RIHSHH
