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Adenylyl cyclase-associated protein 1 (CAP 1)

 CAP1_MOUSE              Reviewed;         474 AA.
P40124; Q8BPT7;
01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
27-JUL-2011, sequence version 4.
22-NOV-2017, entry version 147.
RecName: Full=Adenylyl cyclase-associated protein 1;
Short=CAP 1;
Name=Cap1; Synonyms=Cap;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=7691848;
Vojtek A.B., Cooper J.A.;
"Identification and characterization of a cDNA encoding mouse CAP: a
homolog of the yeast adenylyl cyclase associated protein.";
J. Cell Sci. 105:777-785(1993).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J; TISSUE=Eye;
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=C57BL/6J;
PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
Lindblad-Toh K., Eichler E.E., Ponting C.P.;
"Lineage-specific biology revealed by a finished genome assembly of
the mouse.";
PLoS Biol. 7:E1000112-E1000112(2009).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=Czech II; TISSUE=Mammary gland;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[5]
PROTEIN SEQUENCE OF 254-271, AND IDENTIFICATION BY MASS SPECTROMETRY.
STRAIN=OF1; TISSUE=Hippocampus;
Lubec G., Sunyer B., Chen W.-Q.;
Submitted (JAN-2009) to UniProtKB.
[6]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-31, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=15592455; DOI=10.1038/nbt1046;
Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H.,
Zha X.-M., Polakiewicz R.D., Comb M.J.;
"Immunoaffinity profiling of tyrosine phosphorylation in cancer
cells.";
Nat. Biotechnol. 23:94-101(2005).
[7]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung,
Pancreas, Spleen, and Testis;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
-!- FUNCTION: Directly regulates filament dynamics and has been
implicated in a number of complex developmental and morphological
processes, including mRNA localization and the establishment of
cell polarity. {ECO:0000250}.
-!- SUBUNIT: Homodimer. Binds actin monomers (By similarity).
{ECO:0000250}.
-!- INTERACTION:
Q99N72:Mcf2; NbExp=3; IntAct=EBI-641927, EBI-641874;
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Peripheral
membrane protein {ECO:0000250}.
-!- TISSUE SPECIFICITY: Ubiquitous.
-!- SIMILARITY: Belongs to the CAP family. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; L12367; AAC37610.1; -; mRNA.
EMBL; AK053351; BAC35357.1; -; mRNA.
EMBL; AL606906; CAM13994.1; -; Genomic_DNA.
EMBL; BX545849; CAM13994.1; JOINED; Genomic_DNA.
EMBL; BX545849; CAM18197.1; -; Genomic_DNA.
EMBL; AL606906; CAM18197.1; JOINED; Genomic_DNA.
EMBL; BC005446; AAH05446.1; -; mRNA.
EMBL; BC005472; AAH05472.1; -; mRNA.
CCDS; CCDS18604.1; -.
PIR; I49572; I49572.
RefSeq; NP_001287996.1; NM_001301067.1.
RefSeq; NP_031624.2; NM_007598.4.
RefSeq; XP_006502758.1; XM_006502695.1.
RefSeq; XP_006502760.1; XM_006502697.3.
UniGene; Mm.8687; -.
ProteinModelPortal; P40124; -.
SMR; P40124; -.
BioGrid; 198468; 1.
DIP; DIP-49641N; -.
IntAct; P40124; 8.
MINT; MINT-1591929; -.
STRING; 10090.ENSMUSP00000068260; -.
iPTMnet; P40124; -.
PhosphoSitePlus; P40124; -.
SwissPalm; P40124; -.
REPRODUCTION-2DPAGE; P40124; -.
EPD; P40124; -.
MaxQB; P40124; -.
PaxDb; P40124; -.
PeptideAtlas; P40124; -.
PRIDE; P40124; -.
Ensembl; ENSMUST00000069533; ENSMUSP00000068260; ENSMUSG00000028656.
Ensembl; ENSMUST00000106255; ENSMUSP00000101862; ENSMUSG00000028656.
Ensembl; ENSMUST00000106257; ENSMUSP00000101864; ENSMUSG00000028656.
GeneID; 12331; -.
KEGG; mmu:12331; -.
UCSC; uc008uok.3; mouse.
CTD; 10487; -.
MGI; MGI:88262; Cap1.
eggNOG; KOG2675; Eukaryota.
eggNOG; ENOG410XPXJ; LUCA.
GeneTree; ENSGT00390000017955; -.
HOGENOM; HOG000206192; -.
HOVERGEN; HBG003080; -.
InParanoid; P40124; -.
KO; K17261; -.
OMA; HCGYGDS; -.
OrthoDB; EOG091G0DLX; -.
TreeFam; TF313791; -.
Reactome; R-MMU-6798695; Neutrophil degranulation.
ChiTaRS; Cap1; mouse.
PRO; PR:P40124; -.
Proteomes; UP000000589; Chromosome 4.
Bgee; ENSMUSG00000028656; -.
ExpressionAtlas; P40124; baseline and differential.
Genevisible; P40124; MM.
GO; GO:0030864; C:cortical actin cytoskeleton; IDA:MGI.
GO; GO:0005737; C:cytoplasm; IDA:MGI.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0070062; C:extracellular exosome; ISO:MGI.
GO; GO:0005576; C:extracellular region; TAS:Reactome.
GO; GO:0005615; C:extracellular space; IDA:BHF-UCL.
GO; GO:0005925; C:focal adhesion; ISO:MGI.
GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
GO; GO:0003779; F:actin binding; IBA:GO_Central.
GO; GO:0008179; F:adenylate cyclase binding; IBA:GO_Central.
GO; GO:0030036; P:actin cytoskeleton organization; IMP:MGI.
GO; GO:0008154; P:actin polymerization or depolymerization; IBA:GO_Central.
GO; GO:0001667; P:ameboidal-type cell migration; IMP:MGI.
GO; GO:0000902; P:cell morphogenesis; IGI:MGI.
GO; GO:0007163; P:establishment or maintenance of cell polarity; IBA:GO_Central.
GO; GO:0002576; P:platelet degranulation; TAS:Reactome.
GO; GO:0006898; P:receptor-mediated endocytosis; IMP:MGI.
GO; GO:0045761; P:regulation of adenylate cyclase activity; IBA:GO_Central.
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; IPR028415; CAP1.
InterPro; IPR036223; CAP_C_sf.
InterPro; IPR028417; CAP_CS_C.
InterPro; IPR018106; CAP_CS_N.
InterPro; IPR036222; CAP_N_sf.
InterPro; IPR006599; CARP_motif.
PANTHER; PTHR10652; PTHR10652; 1.
PANTHER; PTHR10652:SF1; PTHR10652:SF1; 1.
Pfam; PF08603; CAP_C; 1.
Pfam; PF01213; CAP_N; 1.
SMART; SM00673; CARP; 2.
SUPFAM; SSF101278; SSF101278; 1.
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;
Acetylation; Actin-binding; Cell membrane; Complete proteome;
Direct protein sequencing; Isopeptide bond; Membrane; Methylation;
Phosphoprotein; Reference proteome; Ubl conjugation.
INIT_MET 1 1 Removed. {ECO:0000250|UniProtKB:Q01518}.
CHAIN 2 474 Adenylyl cyclase-associated protein 1.
/FTId=PRO_0000205697.
DOMAIN 312 452 C-CAP/cofactor C-like.
{ECO:0000255|PROSITE-ProRule:PRU00659}.
COMPBIAS 217 255 Ala/Pro/Ser-rich.
COMPBIAS 229 240 Poly-Pro.
MOD_RES 2 2 N-acetylalanine.
{ECO:0000250|UniProtKB:Q01518}.
MOD_RES 31 31 Phosphotyrosine.
{ECO:0000244|PubMed:15592455}.
MOD_RES 34 34 Phosphoserine.
{ECO:0000250|UniProtKB:Q01518}.
MOD_RES 80 80 N6-acetyllysine.
{ECO:0000250|UniProtKB:Q01518}.
MOD_RES 286 286 N6-methyllysine.
{ECO:0000250|UniProtKB:Q01518}.
MOD_RES 289 289 Phosphoserine.
{ECO:0000250|UniProtKB:Q01518}.
MOD_RES 294 294 Phosphoserine.
{ECO:0000250|UniProtKB:Q01518}.
MOD_RES 300 300 Phosphoserine.
{ECO:0000250|UniProtKB:Q01518}.
MOD_RES 306 306 Phosphothreonine.
{ECO:0000250|UniProtKB:Q01518}.
MOD_RES 307 307 Phosphoserine.
{ECO:0000250|UniProtKB:Q01518}.
MOD_RES 309 309 Phosphoserine.
{ECO:0000250|UniProtKB:Q01518}.
CROSSLNK 347 347 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO1).
{ECO:0000250|UniProtKB:Q01518}.
CONFLICT 242 242 S -> P (in Ref. 1; AAC37610 and 4;
AAH05446/AAH05472). {ECO:0000305}.
SEQUENCE 474 AA; 51565 MW; 076863277E7AF2F5 CRC64;
MADMQNLVER LERAVGRLEA VSHTSDMHCG YGDSPSKGAV PYVQAFDSLL ANPVAEYLKM
SKEIGGDVQK HAEMVHTGLK LERALLATAS QCQQPAGNKL SDLLAPISEQ IQEVITFREK
NRGSKFFNHL SAVSESIQAL GWVALAAKPG PFVKEMNDAA MFYTNRVLKE YRDVDKKHVD
WVRAYLSIWT ELQAYIKEFH TTGLAWSKTG PVAKELSGLP SGPSVGSGPP PPPPGPPPPP
ISTSSGSDDS ASRSALFAQI NQGESITHAL KHVSDDMKTH KNPALKAQSG PVRSGPKPFS
APKPQTSPSP KPATKKEPAL LELEGKKWRV ENQENVSNLV IDDTELKQVA YIYKCVNTTL
QIKGKINSIT VDNCKKLGLV FDDVVGIVEI INSRDVKVQV MGKVPTISIN KTDGCHAYLS
KNSLDCEIVS AKSSEMNVLI PTEGGDFNEF PVPEQFKTLW NGQKLVTTVT EIAG


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