FAP1H_SCHPO
ID FAP1H_SCHPO Reviewed; 1077 AA.
AC O74853;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 25-MAY-2022, entry version 143.
DE RecName: Full=FKBP12-associated protein 1 homolog;
GN Name=fap1; ORFNames=SPCC18.03;
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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-33, AND IDENTIFICATION BY
RP MASS SPECTROMETRY.
RX PubMed=18257517; DOI=10.1021/pr7006335;
RA Wilson-Grady J.T., Villen J., Gygi S.P.;
RT "Phosphoproteome analysis of fission yeast.";
RL J. Proteome Res. 7:1088-1097(2008).
CC -!- FUNCTION: May play a role in transcription regulation. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16823372}. Golgi
CC apparatus {ECO:0000269|PubMed:16823372}. Nucleus {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the NFX1 family. {ECO:0000305}.
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DR EMBL; CU329672; CAA21417.1; -; Genomic_DNA.
DR PIR; T41146; T41146.
DR RefSeq; NP_588382.1; NM_001023373.2.
DR AlphaFoldDB; O74853; -.
DR SMR; O74853; -.
DR STRING; 4896.SPCC18.03.1; -.
DR iPTMnet; O74853; -.
DR MaxQB; O74853; -.
DR PaxDb; O74853; -.
DR PRIDE; O74853; -.
DR EnsemblFungi; SPCC18.03.1; SPCC18.03.1:pep; SPCC18.03.
DR GeneID; 2538928; -.
DR KEGG; spo:SPCC18.03; -.
DR PomBase; SPCC18.03; -.
DR VEuPathDB; FungiDB:SPCC18.03; -.
DR eggNOG; KOG1952; Eukaryota.
DR HOGENOM; CLU_005714_2_2_1; -.
DR InParanoid; O74853; -.
DR OMA; WCEKEVD; -.
DR PhylomeDB; O74853; -.
DR PRO; PR:O74853; -.
DR Proteomes; UP000002485; Chromosome III.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0005794; C:Golgi apparatus; HDA:PomBase.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central.
DR GO; GO:0000977; F:RNA polymerase II transcription regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR GO; GO:0008270; F:zinc ion binding; ISM:PomBase.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; ISS:PomBase.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IBA:GO_Central.
DR CDD; cd06006; R3H_unknown_2; 1.
DR Gene3D; 3.30.1370.50; -; 1.
DR InterPro; IPR034078; NFX1_fam.
DR InterPro; IPR001374; R3H_dom.
DR InterPro; IPR036867; R3H_dom_sf.
DR InterPro; IPR034077; R3H_FAP1.
DR InterPro; IPR019786; Zinc_finger_PHD-type_CS.
DR InterPro; IPR000967; Znf_NFX1.
DR InterPro; IPR019787; Znf_PHD-finger.
DR InterPro; IPR001841; Znf_RING.
DR PANTHER; PTHR12360; PTHR12360; 1.
DR Pfam; PF01424; R3H; 1.
DR Pfam; PF01422; zf-NF-X1; 8.
DR SMART; SM00393; R3H; 1.
DR SMART; SM00438; ZnF_NFX; 8.
DR SUPFAM; SSF82708; SSF82708; 1.
DR PROSITE; PS51061; R3H; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Golgi apparatus; Metal-binding; Nucleus; Phosphoprotein;
KW Reference proteome; Repeat; Transcription; Transcription regulation; Zinc;
KW Zinc-finger.
FT CHAIN 1..1077
FT /note="FKBP12-associated protein 1 homolog"
FT /id="PRO_0000317322"
FT DOMAIN 835..897
FT /note="R3H"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00382"
FT ZN_FING 197..247
FT /note="RING-type; atypical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT ZN_FING 290..308
FT /note="NF-X1-type 1"
FT ZN_FING 348..367
FT /note="NF-X1-type 2"
FT ZN_FING 420..441
FT /note="NF-X1-type 3"
FT ZN_FING 485..503
FT /note="NF-X1-type 4"
FT ZN_FING 541..558
FT /note="NF-X1-type 5"
FT ZN_FING 595..614
FT /note="NF-X1-type 6"
FT ZN_FING 708..729
FT /note="NF-X1-type 7"
FT ZN_FING 738..760
FT /note="NF-X1-type 8"
FT REGION 1..173
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 29..53
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 72..90
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 96..112
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 133..151
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 152..173
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 33
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
SQ SEQUENCE 1077 AA; 121088 MW; B96B3B8B871A10C0 CRC64;
METSKNPSDL PKKPANVKKN RRRFQKSQKK SISPSSGSEL PNFKTTISQN NEEVKTSLKE
DSSKFHPSAS APIFVPTSSV QLNVSKNNGH KASDIVDAVS SKDEELRKHA KGEGKRSKNR
KRSSKHSEKQ AVDLKSSNSS QETSSSKGSV NNKSERSREA KSRMPKNSKE IKKGLDLSKL
DMTSRMIVEL KNRLYECSVC TDTINPSTSI WSCGTCYHVF HLSCIRKWCK NSIEQRNEDA
WRCPYCQSNQ TETSLHYLCW CGKQEKPEFV KNLVPHSCGD PCGKTRGQDC EHPCPLLCHP
GPCPPCTATV EKFCLCGKES IHARCSNISK VNTEPFRCEN VCDELLPCGE HTCKKRCHSG
LCGACFEPIN AKCYCGLHSK TYPCSSLPSP SISKKDENGS VKEWFGYYSC NNPCTLFFDC
GLHKCSKTCH PISETRAHCP FATDVLTKCP CGKEDISFLL KGHERKSCSD PIPTCENICG
KLLSCGHRCK YKCHLGSCGT CSETLTIPCR CTANEVQVTC EQLQNGFIPT CERLCTILLS
CGRHQCNKKC CSGYSKAQTR LARRPKGAKL RYHLLTEEFE EEHICFRPCN KKLSCGNHFC
QHMCHRGPCP RCLEASFEEL PCTCGRTRLY PPVACGTPIP DCPYLCVLPK SCHHPQVKHN
CHPTSEPCPP CPYFVKKRCL CGKHILENQP CYRENVRCGE LCNKLLSCKT HFCEKLCHPD
GECESSCKKE CGKRRMYCEH VCQSPCHAGH PCDERIPCKA PLEVSCECGR IRKKVTCDAS
YDNPDPQHKV SCTLECSQQQ RNKLFAEALN IKTDRRSNDV AQYTKSLLVF YGKHSDFADE
VESLLRNFVN NKASSFRFPS MRREQRAFVH MFAKLLGLES VSFDPEPKRN VMVYNKGEAK
LPNMLLKEAN LYHLQHPEIP LKPDSLLGPE EENATASHID GSSNASDSGY NAFVLKELLK
EVNDESAIFS VLDDIVDFNH LTWSILFGEN YIILKPLNTD LIVNKTGKLV ALRPLVNRRL
ADAGIASRCE ICEINDKNEI VKTRSQRIHS KKKAFLSLVP DKSIGVINRY KELATEL
