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Adenylyl cyclase-associated protein (CAP)

 CAP_SCHPO               Reviewed;         551 AA.
P36621;
01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
01-JUN-1994, sequence version 1.
22-NOV-2017, entry version 124.
RecName: Full=Adenylyl cyclase-associated protein;
Short=CAP;
Name=cap1; Synonyms=cap; ORFNames=SPCC306.09c;
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
Schizosaccharomycetes; Schizosaccharomycetales;
Schizosaccharomycetaceae; Schizosaccharomyces.
NCBI_TaxID=284812;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=MK141;
PubMed=1550959; DOI=10.1091/mbc.3.2.167;
Kawamukai M., Gerst J., Field J., Riggs M., Rodgers L., Wigler M.,
Young D.;
"Genetic and biochemical analysis of the adenylyl cyclase-associated
protein, cap, in Schizosaccharomyces pombe.";
Mol. Biol. Cell 3:167-180(1992).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=972 / ATCC 24843;
PubMed=11859360; DOI=10.1038/nature724;
Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M.,
Collins M., Connor R., Cronin A., Davis P., Feltwell T., Fraser A.,
Gentles S., Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G.,
Holroyd S., Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K.,
James K.D., Jones L., Jones M., Leather S., McDonald S., McLean J.,
Mooney P., Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C.,
Oliver K., O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E.,
Rutherford K.M., Rutter S., Saunders D., Seeger K., Sharp S.,
Skelton J., Simmonds M.N., Squares R., Squares S., Stevens K.,
Taylor K., Taylor R.G., Tivey A., Walsh S.V., Warren T., Whitehead S.,
Woodward J.R., Volckaert G., Aert R., Robben J., Grymonprez B.,
Weltjens I., Vanstreels E., Rieger M., Schaefer M., Mueller-Auer S.,
Gabel C., Fuchs M., Duesterhoeft A., Fritzc C., Holzer E., Moestl D.,
Hilbert H., Borzym K., Langer I., Beck A., Lehrach H., Reinhardt R.,
Pohl T.M., Eger P., Zimmermann W., Wedler H., Wambutt R., Purnelle B.,
Goffeau A., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S.,
Galibert F., Aves S.J., Xiang Z., Hunt C., Moore K., Hurst S.M.,
Lucas M., Rochet M., Gaillardin C., Tallada V.A., Garzon A., Thode G.,
Daga R.R., Cruzado L., Jimenez J., Sanchez M., del Rey F., Benito J.,
Dominguez A., Revuelta J.L., Moreno S., Armstrong J., Forsburg S.L.,
Cerutti L., Lowe T., McCombie W.R., Paulsen I., Potashkin J.,
Shpakovski G.V., Ussery D., Barrell B.G., Nurse P.;
"The genome sequence of Schizosaccharomyces pombe.";
Nature 415:871-880(2002).
[3]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-92 AND THR-96, AND
IDENTIFICATION BY MASS SPECTROMETRY.
PubMed=18257517; DOI=10.1021/pr7006335;
Wilson-Grady J.T., Villen J., Gygi S.P.;
"Phosphoproteome analysis of fission yeast.";
J. Proteome Res. 7:1088-1097(2008).
-!- FUNCTION: The N-terminal domain binds to adenylyl cyclase, thereby
enabling adenylyl cyclase to be activated by upstream regulatory
signals, such as Ras. The C-terminal domain is required for normal
cellular morphology and growth control.
-!- SIMILARITY: Belongs to the CAP family. {ECO:0000305}.
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EMBL; L16577; AAA35292.1; -; mRNA.
EMBL; CU329672; CAB41657.1; -; Genomic_DNA.
PIR; A60047; A60047.
RefSeq; NP_587817.1; NM_001022810.2.
ProteinModelPortal; P36621; -.
SMR; P36621; -.
BioGrid; 275410; 9.
MINT; MINT-4689131; -.
STRING; 4896.SPCC306.09c.1; -.
iPTMnet; P36621; -.
MaxQB; P36621; -.
PRIDE; P36621; -.
EnsemblFungi; SPCC306.09c.1; SPCC306.09c.1:pep; SPCC306.09c.
GeneID; 2538829; -.
KEGG; spo:SPCC306.09c; -.
EuPathDB; FungiDB:SPCC306.09c; -.
PomBase; SPCC306.09c; cap1.
HOGENOM; HOG000206192; -.
InParanoid; P36621; -.
KO; K17261; -.
OMA; HCGYGDS; -.
OrthoDB; EOG092C2MM2; -.
PhylomeDB; P36621; -.
Reactome; R-SPO-6798695; Neutrophil degranulation.
PRO; PR:P36621; -.
Proteomes; UP000002485; Chromosome III.
GO; GO:0030864; C:cortical actin cytoskeleton; IBA:GO_Central.
GO; GO:0005737; C:cytoplasm; IDA:PomBase.
GO; GO:0000935; C:division septum; IDA:PomBase.
GO; GO:0035838; C:growing cell tip; IDA:PomBase.
GO; GO:0003779; F:actin binding; IBA:GO_Central.
GO; GO:0008179; F:adenylate cyclase binding; IBA:GO_Central.
GO; GO:0008154; P:actin polymerization or depolymerization; IBA:GO_Central.
GO; GO:0000902; P:cell morphogenesis; IBA:GO_Central.
GO; GO:0007163; P:establishment or maintenance of cell polarity; IBA:GO_Central.
GO; GO:0031138; P:negative regulation of conjugation with cellular fusion; IMP:PomBase.
GO; GO:0045761; P:regulation of adenylate cyclase activity; IGI:PomBase.
GO; GO:0007165; P:signal transduction; IBA:GO_Central.
InterPro; IPR001837; Adenylate_cyclase-assoc_CAP.
InterPro; IPR013912; Adenylate_cyclase-assoc_CAP_C.
InterPro; IPR013992; Adenylate_cyclase-assoc_CAP_N.
InterPro; IPR017901; C-CAP_CF_C-like.
InterPro; IPR036223; CAP_C_sf.
InterPro; IPR028417; CAP_CS_C.
InterPro; IPR018106; CAP_CS_N.
InterPro; IPR028419; CAP_fungal_type.
InterPro; IPR036222; CAP_N_sf.
InterPro; IPR006599; CARP_motif.
PANTHER; PTHR10652; PTHR10652; 1.
PANTHER; PTHR10652:SF0; PTHR10652:SF0; 1.
Pfam; PF08603; CAP_C; 1.
Pfam; PF01213; CAP_N; 1.
SMART; SM00673; CARP; 2.
SUPFAM; SSF101278; SSF101278; 2.
SUPFAM; SSF69340; SSF69340; 1.
PROSITE; PS51329; C_CAP_COFACTOR_C; 1.
PROSITE; PS01088; CAP_1; 1.
PROSITE; PS01089; CAP_2; 1.
1: Evidence at protein level;
Complete proteome; Phosphoprotein; Reference proteome.
CHAIN 1 551 Adenylyl cyclase-associated protein.
/FTId=PRO_0000205705.
DOMAIN 395 529 C-CAP/cofactor C-like.
{ECO:0000255|PROSITE-ProRule:PRU00659}.
COMPBIAS 288 315 Ala/Pro/Ser-rich.
COMPBIAS 306 314 Poly-Pro.
MOD_RES 92 92 Phosphoserine.
{ECO:0000269|PubMed:18257517}.
MOD_RES 96 96 Phosphothreonine.
{ECO:0000269|PubMed:18257517}.
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


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