CAP1_MOUSE
ID CAP1_MOUSE Reviewed; 474 AA.
AC P40124; Q8BPT7;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 4.
DT 03-AUG-2022, entry version 173.
DE RecName: Full=Adenylyl cyclase-associated protein 1;
DE Short=CAP 1;
GN Name=Cap1; Synonyms=Cap;
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 [MRNA].
RX PubMed=7691848; DOI=10.1242/jcs.105.3.777;
RA Vojtek A.B., Cooper J.A.;
RT "Identification and characterization of a cDNA encoding mouse CAP: a
RT homolog of the yeast adenylyl cyclase associated protein.";
RL J. Cell Sci. 105:777-785(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Eye;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Czech II; TISSUE=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 [5]
RP PROTEIN SEQUENCE OF 254-271, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=OF1; TISSUE=Hippocampus;
RA Lubec G., Sunyer B., Chen W.-Q.;
RL Submitted (JAN-2009) to UniProtKB.
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-31, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=15592455; DOI=10.1038/nbt1046;
RA Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H.,
RA Zha X.-M., Polakiewicz R.D., Comb M.J.;
RT "Immunoaffinity profiling of tyrosine phosphorylation in cancer cells.";
RL Nat. Biotechnol. 23:94-101(2005).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, 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: Directly regulates filament dynamics and has been implicated
CC in a number of complex developmental and morphological processes,
CC including mRNA localization and the establishment of cell polarity.
CC {ECO:0000250}.
CC -!- SUBUNIT: Homodimer. Binds actin monomers (By similarity).
CC {ECO:0000250}.
CC -!- INTERACTION:
CC P40124; Q99N72: Mcf2; NbExp=3; IntAct=EBI-641927, EBI-641874;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Peripheral membrane
CC protein {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Ubiquitous.
CC -!- SIMILARITY: Belongs to the CAP family. {ECO:0000305}.
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DR EMBL; L12367; AAC37610.1; -; mRNA.
DR EMBL; AK053351; BAC35357.1; -; mRNA.
DR EMBL; AL606906; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BX545849; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC005446; AAH05446.1; -; mRNA.
DR EMBL; BC005472; AAH05472.1; -; mRNA.
DR CCDS; CCDS18604.1; -.
DR PIR; I49572; I49572.
DR RefSeq; NP_001287996.1; NM_001301067.1.
DR RefSeq; NP_031624.2; NM_007598.4.
DR RefSeq; XP_006502758.1; XM_006502695.1.
DR RefSeq; XP_006502760.1; XM_006502697.3.
DR PDB; 6FM2; X-ray; 2.80 A; B=317-474.
DR PDB; 6RSQ; X-ray; 2.37 A; A/B/C/D=41-216.
DR PDB; 6RSW; X-ray; 1.95 A; C=39-210.
DR PDBsum; 6FM2; -.
DR PDBsum; 6RSQ; -.
DR PDBsum; 6RSW; -.
DR AlphaFoldDB; P40124; -.
DR SMR; P40124; -.
DR BioGRID; 198468; 28.
DR DIP; DIP-49641N; -.
DR IntAct; P40124; 7.
DR MINT; P40124; -.
DR STRING; 10090.ENSMUSP00000101862; -.
DR iPTMnet; P40124; -.
DR PhosphoSitePlus; P40124; -.
DR SwissPalm; P40124; -.
DR REPRODUCTION-2DPAGE; P40124; -.
DR CPTAC; non-CPTAC-3773; -.
DR EPD; P40124; -.
DR jPOST; P40124; -.
DR MaxQB; P40124; -.
DR PaxDb; P40124; -.
DR PeptideAtlas; P40124; -.
DR PRIDE; P40124; -.
DR ProteomicsDB; 281770; -.
DR Antibodypedia; 32000; 216 antibodies from 30 providers.
DR DNASU; 12331; -.
DR Ensembl; ENSMUST00000069533; ENSMUSP00000068260; ENSMUSG00000028656.
DR Ensembl; ENSMUST00000106255; ENSMUSP00000101862; ENSMUSG00000028656.
DR Ensembl; ENSMUST00000106257; ENSMUSP00000101864; ENSMUSG00000028656.
DR GeneID; 12331; -.
DR KEGG; mmu:12331; -.
DR UCSC; uc008uok.3; mouse.
DR CTD; 10487; -.
DR MGI; MGI:88262; Cap1.
DR VEuPathDB; HostDB:ENSMUSG00000028656; -.
DR eggNOG; KOG2675; Eukaryota.
DR GeneTree; ENSGT00390000017955; -.
DR HOGENOM; CLU_015780_1_1_1; -.
DR InParanoid; P40124; -.
DR OMA; LDGNKWI; -.
DR OrthoDB; 1098760at2759; -.
DR PhylomeDB; P40124; -.
DR TreeFam; TF313791; -.
DR Reactome; R-MMU-6798695; Neutrophil degranulation.
DR BioGRID-ORCS; 12331; 20 hits in 75 CRISPR screens.
DR ChiTaRS; Cap1; mouse.
DR PRO; PR:P40124; -.
DR Proteomes; UP000000589; Chromosome 4.
DR RNAct; P40124; protein.
DR Bgee; ENSMUSG00000028656; Expressed in granulocyte and 244 other tissues.
DR ExpressionAtlas; P40124; baseline and differential.
DR Genevisible; P40124; MM.
DR GO; GO:0030864; C:cortical actin cytoskeleton; IDA:MGI.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0003779; F:actin binding; IBA:GO_Central.
DR GO; GO:0008179; F:adenylate cyclase binding; IBA:GO_Central.
DR GO; GO:0030036; P:actin cytoskeleton organization; IMP:MGI.
DR GO; GO:0001667; P:ameboidal-type cell migration; IMP:MGI.
DR GO; GO:0019933; P:cAMP-mediated signaling; IBA:GO_Central.
DR GO; GO:0000902; P:cell morphogenesis; IGI:MGI.
DR GO; GO:0006898; P:receptor-mediated endocytosis; IMP:MGI.
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; IPR028415; CAP1.
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:SF1; PTHR10652:SF1; 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 3D-structure; Acetylation; Actin-binding; Cell membrane;
KW Direct protein sequencing; Isopeptide bond; Membrane; Methylation;
KW Phosphoprotein; Reference proteome; Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q01518"
FT CHAIN 2..474
FT /note="Adenylyl cyclase-associated protein 1"
FT /id="PRO_0000205697"
FT DOMAIN 312..452
FT /note="C-CAP/cofactor C-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00659"
FT REGION 215..253
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 277..316
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 224..243
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 297..311
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:Q01518"
FT MOD_RES 31
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:15592455"
FT MOD_RES 34
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q01518"
FT MOD_RES 80
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q01518"
FT MOD_RES 286
FT /note="N6-methyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q01518"
FT MOD_RES 289
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q01518"
FT MOD_RES 294
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q01518"
FT MOD_RES 300
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q01518"
FT MOD_RES 306
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q01518"
FT MOD_RES 307
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q01518"
FT MOD_RES 309
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q01518"
FT CROSSLNK 347
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1)"
FT /evidence="ECO:0000250|UniProtKB:Q01518"
FT CONFLICT 242
FT /note="S -> P (in Ref. 1; AAC37610 and 4; AAH05446/
FT AAH05472)"
FT /evidence="ECO:0000305"
FT HELIX 41..51
FT /evidence="ECO:0007829|PDB:6RSW"
FT HELIX 53..64
FT /evidence="ECO:0007829|PDB:6RSW"
FT HELIX 66..90
FT /evidence="ECO:0007829|PDB:6RSW"
FT HELIX 97..119
FT /evidence="ECO:0007829|PDB:6RSW"
FT HELIX 127..134
FT /evidence="ECO:0007829|PDB:6RSW"
FT HELIX 137..144
FT /evidence="ECO:0007829|PDB:6RSW"
FT HELIX 149..171
FT /evidence="ECO:0007829|PDB:6RSW"
FT TURN 172..174
FT /evidence="ECO:0007829|PDB:6RSW"
FT HELIX 176..199
FT /evidence="ECO:0007829|PDB:6RSW"
FT STRAND 320..324
FT /evidence="ECO:0007829|PDB:6FM2"
FT STRAND 327..332
FT /evidence="ECO:0007829|PDB:6FM2"
FT STRAND 339..341
FT /evidence="ECO:0007829|PDB:6FM2"
FT STRAND 349..354
FT /evidence="ECO:0007829|PDB:6FM2"
FT STRAND 359..367
FT /evidence="ECO:0007829|PDB:6FM2"
FT STRAND 369..373
FT /evidence="ECO:0007829|PDB:6FM2"
FT STRAND 378..392
FT /evidence="ECO:0007829|PDB:6FM2"
FT STRAND 394..402
FT /evidence="ECO:0007829|PDB:6FM2"
FT STRAND 405..411
FT /evidence="ECO:0007829|PDB:6FM2"
FT STRAND 413..418
FT /evidence="ECO:0007829|PDB:6FM2"
FT HELIX 423..425
FT /evidence="ECO:0007829|PDB:6FM2"
FT STRAND 427..432
FT /evidence="ECO:0007829|PDB:6FM2"
FT STRAND 434..441
FT /evidence="ECO:0007829|PDB:6FM2"
FT STRAND 445..451
FT /evidence="ECO:0007829|PDB:6FM2"
FT STRAND 456..460
FT /evidence="ECO:0007829|PDB:6FM2"
FT STRAND 462..469
FT /evidence="ECO:0007829|PDB:6FM2"
SQ 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
