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Database: UniProt
Entry: A0A2G5DQJ5_AQUCA
LinkDB: A0A2G5DQJ5_AQUCA
Original site: A0A2G5DQJ5_AQUCA 
ID   A0A2G5DQJ5_AQUCA        Unreviewed;       358 AA.
AC   A0A2G5DQJ5;
DT   31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT   31-JAN-2018, sequence version 1.
DT   27-MAR-2024, entry version 22.
DE   RecName: Full=Afadin/alpha-actinin-binding protein {ECO:0008006|Google:ProtNLM};
DE   Flags: Fragment;
GN   ORFNames=AQUCO_01600010v1 {ECO:0000313|EMBL:PIA45527.1};
OS   Aquilegia coerulea (Rocky mountain columbine).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Ranunculales; Ranunculaceae; Thalictroideae;
OC   Aquilegia.
OX   NCBI_TaxID=218851 {ECO:0000313|EMBL:PIA45527.1, ECO:0000313|Proteomes:UP000230069};
RN   [1] {ECO:0000313|EMBL:PIA45527.1, ECO:0000313|Proteomes:UP000230069}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Goldsmith {ECO:0000313|Proteomes:UP000230069};
RA   Hodges S., Kramer E., Nordborg M., Tomkins J., Borevitz J., Derieg N.,
RA   Yan J., Mihaltcheva S., Hayes R.D., Rokhsar D.;
RT   "WGS assembly of Aquilegia coerulea Goldsmith.";
RL   Submitted (SEP-2017) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the ADIP family.
CC       {ECO:0000256|ARBA:ARBA00009291}.
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DR   EMBL; KZ305033; PIA45527.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2G5DQJ5; -.
DR   STRING; 218851.A0A2G5DQJ5; -.
DR   InParanoid; A0A2G5DQJ5; -.
DR   OrthoDB; 1057917at2759; -.
DR   Proteomes; UP000230069; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   InterPro; IPR021622; Afadin/alpha-actinin-bd.
DR   PANTHER; PTHR47057; AFADIN/ALPHA-ACTININ-BINDING; 1.
DR   PANTHER; PTHR47057:SF1; AFADIN_ALPHA-ACTININ-BINDING PROTEIN; 1.
DR   Pfam; PF11559; ADIP; 1.
PE   3: Inferred from homology;
KW   Coiled coil {ECO:0000256|ARBA:ARBA00023054, ECO:0000256|SAM:Coils};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000230069};
KW   Signal {ECO:0000256|SAM:SignalP}; Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   SIGNAL          1..24
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           25..358
FT                   /note="Afadin/alpha-actinin-binding protein"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5013861960"
FT   TRANSMEM        250..268
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   REGION          305..327
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          105..199
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          270..297
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   NON_TER         358
FT                   /evidence="ECO:0000313|EMBL:PIA45527.1"
SQ   SEQUENCE   358 AA;  41314 MW;  5512B7772F64B601 CRC64;
     MLPVSLSLFI YLLIAILNSF QASTQPGFGI SDCTFADAGN LEHCAKYLNQ TLVTFGFPAS
     LDLFANDPVS IARTCNCIYS LLQQRQRDIE FRESTNEQRQ RIFLDMLLSS DMSRLEAKVE
     RLEAQLAAKD RELATLTRTE AKATATFKAQ IEKLQQERDE FQRMVIGNQQ VRTQQIHEMK
     KKEKEYIKLQ ERLNQVLMEK KKESRSGMEI MNLLQKEERQ RGTWNGKKAD NDFYKMIIRN
     NKNENLICNY ITFNALGQLC FIIFLLVLQV DSYEVNKQEL MSENADLKAL LRSMQMDMRE
     FLNAPNGLSK PTVPLNERID ADPPQSPLGG KTDVFDLPFH MARDQIEESL RTKMASIK
//
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