FHI2B_MOUSE
ID FHI2B_MOUSE Reviewed; 744 AA.
AC Q80YR2; Q6PED9; Q8C1Y2;
DT 17-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT 17-APR-2007, sequence version 2.
DT 03-AUG-2022, entry version 107.
DE RecName: Full=FHF complex subunit HOOK interacting protein 2B;
DE Short=FHIP2B;
DE AltName: Full=Retinoic acid-induced protein 16 {ECO:0000303|PubMed:31862898};
GN Name=Fhip2b; Synonyms=Fam160b2, Rai16 {ECO:0000303|PubMed:31862898};
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 GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 550-744 (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Brain, and Embryo;
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 235-744 (ISOFORM 1).
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 [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
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).
RN [5]
RP FUNCTION, DISRUPTION PHENOTYPE, AND TISSUE SPECIFICITY.
RX PubMed=31862898; DOI=10.1038/s41419-019-2186-9;
RA Xu Y.L., Ding C.L., Qian C.L., Qi Z.T., Wang W.;
RT "Retinoid acid induced 16 deficiency aggravates colitis and colitis-
RT associated tumorigenesis in mice.";
RL Cell Death Dis. 10:958-958(2019).
CC -!- FUNCTION: Able to activate MAPK/ERK and TGFB signaling pathways (By
CC similarity). May regulate the activity of genes involved in intestinal
CC barrier function and immunoprotective inflammation (PubMed:31862898).
CC May play a role in cell proliferation (By similarity).
CC {ECO:0000250|UniProtKB:Q86V87, ECO:0000269|PubMed:31862898}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q80YR2-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q80YR2-2; Sequence=VSP_024588, VSP_024589;
CC -!- TISSUE SPECIFICITY: Expressed in colon. {ECO:0000269|PubMed:31862898}.
CC -!- DISRUPTION PHENOTYPE: Mutants are viable, fertile with no apparent
CC defects. Mice are more susceptibility to colitis induced by dextran
CC sodium sulfate (DSS) than wild type littermates (PubMed:31862898). They
CC display significantly increased tumor burden compared with WT mice
CC assessed in colitis-associated colorectal cancer model induced by
CC azoxymethane (AOM)-DSS (PubMed:31862898).
CC {ECO:0000269|PubMed:31862898}.
CC -!- SIMILARITY: Belongs to the FHIP family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH50861.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAC41057.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AC154563; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC050861; AAH50861.1; ALT_INIT; mRNA.
DR EMBL; BC058108; AAH58108.1; -; mRNA.
DR EMBL; AK090035; BAC41057.1; ALT_FRAME; mRNA.
DR CCDS; CCDS49537.1; -. [Q80YR2-1]
DR RefSeq; NP_919326.1; NM_194345.1. [Q80YR2-1]
DR AlphaFoldDB; Q80YR2; -.
DR BioGRID; 232057; 1.
DR IntAct; Q80YR2; 1.
DR STRING; 10090.ENSMUSP00000022690; -.
DR PhosphoSitePlus; Q80YR2; -.
DR EPD; Q80YR2; -.
DR MaxQB; Q80YR2; -.
DR PaxDb; Q80YR2; -.
DR PeptideAtlas; Q80YR2; -.
DR PRIDE; Q80YR2; -.
DR ProteomicsDB; 275715; -. [Q80YR2-1]
DR ProteomicsDB; 275716; -. [Q80YR2-2]
DR Antibodypedia; 9275; 103 antibodies from 23 providers.
DR Ensembl; ENSMUST00000022690; ENSMUSP00000022690; ENSMUSG00000022095. [Q80YR2-1]
DR GeneID; 239170; -.
DR KEGG; mmu:239170; -.
DR UCSC; uc007uol.2; mouse. [Q80YR2-1]
DR CTD; 64760; -.
DR MGI; MGI:3036290; Fam160b2.
DR VEuPathDB; HostDB:ENSMUSG00000022095; -.
DR eggNOG; KOG3695; Eukaryota.
DR GeneTree; ENSGT00950000182936; -.
DR HOGENOM; CLU_023718_0_0_1; -.
DR InParanoid; Q80YR2; -.
DR OMA; CDHLIME; -.
DR OrthoDB; 266554at2759; -.
DR PhylomeDB; Q80YR2; -.
DR TreeFam; TF313941; -.
DR BioGRID-ORCS; 239170; 1 hit in 72 CRISPR screens.
DR ChiTaRS; Fam160b2; mouse.
DR PRO; PR:Q80YR2; -.
DR Proteomes; UP000000589; Chromosome 14.
DR RNAct; Q80YR2; protein.
DR Bgee; ENSMUSG00000022095; Expressed in otolith organ and 219 other tissues.
DR Genevisible; Q80YR2; MM.
DR InterPro; IPR019384; FHIP.
DR InterPro; IPR045669; FHIP_C.
DR InterPro; IPR045668; FHIP_KELAA_motif.
DR PANTHER; PTHR21705; PTHR21705; 1.
DR Pfam; PF19314; DUF5917; 1.
DR Pfam; PF19311; KELAA; 1.
DR Pfam; PF10257; RAI16-like; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Reference proteome.
FT CHAIN 1..744
FT /note="FHF complex subunit HOOK interacting protein 2B"
FT /id="PRO_0000284646"
FT REGION 184..213
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 510..530
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 540..544
FT /note="SFLCL -> RWEEG (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_024588"
FT VAR_SEQ 545..744
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_024589"
FT CONFLICT 423
FT /note="H -> R (in Ref. 3; BAC41057)"
FT /evidence="ECO:0000305"
FT CONFLICT 575
FT /note="S -> R (in Ref. 2; AAH58108)"
FT /evidence="ECO:0000305"
FT CONFLICT 698
FT /note="E -> G (in Ref. 3; BAC41057)"
FT /evidence="ECO:0000305"
FT CONFLICT 736
FT /note="F -> C (in Ref. 3; BAC41057)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 744 AA; 82456 MW; 00D89D62589F7F26 CRC64;
MLSRLGALLQ EAVGAREPSI DLLQAFVEHW KGITHYYIES TDENTPAKKT DIPWRLKQML
DILVYEEKQQ ASSGEAGPCL EYLLQHKILE TLCTLGKAEY PPGMRQQVFQ FFSKVLSQVQ
HPLLHYLSVH RPVQKLLRLG GTVPGSLTEK EEVQFTSVLC SKIQQDPELL AYILEGKKII
GKKKTAREST APPKDIAGYR DKDCPHSDAL NRDPGLDKEH CGVPALSIHL PAETEGPENG
PGESNLITSL LGLCKSKKSR LALKAQENIL LLVSVASPAA ATYLTQSTSC CMAIAEHLCQ
LYRSMPACLD PADIATLEGI SWRLPSAPSD ETAFPGKEAL AAFLGWFDYC DHLITEAHTV
VADALAKAVA EKLFVETLQP QLLHVSEQSI LTSTALLTAL LRQLRSPALL QEAMTFLLGT
DQHPAAIEDS PHTLGTHLIM HCDHLSDEIS IATLRLFEEL LQKPHEQAIR SLVLQNLEGR
LYVARGSPEP ESYEDTLDLE EDPYFTDGFL DSGLQPSTKP PPAPATSSDG KTAVTEIVNS
FLCLVPEEAK TSAFLEENGY DTYVHDAYGL FQECSSRVAH WGWPLGPAPL DSHEPERPFF
EGRFLQVLFD RIARILDQPY SLNLQVTSVL SRLALFPHPH IHEYLLDPYI SLAPGCRSLF
SVLVRVIGDL MQRIQRVPQF SGKLLLVRKQ LMGQVPGEHL DHQTLLQGVV VLEEFCKELA
AIAFVKFPPH GPYLNFSPPP EGQV
