ID   AKTIP_MOUSE             Reviewed;         292 AA.
AC   Q64362; Q3TYE3;
DT   11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 149.
DE   RecName: Full=AKT-interacting protein;
DE   AltName: Full=FT1;
DE   AltName: Full=Fused toes protein;
GN   Name=Aktip; Synonyms=Fif, Ft1, Fts;
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 [MRNA], AND TISSUE SPECIFICITY.
RC   STRAIN=C57BL/6J;
RX   PubMed=9383278; DOI=10.1007/s003359900604;
RA   Lesche R., Peetz A., van der Hoeven F., Ruether U.;
RT   "Ft1, a novel gene related to ubiquitin conjugating enzymes, is deleted in
RT   the Fused toes mouse mutation.";
RL   Mamm. Genome 8:879-883(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Amnion, and Visual cortex;
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   [3]
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 (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N; TISSUE=Mammary tumor;
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   [5]
RP   DISEASE.
RX   PubMed=7956835; DOI=10.1242/dev.120.9.2601;
RA   van der Hoeven F., Schimmang T., Volkmann A., Mattei M.-G., Kyewski B.,
RA   Ruether U.;
RT   "Programmed cell death is affected in the novel mouse mutant Fused toes
RT   (Ft).";
RL   Development 120:2601-2607(1994).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-30, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, and
RC   Pancreas;
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: Component of the FTS/Hook/FHIP complex (FHF complex). The FHF
CC       complex may function to promote vesicle trafficking and/or fusion via
CC       the homotypic vesicular protein sorting complex (the HOPS complex).
CC       Regulates apoptosis by enhancing phosphorylation and activation of
CC       AKT1. Increases release of TNFSF6 via the AKT1/GSK3B/NFATC1 signaling
CC       cascade. FHF complex promotes the distribution of AP-4 complex to the
CC       perinuclear area of the cell. {ECO:0000250|UniProtKB:Q9H8T0}.
CC   -!- SUBUNIT: Component of the FTS/Hook/FHIP complex (FHF complex), composed
CC       of AKTIP/FTS, FHIP1B, and one or more members of the Hook family of
CC       proteins HOOK1, HOOK2, and HOOK3. Interacts directly with HOOK1, HOOK2
CC       and HOOK3. The FHF complex associates with the homotypic vesicular
CC       sorting complex (the HOPS complex). Also interacts with AKT1. May
CC       interact with FHIP1A. {ECO:0000250|UniProtKB:Q9H8T0}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9H8T0}. Cell
CC       membrane {ECO:0000250|UniProtKB:Q9H8T0}; Peripheral membrane protein
CC       {ECO:0000250|UniProtKB:Q9H8T0}.
CC   -!- TISSUE SPECIFICITY: Ubiquitous. Highest expression in kidney, testis
CC       and brain and lowest in spleen and liver. {ECO:0000269|PubMed:9383278}.
CC   -!- DISEASE: Note=Defects in Aktip are a cause of embryonic death in
CC       homozygous animals. Death occurs at about 10 days of development.
CC       Symptoms include loss of left-right asymmetry, malformation of the
CC       developing brain and of the spinal cord, syndactyly and polydactyly.
CC       Heterozygous animals are characterized by polydactyly and thymic
CC       hyperplasia. {ECO:0000269|PubMed:7956835}.
CC   -!- SIMILARITY: Belongs to the ubiquitin-conjugating enzyme family. FTS
CC       subfamily. {ECO:0000255|PROSITE-ProRule:PRU00388}.
CC   -!- CAUTION: Lacks the conserved Cys residue necessary for ubiquitin-
CC       conjugating enzyme E2 activity. {ECO:0000305}.
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DR   EMBL; Z67963; CAA91902.1; -; mRNA.
DR   EMBL; X71978; CAA50800.1; -; mRNA.
DR   EMBL; AK146459; BAE27187.1; -; mRNA.
DR   EMBL; AK158704; BAE34620.1; -; mRNA.
DR   EMBL; CH466525; EDL11072.1; -; Genomic_DNA.
DR   EMBL; CH466525; EDL11073.1; -; Genomic_DNA.
DR   EMBL; BC008130; AAH08130.1; -; mRNA.
DR   CCDS; CCDS22519.1; -.
DR   PIR; S33513; S33513.
DR   RefSeq; NP_001289195.1; NM_001302266.1.
DR   RefSeq; NP_001289196.1; NM_001302267.1.
DR   RefSeq; NP_001289197.1; NM_001302268.1.
DR   RefSeq; NP_001289266.1; NM_001302337.1.
DR   RefSeq; NP_034371.1; NM_010241.5.
DR   RefSeq; XP_017168061.1; XM_017312572.1.
DR   RefSeq; XP_017168062.1; XM_017312573.1.
DR   AlphaFoldDB; Q64362; -.
DR   SMR; Q64362; -.
DR   BioGRID; 199761; 2.
DR   STRING; 10090.ENSMUSP00000113769; -.
DR   iPTMnet; Q64362; -.
DR   PhosphoSitePlus; Q64362; -.
DR   jPOST; Q64362; -.
DR   MaxQB; Q64362; -.
DR   PaxDb; Q64362; -.
DR   PRIDE; Q64362; -.
DR   ProteomicsDB; 282067; -.
DR   Antibodypedia; 28404; 281 antibodies from 28 providers.
DR   DNASU; 14339; -.
DR   Ensembl; ENSMUST00000109609; ENSMUSP00000105238; ENSMUSG00000031667.
DR   Ensembl; ENSMUST00000120213; ENSMUSP00000112375; ENSMUSG00000031667.
DR   Ensembl; ENSMUST00000120349; ENSMUSP00000113769; ENSMUSG00000031667.
DR   Ensembl; ENSMUST00000125257; ENSMUSP00000119277; ENSMUSG00000031667.
DR   GeneID; 14339; -.
DR   KEGG; mmu:14339; -.
DR   UCSC; uc009msl.2; mouse.
DR   CTD; 64400; -.
DR   MGI; MGI:3693832; Aktip.
DR   VEuPathDB; HostDB:ENSMUSG00000031667; -.
DR   eggNOG; KOG0429; Eukaryota.
DR   GeneTree; ENSGT00390000010125; -.
DR   HOGENOM; CLU_083049_0_0_1; -.
DR   InParanoid; Q64362; -.
DR   OMA; WGFPEWR; -.
DR   OrthoDB; 1226125at2759; -.
DR   PhylomeDB; Q64362; -.
DR   TreeFam; TF314386; -.
DR   BioGRID-ORCS; 14339; 2 hits in 72 CRISPR screens.
DR   ChiTaRS; Aktip; mouse.
DR   PRO; PR:Q64362; -.
DR   Proteomes; UP000000589; Chromosome 8.
DR   RNAct; Q64362; protein.
DR   Bgee; ENSMUSG00000031667; Expressed in right kidney and 284 other tissues.
DR   ExpressionAtlas; Q64362; baseline and differential.
DR   Genevisible; Q64362; MM.
DR   GO; GO:0005829; C:cytosol; IEA:GOC.
DR   GO; GO:0070695; C:FHF complex; ISS:UniProtKB.
DR   GO; GO:0030897; C:HOPS complex; ISO:MGI.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR   GO; GO:0061631; F:ubiquitin conjugating enzyme activity; IBA:GO_Central.
DR   GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR   GO; GO:0045022; P:early endosome to late endosome transport; ISS:UniProtKB.
DR   GO; GO:0007032; P:endosome organization; ISS:UniProtKB.
DR   GO; GO:0008333; P:endosome to lysosome transport; ISS:UniProtKB.
DR   GO; GO:0007040; P:lysosome organization; ISS:UniProtKB.
DR   GO; GO:0032092; P:positive regulation of protein binding; ISO:MGI.
DR   GO; GO:0001934; P:positive regulation of protein phosphorylation; ISO:MGI.
DR   GO; GO:1905719; P:protein localization to perinuclear region of cytoplasm; ISS:UniProtKB.
DR   GO; GO:0000209; P:protein polyubiquitination; IBA:GO_Central.
DR   GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR   Gene3D; 3.10.110.10; -; 1.
DR   InterPro; IPR000608; UBQ-conjugat_E2.
DR   InterPro; IPR016135; UBQ-conjugating_enzyme/RWD.
DR   Pfam; PF00179; UQ_con; 1.
DR   SUPFAM; SSF54495; SSF54495; 1.
DR   PROSITE; PS50127; UBC_2; 1.
PE   1: Evidence at protein level;
KW   Apoptosis; Cell membrane; Cytoplasm; Membrane; Phosphoprotein;
KW   Protein transport; Reference proteome; Transport.
FT   CHAIN           1..292
FT                   /note="AKT-interacting protein"
FT                   /id="PRO_0000082610"
FT   DOMAIN          74..222
FT                   /note="UBC core"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00388"
FT   REGION          1..63
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         30
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
SQ   SEQUENCE   292 AA;  32942 MW;  A5FFC7F9053B1E3B CRC64;
     MNPLWSMSAG SVRKRAEGEE KTLAGDVKTS PPRSAPKKQL PSIPKNALPI AKPTSPAPAA
     QSTNGTHASY GPFYLEYSLL AEFTLVVKQK LPGVYVQPSY RSALVWFGVI FIRHGLYQDG
     VFKFTVYIPD NYPDGDCPRL LFDIPVFHPL VDPTSGELDV KRAFAKWRRN HNHIWQVLMY
     ARRVFYKIDT TSPLNPEAAV LYEKDIQLFK SKVVDSVKVC TARLFDQPKI EDPYAISFSP
     WNPSVHDEAR EKMLTQKKPD EQHNKSVHVA GLSWVKPGSV QPFSKEEKTV AT