F161A_RAT
ID F161A_RAT Reviewed; 422 AA.
AC Q6AY14;
DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-2004, sequence version 1.
DT 03-AUG-2022, entry version 95.
DE RecName: Full=Protein FAM161A;
GN Name=Fam161a;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis;
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 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).
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
CC {ECO:0000269|PubMed:22940612}. Cell projection, cilium
CC {ECO:0000269|PubMed:22940612}. Note=Localized in the region between the
CC outer and inner photoreceptor segments, corresponding to the
CC photoreceptor connecting cilium.
CC -!- TISSUE SPECIFICITY: Expressed in the retina and kidney.
CC {ECO:0000269|PubMed:22940612}.
CC -!- SIMILARITY: Belongs to the FAM161 family. {ECO:0000305}.
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DR EMBL; BC079233; AAH79233.1; -; mRNA.
DR RefSeq; NP_001013898.2; NM_001013876.2.
DR AlphaFoldDB; Q6AY14; -.
DR SMR; Q6AY14; -.
DR STRING; 10116.ENSRNOP00000013097; -.
DR PaxDb; Q6AY14; -.
DR GeneID; 289833; -.
DR KEGG; rno:289833; -.
DR UCSC; RGD:1304999; rat.
DR CTD; 84140; -.
DR RGD; 1304999; Fam161a.
DR VEuPathDB; HostDB:ENSRNOG00000009881; -.
DR eggNOG; ENOG502QRC3; Eukaryota.
DR InParanoid; Q6AY14; -.
DR OrthoDB; 1085171at2759; -.
DR PhylomeDB; Q6AY14; -.
DR TreeFam; TF321199; -.
DR PRO; PR:Q6AY14; -.
DR Proteomes; UP000002494; Chromosome 14.
DR Bgee; ENSRNOG00000009881; Expressed in testis and 5 other tissues.
DR ExpressionAtlas; Q6AY14; baseline and differential.
DR GO; GO:0000235; C:astral microtubule; ISO:RGD.
DR GO; GO:0005814; C:centriole; ISO:RGD.
DR GO; GO:0005813; C:centrosome; ISO:RGD.
DR GO; GO:0036064; C:ciliary basal body; IDA:UniProtKB.
DR GO; GO:0072686; C:mitotic spindle; ISO:RGD.
DR GO; GO:0097431; C:mitotic spindle pole; ISO:RGD.
DR GO; GO:0097733; C:photoreceptor cell cilium; ISO:RGD.
DR GO; GO:0032391; C:photoreceptor connecting cilium; IDA:UniProtKB.
DR GO; GO:0001917; C:photoreceptor inner segment; ISO:RGD.
DR GO; GO:0005876; C:spindle microtubule; ISO:RGD.
DR GO; GO:0042802; F:identical protein binding; ISO:RGD.
DR GO; GO:0008017; F:microtubule binding; ISO:RGD.
DR GO; GO:0060271; P:cilium assembly; ISS:UniProtKB.
DR GO; GO:0044782; P:cilium organization; ISO:RGD.
DR GO; GO:1901985; P:positive regulation of protein acetylation; ISO:RGD.
DR InterPro; IPR019579; FAM161A/B.
DR Pfam; PF10595; UPF0564; 1.
PE 2: Evidence at transcript level;
KW Cell projection; Cilium; Cilium biogenesis/degradation; Coiled coil;
KW Cytoplasm; Cytoskeleton; Isopeptide bond; Reference proteome;
KW Ubl conjugation.
FT CHAIN 1..422
FT /note="Protein FAM161A"
FT /id="PRO_0000329054"
FT REGION 22..74
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 133..158
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 256..312
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 360..422
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 136..198
FT /evidence="ECO:0000255"
FT COMPBIAS 22..61
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 268..282
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 401..416
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CROSSLNK 345
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q3B820"
FT CROSSLNK 361
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q3B820"
SQ SEQUENCE 422 AA; 48869 MW; 3993D5A40E7F1836 CRC64;
MVKLEKMYQD KLTMKDIQAA LVGDDSSSSA SEKSCSHPAL SATSLSEPDL DRSSSLSTTT
DELPDLEKKT PGEIGTRSYA KELINNMWND FSVEDYTQYD SDLQTAKKNR KKPKAWTPRI
TVPVPFEMTV REQKRREKAS DAQETREKML KRNEDDAECK KKFRANPVPS RLLLPLYEDL
VKQNEERRKK TRERSKAALL ASQKPFKFIA REEQKQAIRE KKLRELCRAK KKPKQFKARP
VPRFIYRPPA NVKPKREELY GDSRTQPKAR DVLQSSPWPS HSTYRAFRDP RSPAMPRGKH
RHRRLSPSDQ GLEKWKEPFS EQSFRNCPVL CDQCCLYESL CDSNKRQKIL ADIRMGEEIL
KETRRPNPSP RHKSPRRSAH ASARPCEYSP PMPTASSRGR EQAIRRSEKA RMKELARIGG
AR
