SESQ2_MOUSE
ID SESQ2_MOUSE Reviewed; 259 AA.
AC Q14B98; Q8BUL8;
DT 31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 22-AUG-2006, sequence version 1.
DT 25-MAY-2022, entry version 95.
DE RecName: Full=Sesquipedalian-2;
DE Short=Ses2;
DE AltName: Full=27 kDa inositol polyphosphate phosphatase interacting protein B;
DE Short=IPIP27B;
DE AltName: Full=PH domain-containing endocytic trafficking adaptor 2 {ECO:0000250|UniProtKB:Q6ICB4};
GN Name=Pheta2 {ECO:0000250|UniProtKB:Q6ICB4};
GN Synonyms=Fam109b {ECO:0000312|MGI:MGI:2443609};
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=Thymus;
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 MRNA].
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).
RN [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Spleen;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
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:Q6ICB4}.
CC -!- SUBUNIT: Forms homodimers and heterodimers with PHETA1. Interacts with
CC OCRL and INPP5B. {ECO:0000250|UniProtKB:Q6ICB4}.
CC -!- SUBCELLULAR LOCATION: Early endosome {ECO:0000250|UniProtKB:Q6ICB4}.
CC Recycling endosome {ECO:0000250|UniProtKB:Q6ICB4}. Golgi apparatus,
CC trans-Golgi network {ECO:0000250|UniProtKB:Q6ICB4}. Cytoplasmic
CC vesicle, clathrin-coated vesicle {ECO:0000250|UniProtKB:Q6ICB4}.
CC Note=Also found on macropinosomes. Not detected in late endosomes, nor
CC in lysosomes. {ECO:0000250|UniProtKB:Q6ICB4}.
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:Q6ICB4}.
CC -!- SIMILARITY: Belongs to the sesquipedalian family. {ECO:0000305}.
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DR EMBL; AK083325; BAC38865.1; -; mRNA.
DR EMBL; BC116256; AAI16257.1; -; mRNA.
DR EMBL; BC116257; AAI16258.1; -; mRNA.
DR CCDS; CCDS27687.1; -.
DR RefSeq; NP_796365.1; NM_177391.4.
DR RefSeq; XP_006521179.1; XM_006521116.1.
DR RefSeq; XP_011243983.1; XM_011245681.2.
DR RefSeq; XP_011243984.1; XM_011245682.1.
DR AlphaFoldDB; Q14B98; -.
DR SMR; Q14B98; -.
DR STRING; 10090.ENSMUSP00000060598; -.
DR iPTMnet; Q14B98; -.
DR PhosphoSitePlus; Q14B98; -.
DR MaxQB; Q14B98; -.
DR PaxDb; Q14B98; -.
DR PRIDE; Q14B98; -.
DR ProteomicsDB; 261323; -.
DR DNASU; 338368; -.
DR GeneID; 338368; -.
DR KEGG; mmu:338368; -.
DR UCSC; uc007wyy.1; mouse.
DR CTD; 150368; -.
DR MGI; MGI:2443609; Pheta2.
DR eggNOG; ENOG502QQ94; Eukaryota.
DR InParanoid; Q14B98; -.
DR OrthoDB; 1329965at2759; -.
DR TreeFam; TF326731; -.
DR BioGRID-ORCS; 338368; 3 hits in 71 CRISPR screens.
DR ChiTaRS; Pheta2; mouse.
DR PRO; PR:Q14B98; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; Q14B98; protein.
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 1: Evidence at protein level;
KW Coiled coil; Cytoplasmic vesicle; Endosome; Golgi apparatus;
KW Reference proteome.
FT CHAIN 1..259
FT /note="Sesquipedalian-2"
FT /id="PRO_0000254134"
FT DOMAIN 17..121
FT /note="PH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT REGION 155..178
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 124..150
FT /evidence="ECO:0000255"
FT MOTIF 223..235
FT /note="F&H"
FT COMPBIAS 163..178
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 155
FT /note="S -> N (in Ref. 1; BAC38865)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 259 AA; 28707 MW; 30B67D59755898BF CRC64;
MKLNKRSVAH YALSDSPADH TGFLRSWGGP GSPPTPSGTG RRYWFVLKGN LLFSFETRES
RVPLSLVVLE GCTVELAEAP VPEEFAFAIR FDAPGVRPHL LAADGQAAQE AWVKALSRAS
FGYMRLVVRE LESQLQDARQ SLALHRCASQ RAVASCSKSQ APDHRAPDPE NGHFLPRDRS
SIGTVEERGI RPIGRDLTEW ELQGPASLLL SMGQSPVSPE SSCFSTLHDW YGKEIMELRR
GWQQRAKGSQ TENKSQNRP
