SESQ2_HUMAN
ID SESQ2_HUMAN Reviewed; 259 AA.
AC Q6ICB4; Q3SXQ3; Q8N6L9;
DT 31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 130.
DE RecName: Full=Sesquipedalian-2 {ECO:0000305|PubMed:20133602};
DE Short=Ses2 {ECO:0000305|PubMed:20133602};
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:0000305};
GN Name=PHETA2 {ECO:0000312|HGNC:HGNC:27161};
GN Synonyms=FAM109B {ECO:0000312|HGNC:HGNC:27161};
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=15461802; DOI=10.1186/gb-2004-5-10-r84;
RA Collins J.E., Wright C.L., Edwards C.A., Davis M.P., Grinham J.A.,
RA Cole C.G., Goward M.E., Aguado B., Mallya M., Mokrab Y., Huckle E.J.,
RA Beare D.M., Dunham I.;
RT "A genome annotation-driven approach to cloning the human ORFeome.";
RL Genome Biol. 5:R84.1-R84.11(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=10591208; DOI=10.1038/990031;
RA Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M., Clamp M.,
RA Smink L.J., Ainscough R., Almeida J.P., Babbage A.K., Bagguley C.,
RA Bailey J., Barlow K.F., Bates K.N., Beasley O.P., Bird C.P., Blakey S.E.,
RA Bridgeman A.M., Buck D., Burgess J., Burrill W.D., Burton J., Carder C.,
RA Carter N.P., Chen Y., Clark G., Clegg S.M., Cobley V.E., Cole C.G.,
RA Collier R.E., Connor R., Conroy D., Corby N.R., Coville G.J., Cox A.V.,
RA Davis J., Dawson E., Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M.,
RA Ellington A.G., Evans K.L., Fey J.M., Fleming K., French L., Garner A.A.,
RA Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C.,
RA Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S., Hunt S.E.,
RA Jones M.C., Kershaw J., Kimberley A.M., King A., Laird G.K., Langford C.F.,
RA Leversha M.A., Lloyd C., Lloyd D.M., Martyn I.D., Mashreghi-Mohammadi M.,
RA Matthews L.H., Mccann O.T., Mcclay J., Mclaren S., McMurray A.A.,
RA Milne S.A., Mortimore B.J., Odell C.N., Pavitt R., Pearce A.V., Pearson D.,
RA Phillimore B.J.C.T., Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y.,
RA Rogers L., Ross M.T., Scott C.E., Sehra H.K., Skuce C.D., Smalley S.,
RA Smith M.L., Soderlund C., Spragon L., Steward C.A., Sulston J.E.,
RA Swann R.M., Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L.,
RA Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L.,
RA Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N.,
RA Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J., Shintani A.,
RA Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S., Roe B.A., Chen F., Chu L.,
RA Crabtree J., Deschamps S., Do A., Do T., Dorman A., Fang F., Fu Y., Hu P.,
RA Hua A., Kenton S., Lai H., Lao H.I., Lewis J., Lewis S., Lin S.-P., Loh P.,
RA Malaj E., Nguyen T., Pan H., Phan S., Qi S., Qian Y., Ray L., Ren Q.,
RA Shaull S., Sloan D., Song L., Wang Q., Wang Y., Wang Z., White J.,
RA Willingham D., Wu H., Yao Z., Zhan M., Zhang G., Chissoe S., Murray J.,
RA Miller N., Minx P., Fulton R., Johnson D., Bemis G., Bentley D.,
RA Bradshaw H., Bourne S., Cordes M., Du Z., Fulton L., Goela D., Graves T.,
RA Hawkins J., Hinds K., Kemp K., Latreille P., Layman D., Ozersky P.,
RA Rohlfing T., Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K.,
RA Nelson J., Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R.,
RA Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S., Budarf M.L.,
RA McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E., Edelmann L., Kim U.J.,
RA Shizuya H., Simon M.I., Dumanski J.P., Peyrard M., Kedra D., Seroussi E.,
RA Fransson I., Tapia I., Bruder C.E., O'Brien K.P., Wilkinson P.,
RA Bodenteich A., Hartman K., Hu X., Khan A.S., Lane L., Tilahun Y.,
RA Wright H.;
RT "The DNA sequence of human chromosome 22.";
RL Nature 402:489-495(1999).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT GLY-188.
RC TISSUE=Colon;
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 [4]
RP INTERACTION WITH OCRL, F&H MOTIF, AND SUBCELLULAR LOCATION.
RX PubMed=20133602; DOI=10.1073/pnas.0914658107;
RA Swan L.E., Tomasini L., Pirruccello M., Lunardi J., De Camilli P.;
RT "Two closely related endocytic proteins that share a common OCRL-binding
RT motif with APPL1.";
RL Proc. Natl. Acad. Sci. U.S.A. 107:3511-3516(2010).
RN [5]
RP FUNCTION, INTERACTION WITH OCRL AND INPP5B, SUBUNIT, SUBCELLULAR LOCATION,
RP AND MUTAGENESIS OF PHE-224; HIS-228 AND 234-GLU-ILE-235.
RX PubMed=21233288; DOI=10.1091/mbc.e10-08-0730;
RA Noakes C.J., Lee G., Lowe M.;
RT "The PH domain proteins IPIP27A and B link OCRL1 to receptor recycling in
RT the endocytic pathway.";
RL Mol. Biol. Cell 22:606-623(2011).
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:0000269|PubMed:21233288}.
CC -!- SUBUNIT: Forms homodimers and heterodimers with PHETA1. Interacts with
CC OCRL and INPP5B. {ECO:0000269|PubMed:20133602,
CC ECO:0000269|PubMed:21233288}.
CC -!- INTERACTION:
CC Q6ICB4; Q5SYC1: CLVS2; NbExp=3; IntAct=EBI-11081747, EBI-12357161;
CC Q6ICB4; Q01968-2: OCRL; NbExp=6; IntAct=EBI-11081747, EBI-11749425;
CC Q6ICB4; Q8N4B1-4: PHETA1; NbExp=5; IntAct=EBI-11081747, EBI-14131832;
CC Q6ICB4; Q9NW61: PLEKHJ1; NbExp=4; IntAct=EBI-11081747, EBI-1057560;
CC -!- SUBCELLULAR LOCATION: Early endosome {ECO:0000269|PubMed:21233288}.
CC Recycling endosome {ECO:0000269|PubMed:21233288}. Golgi apparatus,
CC trans-Golgi network {ECO:0000269|PubMed:21233288}. Cytoplasmic vesicle,
CC clathrin-coated vesicle {ECO:0000269|PubMed:21233288}. Note=Also found
CC on macropinosomes. Not detected in late endosomes, nor in lysosomes.
CC {ECO:0000269|PubMed:20133602, ECO:0000269|PubMed:21233288}.
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:0000305|PubMed:20133602}.
CC -!- SIMILARITY: Belongs to the sesquipedalian family. {ECO:0000305}.
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DR EMBL; CR456454; CAG30340.1; -; mRNA.
DR EMBL; Z99716; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; Z82192; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC029776; AAH29776.1; -; mRNA.
DR EMBL; BC104175; AAI04176.1; -; mRNA.
DR EMBL; BC104176; AAI04177.1; -; mRNA.
DR CCDS; CCDS33655.1; -.
DR RefSeq; NP_001002034.2; NM_001002034.2.
DR RefSeq; XP_005261430.1; XM_005261373.3.
DR AlphaFoldDB; Q6ICB4; -.
DR SMR; Q6ICB4; -.
DR BioGRID; 127287; 14.
DR ELM; Q6ICB4; -.
DR IntAct; Q6ICB4; 9.
DR MINT; Q6ICB4; -.
DR STRING; 9606.ENSP00000312753; -.
DR iPTMnet; Q6ICB4; -.
DR PhosphoSitePlus; Q6ICB4; -.
DR BioMuta; FAM109B; -.
DR DMDM; 74757717; -.
DR EPD; Q6ICB4; -.
DR jPOST; Q6ICB4; -.
DR MassIVE; Q6ICB4; -.
DR MaxQB; Q6ICB4; -.
DR PaxDb; Q6ICB4; -.
DR PeptideAtlas; Q6ICB4; -.
DR PRIDE; Q6ICB4; -.
DR ProteomicsDB; 66383; -.
DR Antibodypedia; 270; 40 antibodies from 11 providers.
DR DNASU; 150368; -.
DR Ensembl; ENST00000321753.8; ENSP00000312753.3; ENSG00000177096.9.
DR GeneID; 150368; -.
DR KEGG; hsa:150368; -.
DR MANE-Select; ENST00000321753.8; ENSP00000312753.3; NM_001002034.3; NP_001002034.2.
DR UCSC; uc003bbz.4; human.
DR CTD; 150368; -.
DR DisGeNET; 150368; -.
DR GeneCards; PHETA2; -.
DR HGNC; HGNC:27161; PHETA2.
DR HPA; ENSG00000177096; Low tissue specificity.
DR MIM; 614240; gene.
DR neXtProt; NX_Q6ICB4; -.
DR OpenTargets; ENSG00000177096; -.
DR PharmGKB; PA143485467; -.
DR VEuPathDB; HostDB:ENSG00000177096; -.
DR eggNOG; ENOG502QQ94; Eukaryota.
DR GeneTree; ENSGT00940000162686; -.
DR HOGENOM; CLU_060423_0_1_1; -.
DR InParanoid; Q6ICB4; -.
DR OMA; CDSPADH; -.
DR OrthoDB; 1329965at2759; -.
DR PhylomeDB; Q6ICB4; -.
DR TreeFam; TF326731; -.
DR PathwayCommons; Q6ICB4; -.
DR SignaLink; Q6ICB4; -.
DR BioGRID-ORCS; 150368; 14 hits in 1075 CRISPR screens.
DR GenomeRNAi; 150368; -.
DR Pharos; Q6ICB4; Tbio.
DR PRO; PR:Q6ICB4; -.
DR Proteomes; UP000005640; Chromosome 22.
DR RNAct; Q6ICB4; protein.
DR Bgee; ENSG00000177096; Expressed in stromal cell of endometrium and 146 other tissues.
DR ExpressionAtlas; Q6ICB4; baseline and differential.
DR Genevisible; Q6ICB4; HS.
DR GO; GO:0030136; C:clathrin-coated vesicle; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; IEA:GOC.
DR GO; GO:0005769; C:early endosome; IDA:UniProtKB.
DR GO; GO:0055037; C:recycling endosome; IDA:UniProtKB.
DR GO; GO:0005802; C:trans-Golgi network; IDA:UniProtKB.
DR GO; GO:0042803; F:protein homodimerization activity; IPI:UniProtKB.
DR GO; GO:0007032; P:endosome organization; IMP:UniProtKB.
DR GO; GO:0001881; P:receptor recycling; IMP:UniProtKB.
DR GO; GO:0042147; P:retrograde transport, endosome to Golgi; IMP:UniProtKB.
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_0000254133"
FT DOMAIN 17..121
FT /note="PH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT COILED 124..149
FT /evidence="ECO:0000255"
FT MOTIF 223..235
FT /note="F&H"
FT VARIANT 188
FT /note="A -> G (in dbSNP:rs1807493)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_028822"
FT MUTAGEN 224
FT /note="F->A: Loss of OCRL-binding."
FT /evidence="ECO:0000269|PubMed:21233288"
FT MUTAGEN 228
FT /note="H->A: Loss of OCRL-binding."
FT /evidence="ECO:0000269|PubMed:21233288"
FT MUTAGEN 234..235
FT /note="EI->AA: Loss of OCRL-binding."
FT /evidence="ECO:0000269|PubMed:21233288"
SQ SEQUENCE 259 AA; 28338 MW; F82FDD0D2314BB0F CRC64;
MKLNERSVAH YALSDSPADH MGFLRTWGGP GTPPTPSGTG RRCWFVLKGN LLFSFESREG
RAPLSLVVLE GCTVELAEAP VPEEFAFAIC FDAPGVRPHL LAAEGPAAQE AWVKVLSRAS
FGYMRLVVRE LESQLQDARQ SLALQRRSSW KSVASRCKPQ APNHRAAGLE NGHCLSKDSS
PVGLVEEAGS RSAGWGLAEW ELQGPASLLL GKGQSPVSPE TSCFSTLHDW YGQEIVELRQ
CWQKRAQGSH SKCEEQDRP
