AHI1_MOUSE
ID AHI1_MOUSE Reviewed; 1047 AA.
AC Q8K3E5; Q7TNV2; Q9CVY1;
DT 30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 30-AUG-2005, sequence version 2.
DT 03-AUG-2022, entry version 151.
DE RecName: Full=Jouberin;
DE AltName: Full=Abelson helper integration site 1 protein;
DE Short=AHI-1;
GN Name=Ahi1;
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 TISSUE SPECIFICITY.
RC STRAIN=C3H/HeJ;
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 [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Eye;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-322.
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 [4]
RP TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=15467982; DOI=10.1086/425985;
RA Dixon-Salazar T., Silhavy J.L., Marsh S.E., Louie C.M., Scott L.C.,
RA Gururaj A., Al-Gazali L., Al-Tawari A.A., Kayserili H., Sztriha L.,
RA Gleeson J.G.;
RT "Mutations in the AHI1 gene, encoding jouberin, cause Joubert syndrome with
RT cortical polymicrogyria.";
RL Am. J. Hum. Genet. 75:979-987(2004).
RN [5]
RP INTERACTION WITH NPHP1, AND SUBCELLULAR LOCATION.
RX PubMed=18633336; DOI=10.1038/ki.2008.377;
RA Eley L., Gabrielides C., Adams M., Johnson C.A., Hildebrandt F.,
RA Sayer J.A.;
RT "Jouberin localizes to collecting ducts and interacts with nephrocystin-
RT 1.";
RL Kidney Int. 74:1139-1149(2008).
RN [6]
RP FUNCTION, INTERACTION WITH RAB8A, AND SUBCELLULAR LOCATION.
RX PubMed=19625297; DOI=10.1093/hmg/ddp335;
RA Hsiao Y.C., Tong Z.J., Westfall J.E., Ault J.G., Page-McCaw P.S.,
RA Ferland R.J.;
RT "Ahi1, whose human ortholog is mutated in Joubert syndrome, is required for
RT Rab8a localization, ciliogenesis and vesicle trafficking.";
RL Hum. Mol. Genet. 18:3926-3941(2009).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
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 [8]
RP INTERACTION WITH MKS1.
RX PubMed=21565611; DOI=10.1016/j.cell.2011.04.019;
RA Sang L., Miller J.J., Corbit K.C., Giles R.H., Brauer M.J., Otto E.A.,
RA Baye L.M., Wen X., Scales S.J., Kwong M., Huntzicker E.G., Sfakianos M.K.,
RA Sandoval W., Bazan J.F., Kulkarni P., Garcia-Gonzalo F.R., Seol A.D.,
RA O'Toole J.F., Held S., Reutter H.M., Lane W.S., Rafiq M.A., Noor A.,
RA Ansar M., Devi A.R., Sheffield V.C., Slusarski D.C., Vincent J.B.,
RA Doherty D.A., Hildebrandt F., Reiter J.F., Jackson P.K.;
RT "Mapping the NPHP-JBTS-MKS protein network reveals ciliopathy disease genes
RT and pathways.";
RL Cell 145:513-528(2011).
RN [9]
RP FUNCTION, SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
RX PubMed=21623382; DOI=10.1038/nm.2380;
RA Lancaster M.A., Gopal D.J., Kim J., Saleem S.N., Silhavy J.L., Louie C.M.,
RA Thacker B.E., Williams Y., Zaki M.S., Gleeson J.G.;
RT "Defective Wnt-dependent cerebellar midline fusion in a mouse model of
RT Joubert syndrome.";
RL Nat. Med. 17:726-731(2011).
RN [10]
RP FUNCTION, AND IDENTIFICATION IN THE TECTONIC-LIKE COMPLEX.
RX PubMed=22179047; DOI=10.1038/ncb2410;
RA Chih B., Liu P., Chinn Y., Chalouni C., Komuves L.G., Hass P.E.,
RA Sandoval W., Peterson A.S.;
RT "A ciliopathy complex at the transition zone protects the cilia as a
RT privileged membrane domain.";
RL Nat. Cell Biol. 14:61-72(2012).
RN [11]
RP FUNCTION, INTERACTION WITH HAP1 AND CEND1, AND DISRUPTION PHENOTYPE.
RX PubMed=23658157; DOI=10.1523/jneurosci.0119-13.2013;
RA Weng L., Lin Y.F., Li A.L., Wang C.E., Yan S., Sun M., Gaertig M.A.,
RA Mitha N., Kosaka J., Wakabayashi T., Xu X., Tang B., Li S., Li X.J.;
RT "Loss of Ahi1 affects early development by impairing BM88/Cend1-mediated
RT neuronal differentiation.";
RL J. Neurosci. 33:8172-8184(2013).
RN [12]
RP INTERACTION WITH SPATA7, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=29899041; DOI=10.1083/jcb.201712117;
RA Dharmat R., Eblimit A., Robichaux M.A., Zhang Z., Nguyen T.T., Jung S.Y.,
RA He F., Jain A., Li Y., Qin J., Overbeek P., Roepman R., Mardon G.,
RA Wensel T.G., Chen R.;
RT "SPATA7 maintains a novel photoreceptor-specific zone in the distal
RT connecting cilium.";
RL J. Cell Biol. 217:2851-2865(2018).
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 (PubMed:19625297).
CC Component of the tectonic-like complex, a complex localized at the
CC transition zone of primary cilia and acting as a barrier that prevents
CC diffusion of transmembrane proteins between the cilia and plasma
CC membranes (PubMed:22179047). Involved in neuronal differentiation
CC (PubMed:23658157). As a positive modulator of classical Wnt signaling,
CC may play a crucial role in ciliary signaling during cerebellum
CC embryonic development (PubMed:21623382). {ECO:0000269|PubMed:19625297,
CC ECO:0000269|PubMed:21623382, ECO:0000269|PubMed:22179047,
CC ECO:0000269|PubMed:23658157}.
CC -!- SUBUNIT: Self-associates (By similarity). Part of the tectonic-like
CC complex (also named B9 complex) (PubMed:22179047). Interacts with MKS1
CC (PubMed:21565611). Interacts with NPHP1; probably as heterodimers
CC and/or AHI1(2):NPHP1(2) heterotetramers (PubMed:18633336). Interacts
CC (via SH3 domain) with the dynamin GTPase DNM2 (By similarity).
CC Interacts with HAP1; probably as AHI1(2):HAP1(2) heterotetramers (By
CC similarity) (PubMed:23658157). Interacts with RAB8A (PubMed:19625297).
CC Interacts with CEND1 (PubMed:23658157). Interacts with SPATA7
CC (PubMed:29899041). {ECO:0000250|UniProtKB:Q8N157,
CC ECO:0000269|PubMed:18633336, ECO:0000269|PubMed:19625297,
CC ECO:0000269|PubMed:21565611, ECO:0000269|PubMed:22179047,
CC ECO:0000269|PubMed:23658157, ECO:0000269|PubMed:29899041}.
CC -!- INTERACTION:
CC Q8K3E5; O35668: Hap1; NbExp=3; IntAct=EBI-4280729, EBI-473704;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, cilium basal body
CC {ECO:0000269|PubMed:18633336, ECO:0000269|PubMed:19625297,
CC ECO:0000269|PubMed:21623382}. Cytoplasm, cytoskeleton, microtubule
CC organizing center, centrosome, centriole {ECO:0000269|PubMed:19625297}.
CC Cell junction, adherens junction {ECO:0000250|UniProtKB:Q8N157}.
CC Note=In the retinal photoreceptor cell layer, localizes at the
CC connecting cilium. {ECO:0000269|PubMed:29899041}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8K3E5-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8K3E5-2; Sequence=VSP_015357, VSP_015358;
CC -!- TISSUE SPECIFICITY: Expressed in the retina (at protein level)
CC (PubMed:29899041). Highly expressed in the brain (PubMed:12186888,
CC PubMed:15467982). Highly expressed in the testis (PubMed:12186888).
CC Expressed in the kidney, thymus, heart, lung, spleen (PubMed:12186888).
CC Weakly expressed in the liver, stomach, pancreas, and embryo
CC (PubMed:12186888). Strongly expressed during periods of both cortical
CC and cerebellar development (PubMed:15467982).
CC {ECO:0000269|PubMed:12186888, ECO:0000269|PubMed:15467982,
CC ECO:0000269|PubMed:29899041}.
CC -!- DEVELOPMENTAL STAGE: First detected at 7 days post conception (dpc) and
CC is also present at 11 dpc, 15 dpc and 17 dpc with the highest level at
CC 15 dpc. Expression in whole brain is detected from 14 dpc to adult.
CC Expression in cerebellum appears maximal at 18 dpc and postnatal days 5
CC (P5), whereas expression in cerebral cortex appears maximal at 16 dpc
CC and 18 dpc. {ECO:0000269|PubMed:15467982}.
CC -!- DISRUPTION PHENOTYPE: Mutant mice, when surviving after birth, show
CC retarded growth during the postnatal period, but do not develop severe
CC cerebellar vermis hypoplasia or ataxia associated with cerebellar
CC dysfunction (PubMed:23658157). Adult homozygous knockout mice have a
CC small body size, with slightly reduced brain size compared with wild-
CC type and heterozygous littermates. The overall brain morphology appears
CC normal except for a smaller cerebellum and underdeveloped vermis with a
CC mildly defective foliation pattern. Vermian lobules VI and VII appear
CC fused, whereas lobule V appears smaller and underdeveloped at 3 weeks
CC of age. Overall, the cerebellum is slightly hypoplastic
CC (PubMed:21623382). {ECO:0000269|PubMed:21623382,
CC ECO:0000269|PubMed:23658157}.
CC -!- MISCELLANEOUS: Is targeted by provirus integrations. This deregulation
CC contributes to tumor development.
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DR EMBL; AY133241; AAM94175.1; -; mRNA.
DR EMBL; BC055400; AAH55400.1; -; mRNA.
DR EMBL; AK005991; BAB24355.1; -; mRNA.
DR CCDS; CCDS35860.1; -. [Q8K3E5-1]
DR AlphaFoldDB; Q8K3E5; -.
DR SMR; Q8K3E5; -.
DR BioGRID; 206874; 32.
DR CORUM; Q8K3E5; -.
DR IntAct; Q8K3E5; 18.
DR MINT; Q8K3E5; -.
DR STRING; 10090.ENSMUSP00000101164; -.
DR iPTMnet; Q8K3E5; -.
DR PhosphoSitePlus; Q8K3E5; -.
DR MaxQB; Q8K3E5; -.
DR PaxDb; Q8K3E5; -.
DR PRIDE; Q8K3E5; -.
DR ProteomicsDB; 296142; -. [Q8K3E5-1]
DR ProteomicsDB; 296143; -. [Q8K3E5-2]
DR MGI; MGI:87971; Ahi1.
DR eggNOG; KOG0266; Eukaryota.
DR InParanoid; Q8K3E5; -.
DR PhylomeDB; Q8K3E5; -.
DR Reactome; R-MMU-5620912; Anchoring of the basal body to the plasma membrane.
DR ChiTaRS; Ahi1; mouse.
DR PRO; PR:Q8K3E5; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; Q8K3E5; protein.
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; IDA:UniProtKB.
DR GO; GO:0005813; C:centrosome; ISS:UniProtKB.
DR GO; GO:0036064; C:ciliary basal body; IDA:UniProtKB.
DR GO; GO:0005929; C:cilium; IDA:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0036038; C:MKS complex; IDA:UniProtKB.
DR GO; GO:0097730; C:non-motile cilium; IDA:UniProtKB.
DR GO; GO:0120206; C:photoreceptor distal connecting cilium; IDA:MGI.
DR GO; GO:0001750; C:photoreceptor outer segment; IDA:MGI.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0007417; P:central nervous system development; IGI:UniProtKB.
DR GO; GO:0060271; P:cilium assembly; IMP:UniProtKB.
DR GO; GO:0035844; P:cloaca development; IGI:UniProtKB.
DR GO; GO:0042462; P:eye photoreceptor cell development; IDA:CACAO.
DR GO; GO:0001947; P:heart looping; IGI:UniProtKB.
DR GO; GO:0030902; P:hindbrain development; IGI: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; IMP:UniProtKB.
DR GO; GO:0044458; P:motile cilium assembly; IBA:GO_Central.
DR GO; GO:0043066; P:negative regulation of apoptotic process; IMP:UniProtKB.
DR GO; GO:0046325; P:negative regulation of glucose import; ISO:MGI.
DR GO; GO:1905515; P:non-motile cilium assembly; IMP:MGI.
DR GO; GO:0071599; P:otic vesicle development; IGI:UniProtKB.
DR GO; GO:0035845; P:photoreceptor cell outer segment organization; IMP:MGI.
DR GO; GO:0010628; P:positive regulation of gene expression; IMP:MGI.
DR GO; GO:0045927; P:positive regulation of growth; IDA:CACAO.
DR GO; GO:0010976; P:positive regulation of neuron projection development; IMP:CACAO.
DR GO; GO:0030862; P:positive regulation of polarized epithelial cell differentiation; IMP:UniProtKB.
DR GO; GO:0002092; P:positive regulation of receptor internalization; IMP:UniProtKB.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IMP:UniProtKB.
DR GO; GO:0039023; P:pronephric duct morphogenesis; ISS:UniProtKB.
DR GO; GO:0039008; P:pronephric nephron tubule morphogenesis; IGI:UniProtKB.
DR GO; GO:0008104; P:protein localization; IGI:UniProtKB.
DR GO; GO:0033365; P:protein localization to organelle; IMP:MGI.
DR GO; GO:0050795; P:regulation of behavior; IMP:UniProtKB.
DR GO; GO:0050708; P:regulation of protein secretion; IMP:CACAO.
DR GO; GO:0060041; P:retina development in camera-type eye; IMP:MGI.
DR GO; GO:0010842; P:retina layer formation; IGI:UniProtKB.
DR GO; GO:0046549; P:retinal cone cell development; IMP:CACAO.
DR GO; GO:0046548; P:retinal rod cell development; IMP:CACAO.
DR GO; GO:0065001; P:specification of axis polarity; IGI:UniProtKB.
DR GO; GO:0007169; P:transmembrane receptor protein tyrosine kinase signaling pathway; IMP:UniProtKB.
DR GO; GO:0006903; P:vesicle targeting; IMP:MGI.
DR GO; GO:0016192; P:vesicle-mediated transport; IMP: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 Alternative splicing; Cell junction; Cell projection; Cilium;
KW Cilium biogenesis/degradation; Cytoplasm; Cytoskeleton;
KW Developmental protein; Differentiation; Phosphoprotein; Reference proteome;
KW Repeat; SH3 domain; WD repeat.
FT CHAIN 1..1047
FT /note="Jouberin"
FT /id="PRO_0000050839"
FT REPEAT 457..499
FT /note="WD 1"
FT REPEAT 502..541
FT /note="WD 2"
FT REPEAT 545..585
FT /note="WD 3"
FT REPEAT 592..631
FT /note="WD 4"
FT REPEAT 648..687
FT /note="WD 5"
FT REPEAT 691..730
FT /note="WD 6"
FT REPEAT 735..776
FT /note="WD 7"
FT DOMAIN 902..962
FT /note="SH3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT REGION 1..284
FT /note="Interaction with HAP1"
FT /evidence="ECO:0000250"
FT REGION 1..40
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 67..181
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 963..1047
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..39
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 112..149
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 158..181
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 965..988
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1016..1041
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 853
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8N157"
FT MOD_RES 974
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8N157"
FT VAR_SEQ 994..1005
FT /note="QSLSKGRPLDPR -> GGHEEETKSQTN (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_015357"
FT VAR_SEQ 1006..1047
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_015358"
FT CONFLICT 48
FT /note="Q -> T (in Ref. 1; AAM94175)"
FT /evidence="ECO:0000305"
FT CONFLICT 194
FT /note="V -> L (in Ref. 1; AAM94175)"
FT /evidence="ECO:0000305"
FT CONFLICT 227..234
FT /note="QYVKKDDS -> H (in Ref. 3; BAB24355)"
FT /evidence="ECO:0000305"
FT CONFLICT 632
FT /note="T -> H (in Ref. 2; AAH55400)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1047 AA; 119650 MW; 91908C847218D4C0 CRC64;
MEPETPEKVD SAQEKVRGKT PTADDSDDSR EKTGIEEKGE LTDAYQLQVA EEMAKEIKKK
IRKKLKEQLT YFPPDTLLHD DKLASEKRKK KKKKVPVPTK PESSPSDVCD SAVEGEQKKE
GTPEDSQHME GICSREQDVD ATVPENAKPK PKKTKKKTKA VSNDNEDTNG DGVHEITSRD
SPVHPKCLLD DDLVMGVYIH RTDRLKSDFM ISHPMVKIHV VDEHTGQYVK KDDSERPVSS
YYEKDNVDYI LPIMTQPYDF KKLKSRLPEW EEQVIFNENF PYLLREFEEC PKVILFFEIL
DFLSMDEIKN NSEVQNQECG FRKIAWAFLK LLGANGNANI NSKLRLQLYY PPTKPRSQLN
VVEVFEWWSK CPRNRYPSTL YVTVRGLKVP DCIKPSYRSM MALQEERGTP VYCERHRETS
SVDTEPGLED SKEEVKWKRL PGQACRIPNK HLFSLNAGER GCFCLDFSHN GRILAAACAS
RDGYPIILYE IPSGRFMREL CGHLNIIYDL DWSKDDRYLV TSSSDGTARV WKNEINSTST
FRVLPHPSFV YTAKFHPATR ELVVTGCYDS MIRIWKIDAR EDAAILVRQL DVHKSFVNSI
CFDDEGHHMY SGDCIGVIVV WDTYVKVNDV QTSVRHWTIN KEIKETEFRG VPISYLEVHP
NGKRLLIHTK DSTLRIMDLR ILAARKFVGA ANYREKIHST LTPCGTLLFS GSEDGIVYVW
NPETGEQVAM YSDLPFKSTI RDISYHPLEN MVAFCAFGQS EPILLYIYDF QVAQQEAEML
KRYSGTLPLP GIHQSEDALC TCPKLPQQGS FQIDEFVNTE NSSSRKIQLV KQRLETVTEV
IRSCAAKVNK NLSMTSPPPG PAKKPRVKQS FVLTTDEIIH QFGLPQTAFI SIERGPFVRH
VDPPPMVVAL YDYTASRSDE LTIHRGDIIR VYFKDNEDWW YGSVRKGQEG FFPANHVASE
TLYRDSPPKV KERSPPLTPK EKTKPEKPLA SQKQSLSKGR PLDPRLGPQP VGHSEKGKDQ
NVEDRGHKVD METKKSEPVV RKVTLIE
