RAI14_RAT
ID RAI14_RAT Reviewed; 978 AA.
AC Q5U312;
DT 13-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT 13-JUN-2006, sequence version 2.
DT 03-AUG-2022, entry version 120.
DE RecName: Full=Ankycorbin;
DE AltName: Full=Ankyrin repeat and coiled-coil structure-containing protein;
DE AltName: Full=Retinoic acid-induced protein 14;
GN Name=Rai14;
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 GENOMIC DNA].
RC STRAIN=Brown Norway;
RX PubMed=15057822; DOI=10.1038/nature02426;
RA Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA Mockrin S., Collins F.S.;
RT "Genome sequence of the Brown Norway rat yields insights into mammalian
RT evolution.";
RL Nature 428:493-521(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Lung;
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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-249; SER-281 AND SER-318, 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 [4]
RP FUNCTION, INTERACTION WITH PALLD, SUBCELLULAR LOCATION, TISSUE SPECIFICITY,
RP DEVELOPMENTAL STAGE, AND DISRUPTION PHENOTYPE.
RX PubMed=23565266; DOI=10.1371/journal.pone.0060656;
RA Qian X., Mruk D.D., Cheng C.Y.;
RT "Rai14 (retinoic acid induced protein 14) is involved in regulating f-actin
RT dynamics at the ectoplasmic specialization in the rat testis.";
RL PLoS ONE 8:E60656-E60656(2013).
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:0000269|PubMed:23565266}.
CC -!- SUBUNIT: Interacts with PALLD (PubMed:23565266). Associates with actin
CC (PubMed:23565266). However, does not bind F-actin directly (By
CC similarity). {ECO:0000250|UniProtKB:Q9EP71,
CC ECO:0000269|PubMed:23565266}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000269|PubMed:23565266}. Cytoplasm, cytoskeleton, stress fiber
CC {ECO:0000250|UniProtKB:Q9EP71}. Cytoplasm, cell cortex
CC {ECO:0000269|PubMed:23565266}. Cell junction
CC {ECO:0000269|PubMed:23565266}. Nucleus {ECO:0000250|UniProtKB:Q9P0K7}.
CC Note=Associated with the cortical actin cytoskeleton structures in
CC terminal web and cell-cell adhesion sites (By similarity). Highly
CC expressed at the ectoplasmic specialization, an actin-rich cell
CC junction specific to the testis (PubMed:23565266). Predominantly
CC nuclear in nonconfluent cells (By similarity).
CC {ECO:0000250|UniProtKB:Q9EP71, ECO:0000250|UniProtKB:Q9P0K7,
CC ECO:0000269|PubMed:23565266}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q5U312-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q5U312-2; Sequence=VSP_019250;
CC -!- TISSUE SPECIFICITY: Detected in testis where it is highly expressed in
CC germ cells, and also expressed at lower levels in Sertoli cells (at
CC protein level). {ECO:0000269|PubMed:23565266}.
CC -!- DEVELOPMENTAL STAGE: In testis, first detected in stage VI seminiferous
CC tubules where it is strongly expressed at the apical ectoplasmic
CC speclialization (ES). Initially detected around the entire spermatid
CC head, then during stage VII becomes tightly restricted to the concave
CC side of the spermatid head. From late stage VIII through to stage XII,
CC expressed once again around the entire spermatid head. In stage VIII-IX
CC tubules, detected at lower levels at the basal ES associated with the
CC blood-testis barrier. Detected at the apical spermatid-Sertoli cell
CC junction in stage VIII-XII tubules. {ECO:0000269|PubMed:23565266}.
CC -!- DISRUPTION PHENOTYPE: RNAi-mediated knockdown in testis tissue results
CC in misorientation of spermatids, indicating loss of polarity. Transport
CC of germ cells across the seminiferous epithelium is disrupted leading
CC to partial spermatid entrapment in the epithelium. Premature spermatid
CC release is also detected in stage VII tubules. F-actin is mislocalized
CC and found on the convex side of the spermatid head, in contrast to wild
CC type where it is tightly restricted to the concave side. PALLD
CC localization is also abnormal, showing more diffuse expression away
CC from the spermatid head. {ECO:0000269|PubMed:23565266}.
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DR EMBL; AABR03014275; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR03014450; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR03016256; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR03017461; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC085775; AAH85775.1; -; mRNA.
DR RefSeq; NP_001011947.1; NM_001011947.1. [Q5U312-2]
DR RefSeq; XP_006232122.1; XM_006232060.3. [Q5U312-1]
DR RefSeq; XP_006232123.1; XM_006232061.3. [Q5U312-1]
DR RefSeq; XP_006232124.1; XM_006232062.3. [Q5U312-1]
DR RefSeq; XP_006232125.1; XM_006232063.3. [Q5U312-2]
DR AlphaFoldDB; Q5U312; -.
DR SMR; Q5U312; -.
DR STRING; 10116.ENSRNOP00000048063; -.
DR CarbonylDB; Q5U312; -.
DR iPTMnet; Q5U312; -.
DR PhosphoSitePlus; Q5U312; -.
DR jPOST; Q5U312; -.
DR PaxDb; Q5U312; -.
DR PRIDE; Q5U312; -.
DR Ensembl; ENSRNOT00000040348; ENSRNOP00000048063; ENSRNOG00000028872. [Q5U312-1]
DR Ensembl; ENSRNOT00000046215; ENSRNOP00000049295; ENSRNOG00000028872. [Q5U312-2]
DR GeneID; 294804; -.
DR KEGG; rno:294804; -.
DR CTD; 26064; -.
DR RGD; 1305942; Rai14.
DR eggNOG; ENOG502QUEG; Eukaryota.
DR GeneTree; ENSGT00940000157400; -.
DR HOGENOM; CLU_005323_2_0_1; -.
DR InParanoid; Q5U312; -.
DR OMA; XDGNIPL; -.
DR OrthoDB; 876605at2759; -.
DR PhylomeDB; Q5U312; -.
DR PRO; PR:Q5U312; -.
DR Proteomes; UP000002494; Chromosome 2.
DR Bgee; ENSRNOG00000028872; Expressed in testis and 18 other tissues.
DR Genevisible; Q5U312; RN.
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; IEA:Ensembl.
DR GO; GO:0001650; C:fibrillar center; IEA:Ensembl.
DR GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
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; 5.
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; Alternative splicing; ANK repeat; Cell junction; Coiled coil;
KW Cytoplasm; Cytoskeleton; Differentiation; Nucleus; Phosphoprotein;
KW Reference proteome; Repeat; Spermatogenesis.
FT CHAIN 1..978
FT /note="Ankycorbin"
FT /id="PRO_0000239632"
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 248..299
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 388..424
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 349..374
FT /evidence="ECO:0000255"
FT COILED 427..945
FT /evidence="ECO:0000255"
FT MOTIF 270..276
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000250"
FT COMPBIAS 248..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 388..409
FT /note="Polar 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:0007744|PubMed:22673903"
FT MOD_RES 281
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
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:0000250|UniProtKB:Q9EP71"
FT MOD_RES 318
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
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 511
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9P0K7"
FT MOD_RES 514
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9P0K7"
FT MOD_RES 666
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9P0K7"
FT VAR_SEQ 256..284
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_019250"
SQ SEQUENCE 978 AA; 109134 MW; 1138713A9A2DACBA CRC64;
MKSLKAKFRK SDTNEWNKND DRLLQAVENG DAEKVASLLG KKGASATKHD SEGKTAFHLA
AAKGHVECLK VMVTHGVDVT AQDSSGHSAL HIAAKNGHPE YIKKLLQYKS PAESVDNLGK
TALHYAAAQG SLQAVQVLCE HKSPINLKDL DGNIPLLVAI QNGHSEACHF LLDHGADVNS
RDKNGRTALM LACETGSANT VEALIKKGAD LNLVDSLGHN ALYYSKLSEN AGIQSLLLSK
ISQDADLKTP TKAKQHDQVS KISSERSGTP KKRKAPPPPI SPTQLSDVSS PRSITSTPLS
GKESVFFAEA PFKAEISSIQ ENKDRLSDST AGADSLLDVS SEADQQDLLV LLQAKVASLT
LHNKELQDKL QAKSPKETEA DLSFQSFHST QTDLAPSPSK SSDIPSSDAK SSPPVEHPAG
TSTADRDVII QQLQDTLHDL QKRLETSEAE KKQLQDELQS QRTDTTCLNN TEISENGSDL
SQKLKDTQSK YEEAMKEVLS VQKQMKLGLL SHESADGDSR LREVRVTDED VDALKQDLQR
ALEESKRDKA RVQELETKLV EKEKAEATKP SSEVCEEMRN SYCSVIENMN KEKAFLFEKY
QQAQEEIMKL KDTLKSQMPQ EAPDDSGDMK ETMNRMVDEL NKQVSELSQL YREAQAELED
YRKRKSLEDA TEYIHRAEHE RLMHLSNLSR TKAEESLSDM RSQYSKVLNE LTQLKQLVDA
HKENSVSITE HLEVITTLRT MAKEMEEKTV TLQEHLASKE GEVAKLEKQL AEEKAAMSDA
MVPKASYEKL QASLESEVNA LAAKLKESVK EKEKAHSEVA QVRSEVSQAK REKENIQTLL
KSKEQEVTEL VQKFQRAQEE LAGLKRCSET SSKLEEDKDE KINEMTKEVL KLKEALNSLS
QLSYSTSSSK RQTQQLEMLQ QQVKQLQNQL AECKKQHQEV VSVYRMHLLY AVQGQMDEDV
QKVLKQILTM CKNQSQKK
