RAI14_MOUSE
ID RAI14_MOUSE Reviewed; 979 AA.
AC Q9EP71; Q3URT3; Q6ZPT6;
DT 13-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 146.
DE RecName: Full=Ankycorbin;
DE AltName: Full=Ankyrin repeat and coiled-coil structure-containing protein;
DE AltName: Full=Novel retinal pigment epithelial cell protein;
DE AltName: Full=Retinoic acid-induced protein 14;
DE AltName: Full=p125;
GN Name=Rai14; Synonyms=Kiaa1334, Norpeg;
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], SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND
RP LACK OF INTERACTION TO F-ACTIN.
RC STRAIN=C57BL/6J; TISSUE=Kidney;
RX PubMed=11168586; DOI=10.1046/j.1365-2443.2000.00381.x;
RA Peng Y.-F., Mandai K., Sakisaka T., Okabe N., Yamamoto Y., Yokoyama S.,
RA Mizoguchi A., Shiozaki H., Monden M., Takai Y.;
RT "Ankycorbin: a novel actin cytoskeleton-associated protein.";
RL Genes Cells 5:1001-1008(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=11042181; DOI=10.1074/jbc.m007421200;
RA Kutty R.K., Kutty G., Samuel W., Duncan T., Bridges C.C., El-Sherbeeny A.,
RA Nagineni C.N., Smith S.B., Wiggert B.;
RT "Molecular characterization and developmental expression of NORPEG, a novel
RT gene induced by retinoic acid.";
RL J. Biol. Chem. 276:2831-2840(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Embryonic tail;
RX PubMed=14621295; DOI=10.1093/dnares/10.4.167;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA Saga Y., Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: III.
RT The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL DNA Res. 10:167-180(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Brain;
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 88-876.
RC STRAIN=C57BL/6J;
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 [6]
RP TISSUE SPECIFICITY, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=16806700; DOI=10.1016/j.neulet.2006.06.006;
RA Kutty R.K., Samuel W., Chen S., Vijayasarathy C., Dun Y., Mysona B.,
RA Wiggert B., Smith S.B.;
RT "Immunofluorescence analysis of the expression of Norpeg (Rai14) in retinal
RT Mueller and ganglion cells.";
RL Neurosci. Lett. 404:294-298(2006).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-304; SER-694 AND SER-914, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Kidney, Liver, Lung, Pancreas, Spleen, and Testis;
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).
CC -!- FUNCTION: Plays a role in actin regulation at the ectoplasmic
CC specialization, a type of cell junction specific to testis. Important
CC for establishment of sperm polarity and normal spermatid adhesion. May
CC also promote integrity of Sertoli cell tight junctions at the blood-
CC testis barrier. {ECO:0000250|UniProtKB:Q5U312}.
CC -!- SUBUNIT: Interacts with PALLD (By similarity). Associates with actin
CC (PubMed:11168586). However, does not bind F-actin directly
CC (PubMed:11168586). {ECO:0000250|UniProtKB:Q5U312,
CC ECO:0000269|PubMed:11168586}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000269|PubMed:11168586}. Cytoplasm, cytoskeleton, stress fiber
CC {ECO:0000269|PubMed:11168586}. Cytoplasm, cell cortex
CC {ECO:0000269|PubMed:11168586}. Cell junction
CC {ECO:0000250|UniProtKB:Q5U312}. Nucleus {ECO:0000250|UniProtKB:Q9P0K7}.
CC Note=Associated with the cortical actin cytoskeleton structures in
CC terminal web and cell-cell adhesion sites (PubMed:11168586). Highly
CC expressed at the ectoplasmic specialization, an actin-rich cell
CC junction specific to the testis (By similarity). Predominantly nuclear
CC in nonconfluent cells (By similarity). {ECO:0000250|UniProtKB:Q5U312,
CC ECO:0000250|UniProtKB:Q9P0K7, ECO:0000269|PubMed:11168586}.
CC -!- TISSUE SPECIFICITY: Highly expressed in testis, where it localizes to
CC seminiferous tubules (at protein level) (PubMed:11042181,
CC PubMed:16806700). Expressed in ganglion cell layer and in Muller cell
CC fibers of the retina (at protein level) (PubMed:11042181,
CC PubMed:16806700). In small intestine highly expressed at the apical and
CC lateral borders of absorptive epithelia (at protein level)
CC (PubMed:11168586). In liver highly expressed along the bile canaliculi
CC (at protein level) (PubMed:11168586). {ECO:0000269|PubMed:11042181,
CC ECO:0000269|PubMed:11168586, ECO:0000269|PubMed:16806700}.
CC -!- DEVELOPMENTAL STAGE: At 9.5 days, expression is detected in branchial
CC arch mesenchyme, forebrain, hindbrain, midbrain, and neural tube. At
CC 12.5 days, is detected in the hindbrain, forebrain, lung, genital
CC eminence, spinal ligaments around vertebrae and ribs, and around the
CC cartilage of ribs and nasal sinuses. Also detected in frontonasal mass,
CC mandibular arch, optic sulcus, spinal ganglia and hind limb bud. At
CC 15.5 days, expression is detected in the ventricular layer of neurons
CC subjacent to the neocortex, around the nasal sinuses, bronchioles of
CC the lung, kidney, and around the vertebrae of the tail. Also seen in
CC the olfactory bulb. {ECO:0000269|PubMed:11042181}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC98143.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AF202315; AAG24483.1; -; mRNA.
DR EMBL; AF274866; AAG25937.1; -; mRNA.
DR EMBL; AK129333; BAC98143.1; ALT_INIT; mRNA.
DR EMBL; BC052458; AAH52458.1; -; mRNA.
DR EMBL; AK141233; BAE24605.1; -; mRNA.
DR CCDS; CCDS37043.1; -.
DR RefSeq; NP_001159880.1; NM_001166408.1.
DR RefSeq; NP_109615.1; NM_030690.3.
DR RefSeq; XP_006520250.1; XM_006520187.2.
DR RefSeq; XP_006520251.1; XM_006520188.3.
DR RefSeq; XP_017172264.1; XM_017316775.1.
DR AlphaFoldDB; Q9EP71; -.
DR SMR; Q9EP71; -.
DR BioGRID; 217644; 16.
DR IntAct; Q9EP71; 12.
DR MINT; Q9EP71; -.
DR STRING; 10090.ENSMUSP00000087815; -.
DR iPTMnet; Q9EP71; -.
DR PhosphoSitePlus; Q9EP71; -.
DR EPD; Q9EP71; -.
DR jPOST; Q9EP71; -.
DR MaxQB; Q9EP71; -.
DR PaxDb; Q9EP71; -.
DR PeptideAtlas; Q9EP71; -.
DR PRIDE; Q9EP71; -.
DR ProteomicsDB; 255090; -.
DR Antibodypedia; 22784; 83 antibodies from 21 providers.
DR DNASU; 75646; -.
DR Ensembl; ENSMUST00000090339; ENSMUSP00000087815; ENSMUSG00000022246.
DR Ensembl; ENSMUST00000169385; ENSMUSP00000126325; ENSMUSG00000022246.
DR GeneID; 75646; -.
DR KEGG; mmu:75646; -.
DR UCSC; uc007vgl.1; mouse.
DR CTD; 26064; -.
DR MGI; MGI:1922896; Rai14.
DR VEuPathDB; HostDB:ENSMUSG00000022246; -.
DR eggNOG; ENOG502QUEG; Eukaryota.
DR GeneTree; ENSGT00940000157400; -.
DR HOGENOM; CLU_005323_2_0_1; -.
DR InParanoid; Q9EP71; -.
DR OMA; XDGNIPL; -.
DR OrthoDB; 876605at2759; -.
DR PhylomeDB; Q9EP71; -.
DR TreeFam; TF331274; -.
DR BioGRID-ORCS; 75646; 1 hit in 70 CRISPR screens.
DR ChiTaRS; Rai14; mouse.
DR PRO; PR:Q9EP71; -.
DR Proteomes; UP000000589; Chromosome 15.
DR RNAct; Q9EP71; protein.
DR Bgee; ENSMUSG00000022246; Expressed in renal corpuscle and 248 other tissues.
DR ExpressionAtlas; Q9EP71; baseline and differential.
DR Genevisible; Q9EP71; MM.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-SubCell.
DR GO; GO:0005938; C:cell cortex; IEA:UniProtKB-SubCell.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0001650; C:fibrillar center; ISO:MGI.
DR GO; GO:0005739; C:mitochondrion; HDA:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0003779; F:actin binding; IEA:InterPro.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR GO; GO:0007283; P:spermatogenesis; IEA:UniProtKB-KW.
DR Gene3D; 1.25.40.20; -; 2.
DR InterPro; IPR002110; Ankyrin_rpt.
DR InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR InterPro; IPR042420; RAI14.
DR PANTHER; PTHR24129; PTHR24129; 1.
DR Pfam; PF00023; Ank; 1.
DR Pfam; PF12796; Ank_2; 2.
DR PRINTS; PR01415; ANKYRIN.
DR SMART; SM00248; ANK; 6.
DR SUPFAM; SSF48403; SSF48403; 1.
DR PROSITE; PS50297; ANK_REP_REGION; 1.
DR PROSITE; PS50088; ANK_REPEAT; 5.
PE 1: Evidence at protein level;
KW Acetylation; ANK repeat; Cell junction; Coiled coil; Cytoplasm;
KW Cytoskeleton; Differentiation; Nucleus; Phosphoprotein; Reference proteome;
KW Repeat; Spermatogenesis.
FT CHAIN 1..979
FT /note="Ankycorbin"
FT /id="PRO_0000239631"
FT REPEAT 18..51
FT /note="ANK 1"
FT REPEAT 52..81
FT /note="ANK 2"
FT REPEAT 85..114
FT /note="ANK 3"
FT REPEAT 118..147
FT /note="ANK 4"
FT REPEAT 151..180
FT /note="ANK 5"
FT REPEAT 184..213
FT /note="ANK 6"
FT REPEAT 217..247
FT /note="ANK 7"
FT REGION 247..299
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 392..429
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 446..467
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 349..374
FT /evidence="ECO:0000255"
FT COILED 430..943
FT /evidence="ECO:0000255"
FT MOTIF 270..276
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000250"
FT COMPBIAS 247..272
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 285..299
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 446..460
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:Q9P0K7"
FT MOD_RES 11
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9P0K7"
FT MOD_RES 249
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9P0K7"
FT MOD_RES 281
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9P0K7"
FT MOD_RES 286
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9P0K7"
FT MOD_RES 293
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9P0K7"
FT MOD_RES 295
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9P0K7"
FT MOD_RES 297
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9P0K7"
FT MOD_RES 300
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9P0K7"
FT MOD_RES 304
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 318
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5U312"
FT MOD_RES 327
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9P0K7"
FT MOD_RES 329
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9P0K7"
FT MOD_RES 340
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9P0K7"
FT MOD_RES 341
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9P0K7"
FT MOD_RES 358
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9P0K7"
FT MOD_RES 513
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9P0K7"
FT MOD_RES 516
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9P0K7"
FT MOD_RES 667
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9P0K7"
FT MOD_RES 694
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 914
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT CONFLICT 420
FT /note="P -> L (in Ref. 3; BAC98143)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 979 AA; 108852 MW; B2E8C016D80237C4 CRC64;
MKSLKAKFRK SDTNEWNKND DRLLQAVENG DAEKVASLLG KKGASATKHD SEGKTAFHLA
AAKGHVECLK VMVTHGVDVT AQDSSGHSAL HVAAKNGHPE CIRKLLQYKS PAENIDNSGK
TALHYAAAQG CLQAVQLLCE HKSPINLKDL DGNIPLLVAV QNGHSEACHF LLDHGADVNS
RDKNGRTALM LACETGSSNT VDALIKKGAD LSLVDSLGHN ALHYSKLSEN AGIQNLLLSK
ISQDADLKTP TKPKQHDQVS KISSERSGTP KKRKAPPPPI SPTQLSDVSS PRSITSTPLS
GKESVFFAEA PFKAEISSIQ ENKDRLSDST AGADSLLDIS SEADQQDLLV LLQAKVASLT
LHNKELQDKL QAKSPKDKEA EADLSFQSFH STQTDLAPSP GKASDIPSSD AKSSPPVEHP
AGTSTTDNDV IIRQLQDSLH DLQKRLESSE AEKKQLQDEL QSQRTDTLCL NNTEISENGS
DLSQKLKETQ SKYEEAMKEV LSVQKQMKLG LLSQESADGY SHLREAPADE DIDTLKQDLQ
KAVEESARNK ERVRELETKL AEKEQAEATK PPAEACEELR SSYCSVIENM NKEKAFLFEK
YQQAQEEIMK LKDTLKSQMP QEAPDDSGDM KEAMNRMIDE LNKQVSELSQ LYREAQAELE
DYRKRKSLED AAEYIHKAEH ERLMHVSNLS RAKSEEALSE MKSQYSKVLN ELTQLKQLVD
AHKENSVSIT EHLQVITTLR TTAKEMEEKI SALTGHLANK EAEVAKLEKQ LAEEKAAVSD
AMVPKSSYEK LQASLESEVN ALATKLKESV REREKAHSEV AQVRSEVSQA RREKDNIQTL
LKAKEQEVTA LVQKFQRAQE ELAGMRRCSE TSSKLEEDKD EKINEMTREV LKLKEALNSL
SQLSYSTSSS KRQSQQLDLL QQQVKQLQNQ LAECKKHHQE VISVYRMHLL YAVQGQMDED
VQKVLKQILT MCKNQSQKK
