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AMER2_CHICK
ID   AMER2_CHICK             Reviewed;         624 AA.
AC   E1C2Q8;
DT   21-MAR-2012, integrated into UniProtKB/Swiss-Prot.
DT   02-NOV-2010, sequence version 1.
DT   03-AUG-2022, entry version 57.
DE   RecName: Full=APC membrane recruitment protein 2;
DE            Short=Amer2;
DE   AltName: Full=Protein FAM123A;
GN   Name=AMER2; Synonyms=FAM123A;
OS   Gallus gallus (Chicken).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC   Phasianinae; Gallus.
OX   NCBI_TaxID=9031;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Red jungle fowl;
RX   PubMed=15592404; DOI=10.1038/nature03154;
RA   Hillier L.W., Miller W., Birney E., Warren W., Hardison R.C., Ponting C.P.,
RA   Bork P., Burt D.W., Groenen M.A.M., Delany M.E., Dodgson J.B.,
RA   Chinwalla A.T., Cliften P.F., Clifton S.W., Delehaunty K.D., Fronick C.,
RA   Fulton R.S., Graves T.A., Kremitzki C., Layman D., Magrini V.,
RA   McPherson J.D., Miner T.L., Minx P., Nash W.E., Nhan M.N., Nelson J.O.,
RA   Oddy L.G., Pohl C.S., Randall-Maher J., Smith S.M., Wallis J.W.,
RA   Yang S.-P., Romanov M.N., Rondelli C.M., Paton B., Smith J., Morrice D.,
RA   Daniels L., Tempest H.G., Robertson L., Masabanda J.S., Griffin D.K.,
RA   Vignal A., Fillon V., Jacobbson L., Kerje S., Andersson L.,
RA   Crooijmans R.P., Aerts J., van der Poel J.J., Ellegren H., Caldwell R.B.,
RA   Hubbard S.J., Grafham D.V., Kierzek A.M., McLaren S.R., Overton I.M.,
RA   Arakawa H., Beattie K.J., Bezzubov Y., Boardman P.E., Bonfield J.K.,
RA   Croning M.D.R., Davies R.M., Francis M.D., Humphray S.J., Scott C.E.,
RA   Taylor R.G., Tickle C., Brown W.R.A., Rogers J., Buerstedde J.-M.,
RA   Wilson S.A., Stubbs L., Ovcharenko I., Gordon L., Lucas S., Miller M.M.,
RA   Inoko H., Shiina T., Kaufman J., Salomonsen J., Skjoedt K., Wong G.K.-S.,
RA   Wang J., Liu B., Wang J., Yu J., Yang H., Nefedov M., Koriabine M.,
RA   Dejong P.J., Goodstadt L., Webber C., Dickens N.J., Letunic I., Suyama M.,
RA   Torrents D., von Mering C., Zdobnov E.M., Makova K., Nekrutenko A.,
RA   Elnitski L., Eswara P., King D.C., Yang S.-P., Tyekucheva S.,
RA   Radakrishnan A., Harris R.S., Chiaromonte F., Taylor J., He J.,
RA   Rijnkels M., Griffiths-Jones S., Ureta-Vidal A., Hoffman M.M., Severin J.,
RA   Searle S.M.J., Law A.S., Speed D., Waddington D., Cheng Z., Tuzun E.,
RA   Eichler E., Bao Z., Flicek P., Shteynberg D.D., Brent M.R., Bye J.M.,
RA   Huckle E.J., Chatterji S., Dewey C., Pachter L., Kouranov A.,
RA   Mourelatos Z., Hatzigeorgiou A.G., Paterson A.H., Ivarie R., Brandstrom M.,
RA   Axelsson E., Backstrom N., Berlin S., Webster M.T., Pourquie O.,
RA   Reymond A., Ucla C., Antonarakis S.E., Long M., Emerson J.J., Betran E.,
RA   Dupanloup I., Kaessmann H., Hinrichs A.S., Bejerano G., Furey T.S.,
RA   Harte R.A., Raney B., Siepel A., Kent W.J., Haussler D., Eyras E.,
RA   Castelo R., Abril J.F., Castellano S., Camara F., Parra G., Guigo R.,
RA   Bourque G., Tesler G., Pevzner P.A., Smit A., Fulton L.A., Mardis E.R.,
RA   Wilson R.K.;
RT   "Sequence and comparative analysis of the chicken genome provide unique
RT   perspectives on vertebrate evolution.";
RL   Nature 432:695-716(2004).
CC   -!- FUNCTION: Negative regulator of the canonical Wnt signaling pathway
CC       involved in neuroectodermal patterning. Acts by specifically binding
CC       phosphatidylinositol 4,5-bisphosphate (PtdIns(4,5)P2), translocating to
CC       the cell membrane and interacting with key regulators of the canonical
CC       Wnt signaling pathway, such as components of the beta-catenin
CC       destruction complex (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Peripheral membrane
CC       protein {ECO:0000250}. Note=Translocates to the cell membrane following
CC       binding to PtdIns(4,5)P2. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the Amer family. {ECO:0000305}.
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DR   EMBL; AADN02005159; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   AlphaFoldDB; E1C2Q8; -.
DR   STRING; 9031.ENSGALP00000043401; -.
DR   PaxDb; E1C2Q8; -.
DR   Ensembl; ENSGALT00000044804; ENSGALP00000043401; ENSGALG00000027868.
DR   VEuPathDB; HostDB:geneid_418939; -.
DR   GeneTree; ENSGT00530000063529; -.
DR   InParanoid; E1C2Q8; -.
DR   OMA; IDRICLM; -.
DR   PhylomeDB; E1C2Q8; -.
DR   TreeFam; TF333006; -.
DR   PRO; PR:E1C2Q8; -.
DR   Proteomes; UP000000539; Chromosome 1.
DR   Bgee; ENSGALG00000027868; Expressed in cerebellum and 4 other tissues.
DR   ExpressionAtlas; E1C2Q8; baseline.
DR   GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR   GO; GO:0008013; F:beta-catenin binding; IBA:GO_Central.
DR   GO; GO:0005546; F:phosphatidylinositol-4,5-bisphosphate binding; ISS:UniProtKB.
DR   GO; GO:0007398; P:ectoderm development; ISS:UniProtKB.
DR   GO; GO:0090090; P:negative regulation of canonical Wnt signaling pathway; ISS:UniProtKB.
DR   GO; GO:0060828; P:regulation of canonical Wnt signaling pathway; IBA:GO_Central.
DR   GO; GO:0016055; P:Wnt signaling pathway; IEA:UniProtKB-KW.
DR   InterPro; IPR019003; AMER.
DR   PANTHER; PTHR22237; PTHR22237; 1.
DR   Pfam; PF09422; WTX; 1.
PE   3: Inferred from homology;
KW   Cell membrane; Lipid-binding; Membrane; Reference proteome;
KW   Wnt signaling pathway.
FT   CHAIN           1..624
FT                   /note="APC membrane recruitment protein 2"
FT                   /id="PRO_0000416260"
FT   REGION          1..308
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          342..596
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        66..84
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        98..112
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        122..139
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        149..167
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        451..468
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        471..495
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        531..553
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   624 AA;  65286 MW;  40A36DC13FC71F5D CRC64;
     MDSHCDCAEP PAAEQPSGKI NKTAFKLFKR RKSGGTMPSI FGVRSKGGEG KGASKTGMVR
     SRTHDGLADA VLESGKKEDA GGGEAQGKDA PSRAAGGLGG SASSSVAKSH SFFSLLRKNG
     RPENGKAAEN AEQRAGGRQK KGLKGIFSSM RWHRKDKIGK EERGEASEIP SGLIMPGSLT
     ASLECIKEET PKPLSETPNG AGDTGVESQQ EKRGGDACVS AEEPQAGGGE SRDSKTPPGE
     DPAAAARRLE ELCGERPDPG AGEVGTAKDA AITGDIPITT IPPVEPHCDS GQETAAAPDP
     SSVDPPSEQS IDRICLMFAD VTSLKSFDSL TGCGDIIADQ EEDVGGGSGG CEKSTPGAGK
     LGAPKKHPTM VAYQGGGEEM ASPDQVDDTY LQEFWDMLSQ TEETETGGGG GGGGGTKTPE
     GLKENRGTEG AQNRVAVKRG GLNQIPIHLN NKEEQKGREK EQHEGVPNSD EGYWDSTTPG
     PEEDSTTSIQ KETLPRDSYS GDALYDLYAE PDENPPGGPP EEEVTCMPRS KPVSPITTTC
     SLKTPSSTVK DSKIPISIKH LASHPASHGT DTSNSHHVAH HHLAKSEMHR TKIPVSKVLV
     RRVSNRGLAG TTVKAATHQD SAKK
 
 
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