ID   CAP2_MOUSE              Reviewed;         476 AA.
AC   Q9CYT6; Q80YU7; Q9D6L0;
DT   03-JUL-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   03-AUG-2022, entry version 148.
DE   RecName: Full=Adenylyl cyclase-associated protein 2;
DE            Short=CAP 2;
GN   Name=Cap2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Embryo, and Tongue;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA   Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA   Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA   Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA   Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA   Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA   Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA   Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA   Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA   Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA   Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA   Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA   Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA   Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA   Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA   Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA   Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA   Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA   Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA   Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA   van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA   Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA   Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA   Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA   Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA   Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA   Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA   Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA   Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=NMRI; TISSUE=Brain, and Mammary gland;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain cortex;
RX   PubMed=17114649; DOI=10.1074/mcp.m600046-mcp200;
RA   Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,
RA   Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D., Gerrits B.,
RA   Panse C., Schlapbach R., Mansuy I.M.;
RT   "Qualitative and quantitative analyses of protein phosphorylation in naive
RT   and stimulated mouse synaptosomal preparations.";
RL   Mol. Cell. Proteomics 6:283-293(2007).
RN   [4]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain, Heart, and Testis;
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL   Cell 143:1174-1189(2010).
CC   -!- FUNCTION: May have a regulatory bifunctional role.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Peripheral membrane
CC       protein {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the CAP family. {ECO:0000305}.
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DR   EMBL; AK010235; BAB26786.1; -; mRNA.
DR   EMBL; AK013331; BAB28795.1; -; mRNA.
DR   EMBL; AK033071; BAC28143.1; -; mRNA.
DR   EMBL; AK035556; BAC29104.1; -; mRNA.
DR   EMBL; BC050752; AAH50752.2; -; mRNA.
DR   EMBL; BC057937; AAH57937.1; -; mRNA.
DR   CCDS; CCDS26484.1; -.
DR   RefSeq; NP_080332.1; NM_026056.4.
DR   AlphaFoldDB; Q9CYT6; -.
DR   SMR; Q9CYT6; -.
DR   BioGRID; 212048; 10.
DR   IntAct; Q9CYT6; 2.
DR   MINT; Q9CYT6; -.
DR   STRING; 10090.ENSMUSP00000021802; -.
DR   iPTMnet; Q9CYT6; -.
DR   PhosphoSitePlus; Q9CYT6; -.
DR   SwissPalm; Q9CYT6; -.
DR   jPOST; Q9CYT6; -.
DR   MaxQB; Q9CYT6; -.
DR   PaxDb; Q9CYT6; -.
DR   PeptideAtlas; Q9CYT6; -.
DR   PRIDE; Q9CYT6; -.
DR   ProteomicsDB; 265330; -.
DR   Antibodypedia; 25070; 210 antibodies from 25 providers.
DR   DNASU; 67252; -.
DR   Ensembl; ENSMUST00000021802; ENSMUSP00000021802; ENSMUSG00000021373.
DR   GeneID; 67252; -.
DR   KEGG; mmu:67252; -.
DR   UCSC; uc007qhf.2; mouse.
DR   CTD; 10486; -.
DR   MGI; MGI:1914502; Cap2.
DR   VEuPathDB; HostDB:ENSMUSG00000021373; -.
DR   eggNOG; KOG2675; Eukaryota.
DR   GeneTree; ENSGT00390000017955; -.
DR   HOGENOM; CLU_015780_1_1_1; -.
DR   InParanoid; Q9CYT6; -.
DR   OMA; QQNHAPV; -.
DR   OrthoDB; 1098760at2759; -.
DR   PhylomeDB; Q9CYT6; -.
DR   TreeFam; TF313791; -.
DR   BRENDA; 2.1.1.296; 3474.
DR   BioGRID-ORCS; 67252; 3 hits in 76 CRISPR screens.
DR   ChiTaRS; Cap2; mouse.
DR   PRO; PR:Q9CYT6; -.
DR   Proteomes; UP000000589; Chromosome 13.
DR   RNAct; Q9CYT6; protein.
DR   Bgee; ENSMUSG00000021373; Expressed in hindlimb stylopod muscle and 226 other tissues.
DR   ExpressionAtlas; Q9CYT6; baseline and differential.
DR   Genevisible; Q9CYT6; MM.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0014069; C:postsynaptic density; IDA:MGI.
DR   GO; GO:0003779; F:actin binding; IBA:GO_Central.
DR   GO; GO:0008179; F:adenylate cyclase binding; IBA:GO_Central.
DR   GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR   GO; GO:0019933; P:cAMP-mediated signaling; IBA:GO_Central.
DR   GO; GO:0000902; P:cell morphogenesis; IBA:GO_Central.
DR   GO; GO:0007010; P:cytoskeleton organization; IEA:InterPro.
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; IPR028418; CAP2.
DR   InterPro; IPR036223; CAP_C_sf.
DR   InterPro; IPR028417; CAP_CS_C.
DR   InterPro; IPR018106; CAP_CS_N.
DR   InterPro; IPR036222; CAP_N_sf.
DR   InterPro; IPR006599; CARP_motif.
DR   PANTHER; PTHR10652; PTHR10652; 1.
DR   PANTHER; PTHR10652:SF2; PTHR10652:SF2; 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   Cell membrane; Membrane; Phosphoprotein; Reference proteome.
FT   CHAIN           1..476
FT                   /note="Adenylyl cyclase-associated protein 2"
FT                   /id="PRO_0000205701"
FT   DOMAIN          317..454
FT                   /note="C-CAP/cofactor C-like"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00659"
FT   REGION          223..322
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        228..246
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        290..321
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         300
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P52481"
FT   MOD_RES         308
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P40123"
FT   CONFLICT        132
FT                   /note="H -> D (in Ref. 1; BAB26786)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   476 AA;  52862 MW;  318F0E48768FDD1F CRC64;
     MTDMAGLMER LERAVIRLEQ LSAGLDGPPR GCGEVNGVNG GVAPSVEAFD KLINSMVAEF
     LKNSRVLAGD VETHAEMVHG AFQAQRAFLL MVSQYQQPQE NEVAVLLKPI SEKIQEIQTF
     RERNRGSNMF NHLSAVSESI AALGWIAVSP KPGPYVKEMN DAATFYTNRV LKDYKHSDLR
     HVDWVRSYLN IWSELQAYIR EHHTTGLTWS KTGPVASTAS AFSILSSGPG LPPPPPPPPP
     PGPPPPFENE DKKEEPSPSR SALFAQLNQG EAITKGLRHV TDDKKTYKNP SLRAQGQIRS
     PTKTHTPSPT SPKSNSPQKH TPVLELEGKK WRVEYQEDRN DLVISETELK QVAYIFKCDK
     STLQIKGKVN SITVDNCKKF GLVFDHVVGI VEVINSKDIQ IQVMGRVPTI SINKTEGCHL
     YLSEDALDCE IVSAKSSEMN VLVPQDDDYR EFPIPEQFKT IWDGSKLVTE PAEIMA