HYCCI_MOUSE
ID HYCCI_MOUSE Reviewed; 521 AA.
AC Q6P9N1; D3Z481; Q3TTP7; Q99NC4;
DT 11-OCT-2005, integrated into UniProtKB/Swiss-Prot.
DT 17-FEB-2016, sequence version 3.
DT 03-AUG-2022, entry version 118.
DE RecName: Full=Hyccin;
DE AltName: Full=Down-regulated by CTNNB1 protein A;
DE AltName: Full=Protein FAM126A;
GN Name=Fam126a; Synonyms=Drctnnb1a;
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] (ISOFORM 1), AND INDUCTION.
RC TISSUE=Spleen;
RX PubMed=10910037;
RA Kawasoe T., Furukawa Y., Daigo Y., Nishiwaki T., Ishiguro H., Fujita M.,
RA Satoh S., Miwa N., Nagasawa Y., Miyoshi Y., Ogawa M., Nakamura Y.;
RT "Isolation and characterization of a novel human gene, DRCTNNB1A, the
RT expression of which is down-regulated by beta-catenin.";
RL Cancer Res. 60:3354-3358(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=C57BL/6J; TISSUE=Testis;
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].
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=C57BL/6J; 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).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-453, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA Thibault P.;
RT "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL Immunity 30:143-154(2009).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-321; SER-415; SER-453 AND
RP SER-465, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Heart, Kidney, Lung, and 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).
RN [7]
RP TISSUE SPECIFICITY.
RX PubMed=22461884; DOI=10.1371/journal.pone.0032180;
RA Gazzerro E., Baldassari S., Giacomini C., Musante V., Fruscione F.,
RA La Padula V., Biancheri R., Scarfi S., Prada V., Sotgia F., Duncan I.D.,
RA Zara F., Werner H.B., Lisanti M.P., Nobbio L., Corradi A., Minetti C.;
RT "Hyccin, the Molecule Mutated in the Leukodystrophy Hypomyelination and
RT Congenital Cataract (HCC), Is a Neuronal Protein.";
RL PLoS ONE 7:E32180-E32180(2012).
RN [8]
RP DISRUPTION PHENOTYPE, AND TISSUE SPECIFICITY.
RX PubMed=26571211; DOI=10.1038/ncb3271;
RA Baskin J.M., Wu X., Christiano R., Oh M.S., Schauder C.M., Gazzerro E.,
RA Messa M., Baldassari S., Assereto S., Biancheri R., Zara F., Minetti C.,
RA Raimondi A., Simons M., Walther T.C., Reinisch K.M., De Camilli P.;
RT "The leukodystrophy protein FAM126A (hyccin) regulates PtdIns(4)P synthesis
RT at the plasma membrane.";
RL Nat. Cell Biol. 18:132-138(2016).
CC -!- FUNCTION: Component of a complex required to localize
CC phosphatidylinositol 4-kinase (PI4K) to the plasma membrane. The
CC complex acts as a regulator of phosphatidylinositol 4-phosphate
CC (PtdIns(4)P) synthesis. FAM126A plays a key role in oligodendrocytes
CC formation, a cell type with expanded plasma membrane that requires
CC generation of PtdIns(4)P. Its role in oligodendrocytes formation
CC probably explains its importance in myelination of the central and
CC peripheral nervous system. May also have a role in the beta-catenin/Lef
CC signaling pathway. {ECO:0000250|UniProtKB:Q9BYI3}.
CC -!- SUBUNIT: Component of a phosphatidylinositol 4-kinase (PI4K) complex,
CC composed of PI4KA, EFR3 (EFR3A or EFR3B), TTC7 (TTC7A or TTC7B) and
CC FAM126 (FAM126A or FAM126B). Interacts with TTC7 (TTC7A or TTC7B),
CC interaction is direct. {ECO:0000250|UniProtKB:Q9BYI3}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
CC {ECO:0000250|UniProtKB:Q9BYI3}. Cell membrane
CC {ECO:0000250|UniProtKB:Q9BYI3}. Note=Localizes to the cytosol and is
CC recruited to the plasma membrane following interaction with other
CC components of the phosphatidylinositol 4-kinase (PI4K) complex.
CC {ECO:0000250|UniProtKB:Q9BYI3}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q6P9N1-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q6P9N1-2; Sequence=VSP_058131, VSP_058132;
CC Name=3;
CC IsoId=Q6P9N1-3; Sequence=VSP_058130, VSP_058133;
CC -!- TISSUE SPECIFICITY: Predominantly expressed in the central nervous
CC system, where it is found in neurons but not in myelinating cells.
CC Lower abundance is observed in peripheral neurons, where it is
CC detectable only at early postnatal ages (PubMed:22461884). Expressed in
CC both oligodendrocytes and neurons (PubMed:26571211).
CC {ECO:0000269|PubMed:22461884, ECO:0000269|PubMed:26571211}.
CC -!- INDUCTION: Down-regulated by beta-catenin.
CC {ECO:0000269|PubMed:10910037}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype. Lysates from total brain
CC and optic nerve (a pure white matter tract) display a selective
CC decrease of Ttc7a and Efr3a protein levels.
CC {ECO:0000269|PubMed:26571211}.
CC -!- SIMILARITY: Belongs to the FAM126 family. {ECO:0000305}.
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DR EMBL; AB030242; BAB39850.1; -; mRNA.
DR EMBL; AK161265; BAE36278.1; -; mRNA.
DR EMBL; AC115786; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC117663; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC056381; AAH56381.1; -; mRNA.
DR EMBL; BC060692; AAH60692.1; -; mRNA.
DR CCDS; CCDS19113.1; -. [Q6P9N1-1]
DR CCDS; CCDS80221.1; -. [Q6P9N1-2]
DR RefSeq; NP_001297400.1; NM_001310471.1. [Q6P9N1-2]
DR RefSeq; NP_444320.2; NM_053090.3. [Q6P9N1-1]
DR RefSeq; XP_006535885.1; XM_006535822.2. [Q6P9N1-3]
DR RefSeq; XP_011248100.1; XM_011249798.2. [Q6P9N1-1]
DR RefSeq; XP_017176677.1; XM_017321188.1. [Q6P9N1-2]
DR AlphaFoldDB; Q6P9N1; -.
DR SMR; Q6P9N1; -.
DR STRING; 10090.ENSMUSP00000030849; -.
DR iPTMnet; Q6P9N1; -.
DR PhosphoSitePlus; Q6P9N1; -.
DR EPD; Q6P9N1; -.
DR jPOST; Q6P9N1; -.
DR MaxQB; Q6P9N1; -.
DR PaxDb; Q6P9N1; -.
DR PeptideAtlas; Q6P9N1; -.
DR PRIDE; Q6P9N1; -.
DR ProteomicsDB; 273292; -. [Q6P9N1-1]
DR ProteomicsDB; 273293; -. [Q6P9N1-2]
DR ProteomicsDB; 273294; -. [Q6P9N1-3]
DR Antibodypedia; 53361; 65 antibodies from 19 providers.
DR Ensembl; ENSMUST00000030849; ENSMUSP00000030849; ENSMUSG00000028995. [Q6P9N1-1]
DR Ensembl; ENSMUST00000101513; ENSMUSP00000099050; ENSMUSG00000028995. [Q6P9N1-2]
DR Ensembl; ENSMUST00000115109; ENSMUSP00000110761; ENSMUSG00000028995. [Q6P9N1-3]
DR GeneID; 84652; -.
DR KEGG; mmu:84652; -.
DR UCSC; uc008wqu.1; mouse.
DR UCSC; uc008wqv.1; mouse. [Q6P9N1-1]
DR CTD; 84668; -.
DR MGI; MGI:2149839; Fam126a.
DR VEuPathDB; HostDB:ENSMUSG00000028995; -.
DR eggNOG; KOG4688; Eukaryota.
DR GeneTree; ENSGT00390000011295; -.
DR InParanoid; Q6P9N1; -.
DR OMA; TAGESCK; -.
DR OrthoDB; 673408at2759; -.
DR PhylomeDB; Q6P9N1; -.
DR TreeFam; TF317153; -.
DR BioGRID-ORCS; 84652; 2 hits in 73 CRISPR screens.
DR ChiTaRS; Fam126a; mouse.
DR PRO; PR:Q6P9N1; -.
DR Proteomes; UP000000589; Chromosome 5.
DR RNAct; Q6P9N1; protein.
DR Bgee; ENSMUSG00000028995; Expressed in fetal liver hematopoietic progenitor cell and 247 other tissues.
DR ExpressionAtlas; Q6P9N1; baseline and differential.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR GO; GO:0043005; C:neuron projection; IDA:MGI.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0042552; P:myelination; IMP:UniProtKB.
DR GO; GO:0046854; P:phosphatidylinositol phosphate biosynthetic process; ISS:UniProtKB.
DR GO; GO:0072659; P:protein localization to plasma membrane; ISS:UniProtKB.
DR InterPro; IPR018619; Hyccin.
DR PANTHER; PTHR31220; PTHR31220; 1.
DR Pfam; PF09790; Hyccin; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell membrane; Cytoplasm; Membrane; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..521
FT /note="Hyccin"
FT /id="PRO_0000080006"
FT REGION 355..413
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 355..383
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 386..410
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 306
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9BYI3"
FT MOD_RES 321
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 415
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 422
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9BYI3"
FT MOD_RES 433
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9BYI3"
FT MOD_RES 453
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19144319,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 465
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT VAR_SEQ 331..420
FT /note="GDTELTGQEELMDITEVDEGFYSRAASSTSQSGLSNSSHNCSNKTSVGKNQR
FT RSGGSKAGAKERETAGESCRDHFARKQTQRAQSENLEL -> EQPESSCAAAAEAGILV
FT IPEISVTHVSGERTGNGEKGRALGDIDAQHMQGVQETATDPRSESRGLPELRRQKSVRK
FT MMEDGMSTAGRVQF (in isoform 3)"
FT /id="VSP_058130"
FT VAR_SEQ 332..370
FT /note="DTELTGQEELMDITEVDEGFYSRAASSTSQSGLSNSSHN -> GSKGSRQSR
FT PTIDSDTITCWNLQSRFKYDHNVQKSVSKI (in isoform 2)"
FT /id="VSP_058131"
FT VAR_SEQ 371..521
FT /note="Missing (in isoform 2)"
FT /id="VSP_058132"
FT VAR_SEQ 421..521
FT /note="Missing (in isoform 3)"
FT /id="VSP_058133"
FT CONFLICT 39
FT /note="T -> S (in Ref. 1; BAB39850)"
SQ SEQUENCE 521 AA; 57321 MW; FD4FF7C29DD1B1E2 CRC64;
MFTSEIGVVE EWLSEFKTLP ETSLPNYATN LKDKSSLVTS LYKVIQEPQS ELLEPVCHQL
FEFYRSGEEQ LLRFTLQFLP ELMWCYLAVS ASRDVHSSGC IEALLLGVYN LEIVDKHGHS
KVLSFTIPSL SKPSVYHEPS SIGSMALTES ALSQHGLSKV VYSGPHPQRE MLTAQNRFEV
LTFLLLCYNA ALTYMPSVSL QSLCQICSRI CVCGYPRQHV RKYRGVSSRI PISSGFMVQM
LTGVYFAIYN GEWDLAQKAL DDIIYRAQLE LYPEPLLVAN AIKASLPHGA MKSSKEGTRC
IQVEITPTSS RISRNAVTSM SIRGHRWKRH GDTELTGQEE LMDITEVDEG FYSRAASSTS
QSGLSNSSHN CSNKTSVGKN QRRSGGSKAG AKERETAGES CRDHFARKQT QRAQSENLEL
LSLKRLTLTS SQSLPKPSSQ GLAKTAATVF SKSFEQVSGA PVPRSPSPAI GCVAGADANR
FSACSLQEEK LIYVSERTEL AVKCQAGQQG PPSISVTLSA E
