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SESQ1_MOUSE
ID   SESQ1_MOUSE             Reviewed;         266 AA.
AC   Q8BH49;
DT   08-MAR-2011, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   03-AUG-2022, entry version 123.
DE   RecName: Full=Sesquipedalian-1;
DE            Short=Ses1;
DE   AltName: Full=27 kDa inositol polyphosphate phosphatase interacting protein A;
DE            Short=IPIP27A;
DE   AltName: Full=PH domain-containing endocytic trafficking adaptor 1 {ECO:0000250|UniProtKB:Q8N4B1};
GN   Name=Pheta1 {ECO:0000250|UniProtKB:Q8N4B1};
GN   Synonyms=Fam109a {ECO:0000312|MGI:MGI:2442708};
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Cecum, and Hypothalamus;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA   Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA   Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA   Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA   Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA   Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA   Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA   Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA   Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA   Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA   Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA   Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA   Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA   Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA   Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA   Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA   Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA   Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA   Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA   Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA   van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA   Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA   Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA   Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA   Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA   Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA   Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA   Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA   Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain;
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).
CC   -!- FUNCTION: Plays a role in endocytic trafficking. Required for receptor
CC       recycling from endosomes, both to the trans-Golgi network and the
CC       plasma membrane. {ECO:0000250|UniProtKB:Q8N4B1}.
CC   -!- SUBUNIT: Forms homodimers and heterodimers with PHETA2. Interacts with
CC       OCRL and INPP5B (By similarity). Interaction with OCRL may be important
CC       for endosomal morphology and function (By similarity).
CC       {ECO:0000250|UniProtKB:D3ZL52, ECO:0000250|UniProtKB:Q8N4B1}.
CC   -!- SUBCELLULAR LOCATION: Early endosome {ECO:0000250|UniProtKB:Q8N4B1}.
CC       Recycling endosome {ECO:0000250|UniProtKB:Q8N4B1}. Golgi apparatus,
CC       trans-Golgi network {ECO:0000250|UniProtKB:Q8N4B1}. Cytoplasmic
CC       vesicle, clathrin-coated vesicle {ECO:0000250|UniProtKB:Q8N4B1}.
CC       Note=Interaction with OCRL may be crucial for targeting to endosome and
CC       to the trans-Golgi network. Also found on macropinosomes. Not detected
CC       in late endosomes, nor in lysosomes. {ECO:0000250|UniProtKB:Q8N4B1}.
CC   -!- DOMAIN: The F&H motif, an approximately 12-13 amino-acid sequence
CC       centered around Phe and His residues, is essential for binding to OCRL
CC       and INPP5B. {ECO:0000250|UniProtKB:Q8N4B1}.
CC   -!- MISCELLANEOUS: Was named after 'sesquipedalian', an unnecessarily long
CC       description of a simple thing. {ECO:0000250|UniProtKB:Q8N4B1}.
CC   -!- SIMILARITY: Belongs to the sesquipedalian family. {ECO:0000305}.
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DR   EMBL; AK033618; BAC28394.1; -; mRNA.
DR   EMBL; AK039192; BAC30272.1; -; mRNA.
DR   EMBL; CH466529; EDL19707.1; -; Genomic_DNA.
DR   EMBL; CH466529; EDL19708.1; -; Genomic_DNA.
DR   EMBL; BC120681; AAI20682.1; -; mRNA.
DR   EMBL; BC120683; AAI20684.1; -; mRNA.
DR   CCDS; CCDS19642.1; -.
DR   RefSeq; NP_780683.1; NM_175474.3.
DR   RefSeq; XP_006530367.1; XM_006530304.3.
DR   AlphaFoldDB; Q8BH49; -.
DR   SMR; Q8BH49; -.
DR   STRING; 10090.ENSMUSP00000062386; -.
DR   iPTMnet; Q8BH49; -.
DR   PhosphoSitePlus; Q8BH49; -.
DR   MaxQB; Q8BH49; -.
DR   PaxDb; Q8BH49; -.
DR   PRIDE; Q8BH49; -.
DR   ProteomicsDB; 256970; -.
DR   Antibodypedia; 45279; 73 antibodies from 16 providers.
DR   DNASU; 231717; -.
DR   Ensembl; ENSMUST00000056654; ENSMUSP00000062386; ENSMUSG00000044134.
DR   Ensembl; ENSMUST00000198271; ENSMUSP00000143110; ENSMUSG00000044134.
DR   GeneID; 231717; -.
DR   KEGG; mmu:231717; -.
DR   UCSC; uc008zkj.1; mouse.
DR   CTD; 144717; -.
DR   MGI; MGI:2442708; Pheta1.
DR   VEuPathDB; HostDB:ENSMUSG00000044134; -.
DR   eggNOG; ENOG502QQ94; Eukaryota.
DR   GeneTree; ENSGT00940000162791; -.
DR   InParanoid; Q8BH49; -.
DR   OMA; NGCAVWN; -.
DR   OrthoDB; 1329965at2759; -.
DR   PhylomeDB; Q8BH49; -.
DR   TreeFam; TF326731; -.
DR   BioGRID-ORCS; 231717; 3 hits in 72 CRISPR screens.
DR   ChiTaRS; Pheta1; mouse.
DR   PRO; PR:Q8BH49; -.
DR   Proteomes; UP000000589; Chromosome 5.
DR   RNAct; Q8BH49; protein.
DR   Bgee; ENSMUSG00000044134; Expressed in jejunum and 158 other tissues.
DR   ExpressionAtlas; Q8BH49; baseline and differential.
DR   Genevisible; Q8BH49; MM.
DR   GO; GO:0030136; C:clathrin-coated vesicle; ISO:MGI.
DR   GO; GO:0005829; C:cytosol; IEA:GOC.
DR   GO; GO:0005769; C:early endosome; ISO:MGI.
DR   GO; GO:0055037; C:recycling endosome; ISO:MGI.
DR   GO; GO:0005802; C:trans-Golgi network; ISO:MGI.
DR   GO; GO:0042803; F:protein homodimerization activity; ISO:MGI.
DR   GO; GO:0007032; P:endosome organization; ISO:MGI.
DR   GO; GO:0001881; P:receptor recycling; ISO:MGI.
DR   GO; GO:0042147; P:retrograde transport, endosome to Golgi; ISO:MGI.
DR   Gene3D; 2.30.29.30; -; 1.
DR   InterPro; IPR045188; Boi1/Boi2-like.
DR   InterPro; IPR011993; PH-like_dom_sf.
DR   InterPro; IPR001849; PH_domain.
DR   PANTHER; PTHR22902; PTHR22902; 1.
DR   Pfam; PF00169; PH; 1.
DR   SMART; SM00233; PH; 1.
DR   PROSITE; PS50003; PH_DOMAIN; 1.
PE   2: Evidence at transcript level;
KW   Cytoplasmic vesicle; Endosome; Golgi apparatus; Phosphoprotein;
KW   Reference proteome.
FT   CHAIN           1..266
FT                   /note="Sesquipedalian-1"
FT                   /id="PRO_0000406046"
FT   DOMAIN          17..113
FT                   /note="PH"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT   REGION          164..184
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           191..203
FT                   /note="F&H"
FT   COMPBIAS        167..181
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         183
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8N4B1"
SQ   SEQUENCE   266 AA;  29218 MW;  4D0C3B71A5D23F4F CRC64;
     MKLNERSLAF YATCDAPVDN AGFLYKRGGR GTGSHRRWFV LRGNILFYFE AEGSREPLGV
     ILLEGCTVEL VDAREEFAFA VRFAGGRSRP YVLAADSQAA LEGWVKALSR ASFHYLRLVV
     RELEQQLAAM REGSPANALP ANPSPVLTQR PKENGWVVWS TLPEQPSVAP QRPPPLPPRR
     RASAANGPLA SFAQLHARYG LEVQALRDQW RGGQAGLASL EVPWHPGSAE TQTQDQPALR
     GHSGCKVLHV FRSVEWPVCN PGSQGT
 
 
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