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CAP1_PIG
ID   CAP1_PIG                Reviewed;         233 AA.
AC   P40125;
DT   01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1995, sequence version 1.
DT   25-MAY-2022, entry version 99.
DE   RecName: Full=Adenylyl cyclase-associated protein 1;
DE            Short=CAP 1;
DE   AltName: Full=ASP-56 protein;
DE   Flags: Fragments;
GN   Name=CAP1; Synonyms=CAP;
OS   Sus scrofa (Pig).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX   NCBI_TaxID=9823;
RN   [1]
RP   PROTEIN SEQUENCE.
RC   TISSUE=Platelet;
RX   PubMed=1544438; DOI=10.1016/0014-5793(92)80043-g;
RA   Gieselmann R., Mann K.;
RT   "ASP-56, a new actin sequestering protein from pig platelets with homology
RT   to CAP, an adenylate cyclase-associated protein from yeast.";
RL   FEBS Lett. 298:149-153(1992).
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   PeptideAtlas; P40125; -.
DR   PRIDE; P40125; -.
DR   InParanoid; P40125; -.
DR   Proteomes; UP000008227; Unplaced.
DR   Proteomes; UP000314985; Unplaced.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
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; IEA:InterPro.
DR   GO; GO:0019933; P:cAMP-mediated signaling; IBA:GO_Central.
DR   GO; GO:0000902; P:cell morphogenesis; IBA:GO_Central.
DR   GO; GO:0045761; P:regulation of adenylate cyclase activity; IBA:GO_Central.
DR   Gene3D; 2.160.20.70; -; 1.
DR   InterPro; IPR001837; Adenylate_cyclase-assoc_CAP.
DR   InterPro; IPR013912; Adenylate_cyclase-assoc_CAP_C.
DR   InterPro; IPR016098; CAP/MinC_C.
DR   InterPro; IPR028415; CAP1.
DR   InterPro; IPR036223; CAP_C_sf.
DR   PANTHER; PTHR10652; PTHR10652; 2.
DR   PANTHER; PTHR10652:SF1; PTHR10652:SF1; 2.
DR   Pfam; PF08603; CAP_C; 1.
DR   SUPFAM; SSF69340; SSF69340; 1.
DR   PROSITE; PS01089; CAP_2; 1.
PE   1: Evidence at protein level;
KW   Actin-binding; Cell membrane; Direct protein sequencing; Isopeptide bond;
KW   Membrane; Methylation; Phosphoprotein; Reference proteome; Ubl conjugation.
FT   CHAIN           <1..>233
FT                   /note="Adenylyl cyclase-associated protein 1"
FT                   /id="PRO_0000205698"
FT   DOMAIN          <173..221
FT                   /note="C-CAP/cofactor C-like"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00659"
FT   REGION          1..21
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          43..128
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        83..99
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         14
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000250|UniProtKB:P40124"
FT   MOD_RES         17
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q01518"
FT   MOD_RES         101
FT                   /note="N6-methyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q01518"
FT   MOD_RES         104
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q01518"
FT   MOD_RES         115
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q01518"
FT   MOD_RES         122
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q01518"
FT   MOD_RES         124
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q01518"
FT   CROSSLNK        151
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO1)"
FT                   /evidence="ECO:0000250|UniProtKB:Q01518"
FT   NON_CONS        20..21
FT                   /evidence="ECO:0000305"
FT   NON_CONS        38..39
FT                   /evidence="ECO:0000305"
FT   NON_CONS        45..46
FT                   /evidence="ECO:0000305"
FT   NON_CONS        68..69
FT                   /evidence="ECO:0000305"
FT   NON_CONS        130..131
FT                   /evidence="ECO:0000305"
FT   NON_CONS        151..152
FT                   /evidence="ECO:0000305"
FT   NON_CONS        172..173
FT                   /evidence="ECO:0000305"
FT   NON_TER         1
FT   NON_TER         233
SQ   SEQUENCE   233 AA;  25079 MW;  F9D022193D150698 CRC64;
     LEAVSHASDT HYGYGDSAAK EIGGDVLKHA EMVHTGLKEY KDVDKXGPVA KELSGLPSGP
     SAGSGPPPSA LFAQIHQGES ITHALKHVAD DEKTHKNPAD KAQSGPVRXG PKPFSASKPG
     ISPSPKPVTK KWRXENXENV SNLVIDDTEL KSVNSTLQIK XXINSISVDN YKVPXISINK
     XDGRHIYLSK NSLDCEIVSA KSSEMNVLIP TEGGDFNEFP VPEQXKXIWN GQK
 
 
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