AHI1_RAT
ID AHI1_RAT Reviewed; 1047 AA.
AC Q6DTM3;
DT 30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 1.
DT 03-AUG-2022, entry version 112.
DE RecName: Full=Jouberin;
DE AltName: Full=Abelson helper integration site 1 protein homolog;
DE Short=AHI-1;
GN Name=Ahi1;
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 [MRNA].
RC TISSUE=Brain;
RX PubMed=12186888; DOI=10.1128/jvi.76.18.9046-9059.2002;
RA Jiang X., Hanna Z., Kaouass M., Girard L., Jolicoeur P.;
RT "Ahi-1, a novel gene encoding a modular protein with WD40-repeat and SH3
RT domains, is targeted by the Ahi-1 and Mis-2 provirus integrations.";
RL J. Virol. 76:9046-9059(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Sprague-Dawley; TISSUE=Brain;
RA Kim H., Park S.-H., Sun W., Choi B.-I., Han S.-B.;
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [3]
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).
CC -!- FUNCTION: Involved in vesicle trafficking and required for
CC ciliogenesis, formation of primary non-motile cilium, and recruitment
CC of RAB8A to the basal body of primary cilium. Component of the
CC tectonic-like complex, a complex localized at the transition zone of
CC primary cilia and acting as a barrier that prevents diffusion of
CC transmembrane proteins between the cilia and plasma membranes. Involved
CC in neuronal differentiation. As a positive modulator of classical Wnt
CC signaling, may play a crucial role in ciliary signaling during
CC cerebellum embryonic development. {ECO:0000250|UniProtKB:Q8K3E5}.
CC -!- SUBUNIT: Self-associates. Part of the tectonic-like complex (also named
CC B9 complex). Interacts with MKS1. Interacts with NPHP1; probably as
CC heterodimers and/or AHI1(2):NPHP1(2) heterotetramers. Interacts (via
CC SH3 domain) with the dynamin GTPase DNM2. Interacts with HAP1; probably
CC as AHI1(2):HAP1(2) heterotetramers. Interacts with RAB8A. Interacts
CC with CEND1 (By similarity). Interacts with SPATA7 (By similarity).
CC {ECO:0000250|UniProtKB:Q8K3E5, ECO:0000250|UniProtKB:Q8N157}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, cilium basal body
CC {ECO:0000250|UniProtKB:Q8K3E5}. Cytoplasm, cytoskeleton, microtubule
CC organizing center, centrosome, centriole
CC {ECO:0000250|UniProtKB:Q8K3E5}. Cell junction, adherens junction
CC {ECO:0000250|UniProtKB:Q8N157}. Note=In the retinal photoreceptor cell
CC layer, localizes at the connecting cilium.
CC {ECO:0000250|UniProtKB:Q8K3E5}.
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DR EMBL; AY647140; AAT66919.1; -; mRNA.
DR RefSeq; NP_001002277.1; NM_001002277.1.
DR AlphaFoldDB; Q6DTM3; -.
DR SMR; Q6DTM3; -.
DR STRING; 10116.ENSRNOP00000019077; -.
DR iPTMnet; Q6DTM3; -.
DR PhosphoSitePlus; Q6DTM3; -.
DR PaxDb; Q6DTM3; -.
DR PRIDE; Q6DTM3; -.
DR GeneID; 308923; -.
DR KEGG; rno:308923; -.
DR CTD; 54806; -.
DR RGD; 1303040; Ahi1.
DR eggNOG; KOG0266; Eukaryota.
DR InParanoid; Q6DTM3; -.
DR OrthoDB; 1176970at2759; -.
DR PhylomeDB; Q6DTM3; -.
DR Reactome; R-RNO-5620912; Anchoring of the basal body to the plasma membrane.
DR PRO; PR:Q6DTM3; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0005912; C:adherens junction; ISS:UniProtKB.
DR GO; GO:0005911; C:cell-cell junction; ISS:UniProtKB.
DR GO; GO:0005814; C:centriole; ISS:UniProtKB.
DR GO; GO:0005813; C:centrosome; ISS:UniProtKB.
DR GO; GO:0036064; C:ciliary basal body; ISS:UniProtKB.
DR GO; GO:0005929; C:cilium; ISS:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IDA:RGD.
DR GO; GO:0036038; C:MKS complex; ISS:UniProtKB.
DR GO; GO:0097730; C:non-motile cilium; ISS:UniProtKB.
DR GO; GO:0120206; C:photoreceptor distal connecting cilium; ISO:RGD.
DR GO; GO:0001750; C:photoreceptor outer segment; ISO:RGD.
DR GO; GO:0042802; F:identical protein binding; ISO:RGD.
DR GO; GO:0007417; P:central nervous system development; ISS:UniProtKB.
DR GO; GO:0060271; P:cilium assembly; ISS:UniProtKB.
DR GO; GO:0035844; P:cloaca development; ISS:UniProtKB.
DR GO; GO:1990403; P:embryonic brain development; IEP:RGD.
DR GO; GO:0042462; P:eye photoreceptor cell development; ISO:RGD.
DR GO; GO:0001947; P:heart looping; ISS:UniProtKB.
DR GO; GO:0030902; P:hindbrain development; ISS:UniProtKB.
DR GO; GO:0070121; P:Kupffer's vesicle development; ISS:UniProtKB.
DR GO; GO:0070986; P:left/right axis specification; ISS:UniProtKB.
DR GO; GO:0001738; P:morphogenesis of a polarized epithelium; ISS:UniProtKB.
DR GO; GO:0044458; P:motile cilium assembly; IBA:GO_Central.
DR GO; GO:0043066; P:negative regulation of apoptotic process; ISS:UniProtKB.
DR GO; GO:0046325; P:negative regulation of glucose import; IMP:RGD.
DR GO; GO:1905515; P:non-motile cilium assembly; ISO:RGD.
DR GO; GO:0071599; P:otic vesicle development; ISS:UniProtKB.
DR GO; GO:0035845; P:photoreceptor cell outer segment organization; ISS:UniProtKB.
DR GO; GO:0010628; P:positive regulation of gene expression; ISO:RGD.
DR GO; GO:0045927; P:positive regulation of growth; ISO:RGD.
DR GO; GO:0010976; P:positive regulation of neuron projection development; ISO:RGD.
DR GO; GO:0030862; P:positive regulation of polarized epithelial cell differentiation; ISS:UniProtKB.
DR GO; GO:0002092; P:positive regulation of receptor internalization; ISS:UniProtKB.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISS:UniProtKB.
DR GO; GO:0039023; P:pronephric duct morphogenesis; ISS:UniProtKB.
DR GO; GO:0039008; P:pronephric nephron tubule morphogenesis; ISS:UniProtKB.
DR GO; GO:0008104; P:protein localization; ISS:UniProtKB.
DR GO; GO:0033365; P:protein localization to organelle; ISO:RGD.
DR GO; GO:0050795; P:regulation of behavior; ISS:UniProtKB.
DR GO; GO:0050708; P:regulation of protein secretion; ISO:RGD.
DR GO; GO:0032094; P:response to food; IEP:RGD.
DR GO; GO:0060041; P:retina development in camera-type eye; ISO:RGD.
DR GO; GO:0010842; P:retina layer formation; ISS:UniProtKB.
DR GO; GO:0046549; P:retinal cone cell development; ISO:RGD.
DR GO; GO:0046548; P:retinal rod cell development; ISO:RGD.
DR GO; GO:0065001; P:specification of axis polarity; ISS:UniProtKB.
DR GO; GO:0021510; P:spinal cord development; IEP:RGD.
DR GO; GO:0007169; P:transmembrane receptor protein tyrosine kinase signaling pathway; ISS:UniProtKB.
DR GO; GO:0006903; P:vesicle targeting; ISO:RGD.
DR GO; GO:0016192; P:vesicle-mediated transport; ISS:UniProtKB.
DR CDD; cd11812; SH3_AHI-1; 1.
DR Gene3D; 2.130.10.10; -; 1.
DR InterPro; IPR035832; AHI1_SH3.
DR InterPro; IPR036028; SH3-like_dom_sf.
DR InterPro; IPR001452; SH3_domain.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR001680; WD40_repeat.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
DR Pfam; PF00018; SH3_1; 1.
DR Pfam; PF00400; WD40; 2.
DR PRINTS; PR00452; SH3DOMAIN.
DR SMART; SM00326; SH3; 1.
DR SMART; SM00320; WD40; 7.
DR SUPFAM; SSF50044; SSF50044; 1.
DR SUPFAM; SSF50978; SSF50978; 1.
DR PROSITE; PS50002; SH3; 1.
DR PROSITE; PS50082; WD_REPEATS_2; 4.
DR PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE 1: Evidence at protein level;
KW Cell junction; Cell projection; Cilium; Cilium biogenesis/degradation;
KW Cytoplasm; Cytoskeleton; Developmental protein; Differentiation;
KW Phosphoprotein; Reference proteome; Repeat; SH3 domain; WD repeat.
FT CHAIN 1..1047
FT /note="Jouberin"
FT /id="PRO_0000050840"
FT REPEAT 458..500
FT /note="WD 1"
FT REPEAT 503..542
FT /note="WD 2"
FT REPEAT 546..586
FT /note="WD 3"
FT REPEAT 593..632
FT /note="WD 4"
FT REPEAT 649..688
FT /note="WD 5"
FT REPEAT 692..731
FT /note="WD 6"
FT REPEAT 736..777
FT /note="WD 7"
FT DOMAIN 903..963
FT /note="SH3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT REGION 1..285
FT /note="Interaction with HAP1"
FT /evidence="ECO:0000250"
FT REGION 1..44
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 67..185
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 964..1047
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..37
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 113..135
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 158..185
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 966..1041
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 854
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8N157"
FT MOD_RES 975
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8N157"
SQ SEQUENCE 1047 AA; 119687 MW; 7753D672860ECA58 CRC64;
MEQETPEKVD SAQEKVRGKS QPADDSEDSR EKAGTEGTGE LTEAYELQVA EEMAKEIKKK
IRRKLKEQLT YFPPDTLLHD DKLGSEKRKK KKKKKVPVPA KPETSPSDVC DSAAEGEQKK
EGAPEGSHHR EGGCSTEQNA DASVPENTKP KPKKMKKKPK AVSEDNEETN GDGVHEITGR
DSPVHPKCLL DDDLVMGVYI HRTDRLKSDF MISHPMVKIH VVDEHTGQYV KKDDSERPVS
SYYEKDNVDY ILPIMTQPYD FKKLKSRLPE WEEQVIFNEN FPYLLREFDE CPKVILFFEI
LDFLSMDEIK NNSEFQNQEC GFRKIAWAFL KLLGANGNAN INSKLRLQLY YPPTKPRSQP
NVVEVFEWWS KCPRNRYPST LYVTVRGLKV PDCIKPSYRS MMALQEERGT PVYCERHRET
SSVDTEPGLE DSKEEVKWKR LPGQACRIPN KHLFSLNAGE RGCFCLDFSH NGRILAAACA
SRDGYPIILY EIPSGRFMRE LCGHLNIIYD LDWSKDDRYL VTSSSDGTAR VWKNEINSTS
TFRVLPHPSF VYTARFHPAT RELVVTGCYD SMIRIWKVDA REDAAILVRQ LDVHKSFVNS
ICFDDEGHHM YSGDCIGVIA VWDTYVKVTD VQHSVRHWTI NKEIKETEFR GVPVSYLEVH
PNGKRLLIHT KDSTLRIMDL RILAARKFVG AANYREKIHS TLTPCGTLLF SGSEDGIVYV
WNPETGEQVA MYSELPFKST IRDISYHPFE NMVAFCAFGQ SEPILLYIYD FQVAQQEAEM
LKRYSGTVPL PGIHLSEDAL CTCPKLPQQG SFQIDEFVNT ENNSSRKIQL VKQRLETVTE
VIRSCAAKVN KNLSITSPPP GPAKKPRVKQ SFVLTTDQII HQFGVPQTAF ISIERRPFMR
PVDPPPMVVA LYDYTASRSD ELTIHRGDII RVFFKDNEDW WYGSLGKGQE GFFPANHVAS
ETLYRDSPPK VKERSPPLTP KEKAKMEKPP ASRKSLIKDR FLDSRLGSKP MGHSEKGRDQ
NFEERGHKSD MEMKKSEPTV RKVTLIE
