ID   CAP1_PONAB              Reviewed;         475 AA.
AC   Q5R8B4;
DT   09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   25-MAY-2022, entry version 85.
DE   RecName: Full=Adenylyl cyclase-associated protein 1;
DE            Short=CAP 1;
GN   Name=CAP1;
OS   Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Pongo.
OX   NCBI_TaxID=9601;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain cortex;
RG   The German cDNA consortium;
RL   Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
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   -!- SIMILARITY: Belongs to the CAP family. {ECO:0000305}.
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DR   EMBL; CR859839; CAH91996.1; -; mRNA.
DR   RefSeq; NP_001126158.1; NM_001132686.1.
DR   AlphaFoldDB; Q5R8B4; -.
DR   SMR; Q5R8B4; -.
DR   STRING; 9601.ENSPPYP00000001729; -.
DR   GeneID; 100173118; -.
DR   KEGG; pon:100173118; -.
DR   CTD; 10487; -.
DR   eggNOG; KOG2675; Eukaryota.
DR   InParanoid; Q5R8B4; -.
DR   Proteomes; UP000001595; Unplaced.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
DR   GO; GO:0030036; P:actin cytoskeleton organization; IEA:InterPro.
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   2: Evidence at transcript level;
KW   Acetylation; Actin-binding; Cell membrane; Isopeptide bond; Membrane;
KW   Methylation; Phosphoprotein; Reference proteome; Ubl conjugation.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250|UniProtKB:Q01518"
FT   CHAIN           2..475
FT                   /note="Adenylyl cyclase-associated protein 1"
FT                   /id="PRO_0000271435"
FT   DOMAIN          313..453
FT                   /note="C-CAP/cofactor C-like"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00659"
FT   REGION          216..255
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          278..318
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        225..244
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         81
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q01518"
FT   MOD_RES         287
FT                   /note="N6-methyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q01518"
FT   MOD_RES         290
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q01518"
FT   MOD_RES         295
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q01518"
FT   MOD_RES         301
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q01518"
FT   MOD_RES         307
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:Q01518"
FT   MOD_RES         308
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q01518"
FT   MOD_RES         310
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q01518"
FT   CROSSLNK        348
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO1)"
FT                   /evidence="ECO:0000250|UniProtKB:Q01518"
SQ   SEQUENCE   475 AA;  51561 MW;  650520A1AC263CB7 CRC64;
     MADMQNLVER LERAVGRLEA VSHTSDMHRG YGDSPSKAGA APYVQVFDSL LAGPVAEYLK
     ISKEIGGDVQ KHAEMVHTGL KLERALLVTA SQCQQPADNK LSDLLAPISE QIKEVITFRE
     KNRGSKLFNH LSAVSESIQA LGWVAMAPKP GPYVKEMNDA AMFYTNRVLK EYKDVDKKHV
     DWVKAYLSIW TELQAYIKEF HTTGLAWSKT GPVAKELSGL PSGPSAGSGP PPPPPGPPPP
     PVSTSSGSDE SASRSALFAQ INQGESITHA LKHVSDDMKT HKNPALKAQS GPLRSGPKPF
     SAPKPQTSQS PKPATKKEPA VLELEGKKWR VENQENVSNL VIEDTELKQV AYIYKCVSTT
     LQIKGKINSI TVDNCKKLGL VFDDVVGIVE IINSGDVKVQ VMGKVPTISI NKTDGCHAYL
     SKNSLDCEIV SAKSSEMNVL IPTEGGDFNE FPVPEQFKTL WNGQKLVTTV TEIAG