CAP2_RAT
ID CAP2_RAT Reviewed; 477 AA.
AC P52481;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 131.
DE RecName: Full=Adenylyl cyclase-associated protein 2;
DE Short=CAP 2;
GN Name=Cap2;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=8522189; DOI=10.1016/0378-1119(95)00522-8;
RA Swiston J., Hubberstey A., Yu G., Young D.;
RT "Differential expression of CAP and CAP2 in adult rat tissues.";
RL Gene 165:273-277(1995).
RN [2]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-301, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
CC -!- FUNCTION: May have a regulatory bifunctional role.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Peripheral membrane
CC protein {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Found at relatively high levels in testes, at
CC moderate levels in brain, heart and skeletal muscle, at lower levels in
CC lung, skin, kidney and small intestine, and is undetectable in liver or
CC spleen.
CC -!- SIMILARITY: Belongs to the CAP family. {ECO:0000305}.
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DR EMBL; U31935; AAA92298.1; -; mRNA.
DR PIR; JC4386; JC4386.
DR RefSeq; NP_446326.1; NM_053874.1.
DR RefSeq; XP_006253815.1; XM_006253753.3.
DR RefSeq; XP_006253816.1; XM_006253754.2.
DR AlphaFoldDB; P52481; -.
DR SMR; P52481; -.
DR BioGRID; 250538; 2.
DR IntAct; P52481; 1.
DR MINT; P52481; -.
DR STRING; 10116.ENSRNOP00000062591; -.
DR iPTMnet; P52481; -.
DR PhosphoSitePlus; P52481; -.
DR jPOST; P52481; -.
DR PaxDb; P52481; -.
DR PRIDE; P52481; -.
DR Ensembl; ENSRNOT00000065742; ENSRNOP00000062591; ENSRNOG00000043350.
DR GeneID; 116653; -.
DR KEGG; rno:116653; -.
DR CTD; 10486; -.
DR RGD; 620310; Cap2.
DR eggNOG; KOG2675; Eukaryota.
DR GeneTree; ENSGT00390000017955; -.
DR InParanoid; P52481; -.
DR OMA; QQNHAPV; -.
DR OrthoDB; 1098760at2759; -.
DR PhylomeDB; P52481; -.
DR PRO; PR:P52481; -.
DR Proteomes; UP000002494; Chromosome 17.
DR Bgee; ENSRNOG00000043350; Expressed in frontal cortex and 18 other tissues.
DR Genevisible; P52481; RN.
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; ISO:RGD.
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:RGD.
DR GO; GO:0030036; P:actin cytoskeleton organization; TAS:RGD.
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; TAS:RGD.
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 Acetylation; Cell membrane; Membrane; Phosphoprotein; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P40123"
FT CHAIN 2..477
FT /note="Adenylyl cyclase-associated protein 2"
FT /id="PRO_0000205702"
FT DOMAIN 318..455
FT /note="C-CAP/cofactor C-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00659"
FT REGION 224..262
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 274..324
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 229..252
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 294..320
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:P40123"
FT MOD_RES 301
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 309
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P40123"
SQ SEQUENCE 477 AA; 52912 MW; CFCD65E8F256655B CRC64;
MADMLGLMQR LEFAVSRLER LSSGLHEPPG GCGEVNSLSR GIVAPSVEAF DKLINSMVAE
FLKNSRVLAG DVETHAEMVH GAFQAQRAFL LMVSQHQQPQ ENEVAVLLKP ISEKIQEIQT
FRERNRGSDM FNHLSAVSES IAALGWIAVS PKPGPYVKEM NDAATFYTNR VLRDYKHSDL
RHVDWVRSYL KIWSELQAYI KEHHTTGLTW SKTGPVASTA SAFSILSSGP GLPPPPPPPP
PPGPPPPFEN EGGKEEPSPS RSALFAQLNQ GEAITKGLRH VTDDKKIYKN PSLRAQGQIR
SPTKTRTPSP TSSKSNSPQK HAPVLELEGK KWRVEYQEDR NDLVISETEL KQVAYIFKCD
KSTLQIKGKV NSITVDNCKK FGLVFDHVVG IVEVINSKDI QIQVMGRVPT ISINKTEGCH
LYLSKDALDC EIVSAKSSEM NVLVPQGDDY REFPIPEQFK TIWDGSKLIT EPAEIMA
