F161A_MOUSE
ID F161A_MOUSE Reviewed; 448 AA.
AC Q8QZV6;
DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 99.
DE RecName: Full=Protein FAM161A;
GN Name=Fam161a;
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=FVB/N; TISSUE=Eye, and Kidney;
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 [2]
RP TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=20705278; DOI=10.1016/j.ajhg.2010.07.018;
RA Langmann T., Di Gioia S.A., Rau I., Stohr H., Maksimovic N.S., Corbo J.C.,
RA Renner A.B., Zrenner E., Kumaramanickavel G., Karlstetter M.,
RA Arsenijevic Y., Weber B.H., Gal A., Rivolta C.;
RT "Nonsense mutations in FAM161A cause RP28-associated recessive retinitis
RT pigmentosa.";
RL Am. J. Hum. Genet. 87:376-381(2010).
RN [3]
RP TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=20705279; DOI=10.1016/j.ajhg.2010.07.022;
RA Bandah-Rozenfeld D., Mizrahi-Meissonnier L., Farhy C., Obolensky A.,
RA Chowers I., Pe'er J., Merin S., Ben-Yosef T., Ashery-Padan R., Banin E.,
RA Sharon D.;
RT "Homozygosity mapping reveals null mutations in FAM161A as a cause of
RT autosomal-recessive retinitis pigmentosa.";
RL Am. J. Hum. Genet. 87:382-391(2010).
RN [4]
RP SUBCELLULAR LOCATION.
RX PubMed=22940612; DOI=10.1093/hmg/dds368;
RA Di Gioia S.A., Letteboer S.J., Kostic C., Bandah-Rozenfeld D.,
RA Hetterschijt L., Sharon D., Arsenijevic Y., Roepman R., Rivolta C.;
RT "FAM161A, associated with retinitis pigmentosa, is a component of the
RT cilia-basal body complex and interacts with proteins involved in
RT ciliopathies.";
RL Hum. Mol. Genet. 21:5174-5184(2012).
RN [5]
RP SUBCELLULAR LOCATION.
RX PubMed=22791751; DOI=10.1093/hmg/dds268;
RA Zach F., Grassmann F., Langmann T., Sorusch N., Wolfrum U., Stohr H.;
RT "The retinitis pigmentosa 28 protein FAM161A is a novel ciliary protein
RT involved in intermolecular protein interaction and microtubule
RT association.";
RL Hum. Mol. Genet. 21:4573-4586(2012).
CC -!- FUNCTION: Involved in ciliogenesis. {ECO:0000250|UniProtKB:Q3B820}.
CC -!- SUBUNIT: Interacts (via C-terminus) with microtubules. Interacts with
CC LCA5, CEP290 and SDCCAG8. Interacts with FAM161B. Interacts with POC1B.
CC Interacts with CEP78. {ECO:0000250|UniProtKB:Q3B820}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, cilium basal body. Cell
CC projection, cilium. Note=Localized in the region between the outer and
CC inner photoreceptor segments, corresponding to the photoreceptor
CC connecting cilium.
CC -!- TISSUE SPECIFICITY: Expressed in the retina.
CC {ECO:0000269|PubMed:20705278, ECO:0000269|PubMed:20705279}.
CC -!- DEVELOPMENTAL STAGE: Expressed at low levels from 12.5 to 16.5 dpc in
CC the retinal progenitor cells of the optic cup, as well as in the
CC posterior compartment of the lens. Expression drops in the retina at
CC birth. At P5, highly expressed in the postmigratory photoreceptor
CC precursors at the apical side of the outer nuclear layer. At P10,
CC present in the outer nuclear layer and in the inner segments of
CC photoreceptors and in the outer plexiform layer (at protein level). In
CC adult animals, at P30, reaches a well-defined localization in the inner
CC segment of photoreceptors, as well as in the outer plexiform layer (at
CC protein level). Completely absent from the outer segment of
CC photoreceptors (at protein level). {ECO:0000269|PubMed:20705278,
CC ECO:0000269|PubMed:20705279}.
CC -!- SIMILARITY: Belongs to the FAM161 family. {ECO:0000305}.
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DR EMBL; BC024460; AAH24460.1; -; mRNA.
DR EMBL; BC026495; AAH26495.1; -; mRNA.
DR RefSeq; NP_082948.2; NM_028672.2.
DR AlphaFoldDB; Q8QZV6; -.
DR STRING; 10090.ENSMUSP00000063091; -.
DR PhosphoSitePlus; Q8QZV6; -.
DR MaxQB; Q8QZV6; -.
DR PaxDb; Q8QZV6; -.
DR PRIDE; Q8QZV6; -.
DR ProteomicsDB; 271825; -.
DR Antibodypedia; 30688; 80 antibodies from 11 providers.
DR DNASU; 73873; -.
DR Ensembl; ENSMUST00000058269; ENSMUSP00000063091; ENSMUSG00000049811.
DR Ensembl; ENSMUST00000109557; ENSMUSP00000105184; ENSMUSG00000049811.
DR Ensembl; ENSMUST00000172602; ENSMUSP00000134485; ENSMUSG00000049811.
DR GeneID; 73873; -.
DR KEGG; mmu:73873; -.
DR UCSC; uc007ies.1; mouse.
DR CTD; 84140; -.
DR MGI; MGI:1921123; Fam161a.
DR VEuPathDB; HostDB:ENSMUSG00000049811; -.
DR eggNOG; ENOG502QRC3; Eukaryota.
DR GeneTree; ENSGT00940000157824; -.
DR InParanoid; Q8QZV6; -.
DR OrthoDB; 1085171at2759; -.
DR BioGRID-ORCS; 73873; 1 hit in 71 CRISPR screens.
DR PRO; PR:Q8QZV6; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; Q8QZV6; protein.
DR Bgee; ENSMUSG00000049811; Expressed in retinal neural layer and 217 other tissues.
DR ExpressionAtlas; Q8QZV6; baseline and differential.
DR GO; GO:0000235; C:astral microtubule; ISO:MGI.
DR GO; GO:0005814; C:centriole; IDA:UniProtKB.
DR GO; GO:0005813; C:centrosome; ISO:MGI.
DR GO; GO:0036064; C:ciliary basal body; IDA:UniProtKB.
DR GO; GO:0072686; C:mitotic spindle; ISO:MGI.
DR GO; GO:0097431; C:mitotic spindle pole; ISO:MGI.
DR GO; GO:0097733; C:photoreceptor cell cilium; IDA:UniProtKB.
DR GO; GO:0032391; C:photoreceptor connecting cilium; IDA:UniProtKB.
DR GO; GO:0001917; C:photoreceptor inner segment; IDA:UniProtKB.
DR GO; GO:0005876; C:spindle microtubule; ISO:MGI.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0008017; F:microtubule binding; ISO:MGI.
DR GO; GO:0060271; P:cilium assembly; ISS:UniProtKB.
DR GO; GO:0044782; P:cilium organization; IMP:MGI.
DR GO; GO:1901985; P:positive regulation of protein acetylation; ISO:MGI.
DR InterPro; IPR019579; FAM161A/B.
DR Pfam; PF10595; UPF0564; 1.
PE 1: Evidence at protein level;
KW Cell projection; Cilium; Cilium biogenesis/degradation; Coiled coil;
KW Cytoplasm; Cytoskeleton; Isopeptide bond; Reference proteome;
KW Ubl conjugation.
FT CHAIN 1..448
FT /note="Protein FAM161A"
FT /id="PRO_0000329053"
FT REGION 25..82
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 287..310
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 362..414
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 135..207
FT /evidence="ECO:0000255"
FT COMPBIAS 25..66
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CROSSLNK 350
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q3B820"
SQ SEQUENCE 448 AA; 52029 MW; FFADA9805D1CD115 CRC64;
MSKLEKMYQD KLNIKDIQAG FIRDGISDSS SSSASEKSCS HPALSVTSLS EPDLDGSSSL
STTTDEGLPD LEEKTPGESS AMVHAQELIN NMWNDFSVED YIQYDSDSRT AKKKRKKAKS
LTPKITVPVP FEMTVREQNR REKALSARSD LETKLLKRDE DDAECKKKFR ANPVPSCVLL
PLYEDLVKQS EERRKKARER NRAALLASLK PFKFIAREEQ KQAVREKKLR DLFRAKRKTN
QFKAKPVPRF IYRPAASDKP KEEELYGDSR MLPKVRDLLQ NSPWPSRSAC RRFRDPRSPA
KPRGKHRRRC LRRDGDLEKW KEPFSEYSFL KCPMLCEECC LHESPCDSDK RQKLLADIRA
DEEILRETRR PGRSPRRKSP GRSSNPKPRP HECSPPMPTA SSRGREQAIR RSEKARMREY
WQELEEQEEK LQKRPMLFER VTQVVFIG
