ID CAP1_RAT Reviewed; 474 AA.
AC Q08163; Q5FVS8;
DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 24-JAN-2024, entry version 156.
DE RecName: Full=Adenylyl cyclase-associated protein 1;
DE Short=CAP 1;
GN Name=Cap1; Synonyms=Cap, Mch1;
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=8514780; DOI=10.1016/s0021-9258(19)38670-3;
RA Zelicof A., Gatica J., Gerst J.E.;
RT "Molecular cloning and characterization of a rat homolog of CAP, the
RT adenylyl cyclase-associated protein from Saccharomyces cerevisiae.";
RL J. Biol. Chem. 268:13448-13453(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Thymus;
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 PROTEIN SEQUENCE OF 100-118; 254-272 AND 377-394, AND IDENTIFICATION BY
RP MASS SPECTROMETRY.
RC STRAIN=Sprague-Dawley; TISSUE=Hippocampus, and Spinal cord;
RA Lubec G., Afjehi-Sadat L., Diao W.;
RL Submitted (APR-2007) to UniProtKB.
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 -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Peripheral membrane
CC protein {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: In all cell and tissue types examined.
CC -!- SIMILARITY: Belongs to the CAP family. {ECO:0000305}.
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DR EMBL; L11930; AAA41579.1; -; mRNA.
DR EMBL; BC089801; AAH89801.1; -; mRNA.
DR PIR; A46584; A46584.
DR RefSeq; NP_071778.2; NM_022383.2.
DR RefSeq; XP_006238892.1; XM_006238830.3.
DR RefSeq; XP_006238893.1; XM_006238831.3.
DR RefSeq; XP_006238894.1; XM_006238832.3.
DR AlphaFoldDB; Q08163; -.
DR SMR; Q08163; -.
DR BioGRID; 248992; 1.
DR DIP; DIP-225N; -.
DR IntAct; Q08163; 3.
DR MINT; Q08163; -.
DR STRING; 10116.ENSRNOP00000018711; -.
DR iPTMnet; Q08163; -.
DR PhosphoSitePlus; Q08163; -.
DR SwissPalm; Q08163; -.
DR World-2DPAGE; 0004:Q08163; -.
DR jPOST; Q08163; -.
DR PaxDb; 10116-ENSRNOP00000018711; -.
DR Ensembl; ENSRNOT00055022259; ENSRNOP00055018074; ENSRNOG00055012988.
DR Ensembl; ENSRNOT00060030922; ENSRNOP00060025037; ENSRNOG00060017979.
DR Ensembl; ENSRNOT00065000788; ENSRNOP00065000632; ENSRNOG00065000543.
DR Ensembl; ENSRNOT00065026006; ENSRNOP00065020465; ENSRNOG00065015634.
DR GeneID; 64185; -.
DR KEGG; rno:64185; -.
DR UCSC; RGD:620309; rat.
DR AGR; RGD:620309; -.
DR CTD; 10487; -.
DR RGD; 620309; Cap1.
DR VEuPathDB; HostDB:ENSRNOG00000013492; -.
DR eggNOG; KOG2675; Eukaryota.
DR HOGENOM; CLU_015780_1_1_1; -.
DR InParanoid; Q08163; -.
DR OrthoDB; 1453907at2759; -.
DR PhylomeDB; Q08163; -.
DR TreeFam; TF313791; -.
DR Reactome; R-RNO-6798695; Neutrophil degranulation.
DR PRO; PR:Q08163; -.
DR Proteomes; UP000002494; Chromosome 5.
DR Bgee; ENSRNOG00000013492; Expressed in spleen and 19 other cell types or tissues.
DR Genevisible; Q08163; RN.
DR GO; GO:0030864; C:cortical actin cytoskeleton; ISO:RGD.
DR GO; GO:0005737; C:cytoplasm; ISO:RGD.
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; ISO:RGD.
DR GO; GO:0007015; P:actin filament organization; IBA:GO_Central.
DR GO; GO:0001667; P:ameboidal-type cell migration; ISO:RGD.
DR GO; GO:0019933; P:cAMP-mediated signaling; IBA:GO_Central.
DR GO; GO:0000902; P:cell morphogenesis; ISO:RGD.
DR GO; GO:0006898; P:receptor-mediated endocytosis; ISO:RGD.
DR Gene3D; 2.160.20.70; -; 1.
DR Gene3D; 1.25.40.330; Adenylate cyclase-associated CAP, N-terminal domain; 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; 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; ADENYLYL CYCLASE-ASSOCIATED PROTEIN; 1.
DR PANTHER; PTHR10652:SF1; ADENYLYL CYCLASE-ASSOCIATED PROTEIN 1; 1.
DR Pfam; PF08603; CAP_C; 1.
DR Pfam; PF01213; CAP_N; 1.
DR SMART; SM00673; CARP; 2.
DR SUPFAM; SSF69340; C-terminal domain of adenylylcyclase associated protein; 1.
DR SUPFAM; SSF101278; N-terminal domain of adenylylcyclase associated protein, CAP; 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; Actin-binding; Cell membrane; Direct protein sequencing;
KW Isopeptide bond; Membrane; Methylation; Phosphoprotein; Reference proteome;
KW 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_0000205699"
FT DOMAIN 312..452
FT /note="C-CAP/cofactor C-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00659"
FT REGION 215..252
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..244
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:0000250|UniProtKB:P40124"
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 388
FT /note="V -> G (in Ref. 1; AAA41579)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 474 AA; 51589 MW; EB2CC635109479B3 CRC64;
MADMQNLVER LERAVGRLEA VSHTSDMHCG YGDSPSKGAV PYVQAFDSLL ANPVAEYLKM
SKEIGGDVQK HAEMVHTGLK LERALLVTAS QCQQPAGNKL SDLLAPISEQ IQEVITFREK
NRGSKFFNHL SAVSESIQAL GWVALAAKPG PFVKEMNDAA MFYTNRVLKE YRDVDKKHVD
WVRAYLSIWT ELQAYIKEFH TTGLAWSKTG PVAKELSGLP SGPSVGSGPP PPPPGPPPPP
VPTSSGSDDS ASRSALFAQI NQGESITHAL KHVSDDMKTH KNPALKAQSG PVRSGPKPFS
APKPQTSPSP KPATKKEPAL LELEGKKWRV ENQENVSNLV IDDTELKQVA YIYKCVNTTL
QIKGKINSIT VDNCKKLGLV FDDVVGIVEI INSRDVKVQV MGKVPTISIN KTDGCHAYLS
KNSLDCEIVS AKSSEMNVLI PTEGGDFNEF PVPEQFKTLW NGQKLVTTVT EIAG
//
