ANKS3_RAT
ID ANKS3_RAT Reviewed; 663 AA.
AC Q5M9H0;
DT 04-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-2005, sequence version 1.
DT 03-AUG-2022, entry version 115.
DE RecName: Full=Ankyrin repeat and SAM domain-containing protein 3;
GN Name=Anks3;
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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2 AND SER-5, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
RN [3]
RP INTERACTION WITH ANKS6.
RX PubMed=25671767; DOI=10.1038/ki.2015.17;
RA Yakulov T.A., Yasunaga T., Ramachandran H., Engel C., Mueller B., Hoff S.,
RA Dengjel J., Lienkamp S.S., Walz G.;
RT "Anks3 interacts with nephronophthisis proteins and is required for normal
RT renal development.";
RL Kidney Int. 87:1191-1200(2015).
CC -!- FUNCTION: May be involved in vasopressin signaling in the kidney.
CC {ECO:0000250|UniProtKB:Q9CZK6}.
CC -!- SUBUNIT: Homooligomer (By similarity). Interacts (via SAM domain) with
CC ANKS6 (via SAM domain) (PubMed:25671767). Interacts with BICC1 (By
CC similarity). Interacts with NPHP1 (By similarity). Interacts with NEK8
CC (By similarity). Interacts with HIF1AN (By similarity). Interacts with
CC NEK7; this interaction alters the subcellular distribution of NEK7 by
CC preventing its nuclear translocation (By similarity).
CC {ECO:0000250|UniProtKB:Q6ZW76, ECO:0000250|UniProtKB:Q9CZK6,
CC ECO:0000269|PubMed:25671767}.
CC -!- SUBCELLULAR LOCATION: Cell projection, cilium
CC {ECO:0000250|UniProtKB:Q9CZK6}. Cytoplasm
CC {ECO:0000250|UniProtKB:Q9CZK6}.
CC -!- DOMAIN: The SAM domain mediates homooligomerization.
CC {ECO:0000250|UniProtKB:Q6ZW76}.
CC -!- PTM: Hydroxylated at Asn-96, most probably by HIF1AN.
CC {ECO:0000250|UniProtKB:Q9CZK6}.
CC -!- PTM: Phosphorylations at Ser-5, Ser-225, Thr-318, Ser-319, Ser-366 and
CC Ser-369 occur in a NEK7-dependent manner.
CC {ECO:0000250|UniProtKB:Q9CZK6}.
CC -!- PTM: Polyubiquitinated. {ECO:0000250|UniProtKB:Q9CZK6}.
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DR EMBL; BC087062; AAH87062.1; -; mRNA.
DR RefSeq; NP_001009676.1; NM_001009676.1.
DR AlphaFoldDB; Q5M9H0; -.
DR SMR; Q5M9H0; -.
DR STRING; 10116.ENSRNOP00000004298; -.
DR iPTMnet; Q5M9H0; -.
DR PhosphoSitePlus; Q5M9H0; -.
DR PaxDb; Q5M9H0; -.
DR Ensembl; ENSRNOT00000004298; ENSRNOP00000004298; ENSRNOG00000003186.
DR GeneID; 302937; -.
DR KEGG; rno:302937; -.
DR UCSC; RGD:1305833; rat.
DR CTD; 124401; -.
DR RGD; 1305833; Anks3.
DR eggNOG; KOG0504; Eukaryota.
DR GeneTree; ENSGT00940000156610; -.
DR InParanoid; Q5M9H0; -.
DR OMA; NKGHHSK; -.
DR OrthoDB; 58543at2759; -.
DR PhylomeDB; Q5M9H0; -.
DR TreeFam; TF331487; -.
DR PRO; PR:Q5M9H0; -.
DR Proteomes; UP000002494; Chromosome 10.
DR Bgee; ENSRNOG00000003186; Expressed in frontal cortex and 20 other tissues.
DR ExpressionAtlas; Q5M9H0; baseline and differential.
DR Genevisible; Q5M9H0; RN.
DR GO; GO:0005929; C:cilium; ISO:RGD.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR Gene3D; 1.10.150.50; -; 1.
DR Gene3D; 1.25.40.20; -; 1.
DR InterPro; IPR002110; Ankyrin_rpt.
DR InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR InterPro; IPR001660; SAM.
DR InterPro; IPR013761; SAM/pointed_sf.
DR Pfam; PF12796; Ank_2; 2.
DR Pfam; PF00536; SAM_1; 1.
DR PRINTS; PR01415; ANKYRIN.
DR SMART; SM00248; ANK; 6.
DR SMART; SM00454; SAM; 1.
DR SUPFAM; SSF47769; SSF47769; 1.
DR SUPFAM; SSF48403; SSF48403; 1.
DR PROSITE; PS50297; ANK_REP_REGION; 1.
DR PROSITE; PS50088; ANK_REPEAT; 4.
DR PROSITE; PS50105; SAM_DOMAIN; 1.
PE 1: Evidence at protein level;
KW ANK repeat; Cell projection; Coiled coil; Cytoplasm; Hydroxylation;
KW Phosphoprotein; Reference proteome; Repeat; Ubl conjugation.
FT CHAIN 1..663
FT /note="Ankyrin repeat and SAM domain-containing protein 3"
FT /id="PRO_0000230779"
FT REPEAT 34..64
FT /note="ANK 1"
FT REPEAT 68..97
FT /note="ANK 2"
FT REPEAT 101..130
FT /note="ANK 3"
FT REPEAT 134..163
FT /note="ANK 4"
FT REPEAT 168..197
FT /note="ANK 5"
FT REPEAT 201..220
FT /note="ANK 6"
FT DOMAIN 424..487
FT /note="SAM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00184"
FT REGION 1..421
FT /note="Interaction with NEK7"
FT /evidence="ECO:0000250|UniProtKB:Q9CZK6"
FT REGION 242..261
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 278..425
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 585..604
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 637..663
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 500..575
FT /evidence="ECO:0000255"
FT COMPBIAS 323..367
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 398..421
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 649..663
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 5
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 96
FT /note="3-hydroxyasparagine"
FT /evidence="ECO:0000250|UniProtKB:Q9CZK6"
FT MOD_RES 201
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9CZK6"
FT MOD_RES 225
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9CZK6"
FT MOD_RES 243
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9CZK6"
FT MOD_RES 244
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9CZK6"
FT MOD_RES 245
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9CZK6"
FT MOD_RES 318
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9CZK6"
FT MOD_RES 319
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9CZK6"
FT MOD_RES 366
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9CZK6"
FT MOD_RES 369
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9CZK6"
FT MOD_RES 373
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9CZK6"
FT MOD_RES 540
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9CZK6"
SQ SEQUENCE 663 AA; 73048 MW; C8CC9D5EC8110DB6 CRC64;
MSELSDEASE PELLNRSLSM WHGLGAQVSR EELDVPLDLH TAASIGQYEV VKECVQRREL
DLNKKNGGGW TPLMYASYIG HDTIVHLLLE AGVSVNVPTP EGQTPLMLAS SCGNESIAYF
LLQQGAELEM KDIQGWTALF HCTSAGHQQM VKFLLESGAN ANVREPVYGF TPLMEAAAAG
HEIIVQYFLN HGVKVDTRDH SGATARMLAK QYGHMKIVAL METHSPVLPK SLYRSSENYE
DLSSSDESWP VPQRQRPCRK KGLSIHEGPR ALARITATGL GGKTPDSYEQ VPPRGYVTFT
SSDENTMEGE GLCYRDVTSP INERDVESSS SSSREEPTFC ASLGPVWRSS SSDGLARAQG
LSSEASIESN EDSDHARKSS VRKQTRTYLK NKSRHNNSDG HWPSSTGTAR TPGSEPQAEK
SPYSGPQDLA TLLEQIGCLK YLQVFEEQDV DLRIFLTLTE SDLKEIGITL FGPKRKMTSA
IARWHSSARP PSDALELAYA DRLEAEMQEL AIQLHKCCEE AEALRGQVSQ EQELRAVVES
CLLEQDSARK DIHAQLQEAQ TLAQDAALVL DQLRACQAEL SARLKQHHSP SEATQNPPFL
PADSKGWPIP LQALSLPELS GALEDRVHEM GIMLRNAEPG ETTDAEWEEM EGTIARRDDS
DVG
