CAP_SCHPO
ID CAP_SCHPO Reviewed; 551 AA.
AC P36621;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1994, sequence version 1.
DT 03-AUG-2022, entry version 146.
DE RecName: Full=Adenylyl cyclase-associated protein;
DE Short=CAP;
GN Name=cap1; Synonyms=cap; ORFNames=SPCC306.09c;
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 [MRNA].
RC STRAIN=MK141;
RX PubMed=1550959; DOI=10.1091/mbc.3.2.167;
RA Kawamukai M., Gerst J., Field J., Riggs M., Rodgers L., Wigler M.,
RA Young D.;
RT "Genetic and biochemical analysis of the adenylyl cyclase-associated
RT protein, cap, in Schizosaccharomyces pombe.";
RL Mol. Biol. Cell 3:167-180(1992).
RN [2]
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 [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-92 AND THR-96, AND
RP IDENTIFICATION BY 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: The N-terminal domain binds to adenylyl cyclase, thereby
CC enabling adenylyl cyclase to be activated by upstream regulatory
CC signals, such as Ras. The C-terminal domain is required for normal
CC cellular morphology and growth control.
CC -!- SIMILARITY: Belongs to the CAP family. {ECO:0000305}.
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DR EMBL; L16577; AAA35292.1; -; mRNA.
DR EMBL; CU329672; CAB41657.1; -; Genomic_DNA.
DR PIR; A60047; A60047.
DR RefSeq; NP_587817.1; NM_001022810.2.
DR AlphaFoldDB; P36621; -.
DR SMR; P36621; -.
DR BioGRID; 275410; 11.
DR STRING; 4896.SPCC306.09c.1; -.
DR iPTMnet; P36621; -.
DR MaxQB; P36621; -.
DR PaxDb; P36621; -.
DR PRIDE; P36621; -.
DR EnsemblFungi; SPCC306.09c.1; SPCC306.09c.1:pep; SPCC306.09c.
DR GeneID; 2538829; -.
DR KEGG; spo:SPCC306.09c; -.
DR PomBase; SPCC306.09c; cap1.
DR VEuPathDB; FungiDB:SPCC306.09c; -.
DR eggNOG; KOG2675; Eukaryota.
DR HOGENOM; CLU_015780_1_0_1; -.
DR InParanoid; P36621; -.
DR OMA; LDGNKWI; -.
DR PhylomeDB; P36621; -.
DR Reactome; R-SPO-6798695; Neutrophil degranulation.
DR PRO; PR:P36621; -.
DR Proteomes; UP000002485; Chromosome III.
DR GO; GO:0030428; C:cell septum; IDA:CACAO.
DR GO; GO:0005737; C:cytoplasm; HDA:PomBase.
DR GO; GO:0000935; C:division septum; IDA:PomBase.
DR GO; GO:0035838; C:growing cell tip; IDA:PomBase.
DR GO; GO:0003779; F:actin binding; IBA:GO_Central.
DR GO; GO:0008179; F:adenylate cyclase binding; IBA:GO_Central.
DR GO; GO:0007015; P:actin filament organization; IMP:CACAO.
DR GO; GO:0010619; P:adenylate cyclase-activating glucose-activated G protein-coupled receptor signaling pathway; IMP:PomBase.
DR GO; GO:0019933; P:cAMP-mediated signaling; IBA:GO_Central.
DR GO; GO:0030308; P:negative regulation of cell growth; IGI:CACAO.
DR GO; GO:0031138; P:negative regulation of conjugation with cellular fusion; IMP:PomBase.
DR GO; GO:0045761; P:regulation of adenylate cyclase activity; IBA:GO_Central.
DR Gene3D; 1.25.40.330; -; 1.
DR Gene3D; 2.160.20.70; -; 1.
DR InterPro; IPR001837; Adenylate_cyclase-assoc_CAP.
DR InterPro; IPR013912; Adenylate_cyclase-assoc_CAP_C.
DR InterPro; IPR013992; Adenylate_cyclase-assoc_CAP_N.
DR InterPro; IPR017901; C-CAP_CF_C-like.
DR InterPro; IPR016098; CAP/MinC_C.
DR InterPro; IPR036223; CAP_C_sf.
DR InterPro; IPR028417; CAP_CS_C.
DR InterPro; IPR018106; CAP_CS_N.
DR InterPro; IPR028419; CAP_fungal_type.
DR InterPro; IPR036222; CAP_N_sf.
DR InterPro; IPR006599; CARP_motif.
DR PANTHER; PTHR10652; PTHR10652; 1.
DR PANTHER; PTHR10652:SF0; PTHR10652:SF0; 1.
DR Pfam; PF08603; CAP_C; 1.
DR Pfam; PF01213; CAP_N; 1.
DR SMART; SM00673; CARP; 2.
DR SUPFAM; SSF101278; SSF101278; 1.
DR SUPFAM; SSF69340; SSF69340; 1.
DR PROSITE; PS51329; C_CAP_COFACTOR_C; 1.
DR PROSITE; PS01088; CAP_1; 1.
DR PROSITE; PS01089; CAP_2; 1.
PE 1: Evidence at protein level;
KW Phosphoprotein; Reference proteome.
FT CHAIN 1..551
FT /note="Adenylyl cyclase-associated protein"
FT /id="PRO_0000205705"
FT DOMAIN 395..529
FT /note="C-CAP/cofactor C-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00659"
FT REGION 34..55
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 288..333
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 348..395
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 302..318
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 349..363
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 92
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 96
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:18257517"
SQ SEQUENCE 551 AA; 60243 MW; 2D7E82A953B1339E CRC64;
MSDMINIRET GYNFTTILKR LEAATSRLED LVESGHKPLP NMHRPSRDSN SQTHNISFNI
GTPTAPTVST GSPAVASLHD QVAAAISPRN RSLTSTSAVE AVPASISAYD EFCSKYLSKY
MELSKKIGGL IAEQSEHVEK AFNLLRQVLS VALKAQKPDM DSPELLEFLK PIQSELLTIT
NIRDEHRTAP EFNQLSTVMS GISILGWVTV EPTPLSFMSE MKDSSQFYAN RVMKEFKGKD
DLQIEWVRSY LTLLTELITY VKTHFKTGLT WSTKQDAVPL KTALANLSAS KTQAPSSGDS
ANGGLPPPPP PPPPSNDFWK DSNEPAPADN KGDMGAVFAE INKGEGITSG LRKVDKSEMT
HKNPNLRKTG PTPGPKPKIK SSAPSKPAET APVKPPRIEL ENTKWFVENQ VDNHSIVLDS
VELNHSVQIF GCSNCTIIIK GKLNTVSMSN CKRTSVVVDT LVAAFDIAKC SNFGCQVMNH
VPMIVIDQCD GGSIYLSKSS LSSEVVTSKS TSLNINVPNE EGDYAERAVP EQIKHKVNEK
GELVSEIVRH E
