ANS4B_MOUSE
ID ANS4B_MOUSE Reviewed; 423 AA.
AC Q8K3X6; Q148R3; Q9D8A5;
DT 09-NOV-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 138.
DE RecName: Full=Ankyrin repeat and SAM domain-containing protein 4B {ECO:0000305};
DE AltName: Full=Harmonin-interacting ankyrin repeat-containing protein {ECO:0000303|PubMed:15461667};
DE Short=Harp {ECO:0000303|PubMed:15461667};
GN Name=Anks4b {ECO:0000312|MGI:MGI:1919324};
GN Synonyms=Harp {ECO:0000303|PubMed:15461667};
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], INTERACTION WITH USH1C, MOTIF, AND TISSUE
RP SPECIFICITY.
RC STRAIN=BALB/cJ; TISSUE=Kidney;
RX PubMed=15461667; DOI=10.1111/j.1365-2443.2004.00776.x;
RA Johnston A.M., Naselli G., Niwa H., Brodnicki T., Harrison L.C.,
RA Gonez L.J.;
RT "Harp (harmonin-interacting, ankyrin repeat-containing protein), a novel
RT protein that interacts with harmonin in epithelial tissues.";
RL Genes Cells 9:967-982(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Small intestine;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Kidney;
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 [6]
RP FUNCTION, INTERACTION WITH HSPA5, AND SUBCELLULAR LOCATION.
RX PubMed=22589549; DOI=10.1074/jbc.m112.368779;
RA Sato Y., Hatta M., Karim M.F., Sawa T., Wei F.Y., Sato S., Magnuson M.A.,
RA Gonzalez F.J., Tomizawa K., Akaike T., Yoshizawa T., Yamagata K.;
RT "Anks4b, a novel target of HNF4alpha protein, interacts with GRP78 protein
RT and regulates endoplasmic reticulum stress-induced apoptosis in pancreatic
RT beta-cells.";
RL J. Biol. Chem. 287:23236-23245(2012).
RN [7]
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=26812018; DOI=10.1016/j.devcel.2015.12.022;
RA Crawley S.W., Weck M.L., Grega-Larson N.E., Shifrin D.A. Jr., Tyska M.J.;
RT "ANKS4B is essential for intermicrovillar adhesion complex formation.";
RL Dev. Cell 36:190-200(2016).
RN [8]
RP X-RAY CRYSTALLOGRAPHY (2.65 ANGSTROMS) OF 345-423 IN COMPLEX WITH USH1C,
RP X-RAY CRYSTALLOGRAPHY (3.4 ANGSTROMS) OF 253-352 IN COMPLEX WITH MYO7B, AND
RP REGION.
RX PubMed=26812017; DOI=10.1016/j.devcel.2015.12.020;
RA Li J., He Y., Lu Q., Zhang M.;
RT "Mechanistic basis of organization of the Harmonin/USH1C-mediated brush
RT border microvilli tip-link complex.";
RL Dev. Cell 36:179-189(2016).
CC -!- FUNCTION: As part of the intermicrovillar adhesion complex/IMAC plays a
CC role in epithelial brush border differentiation, controlling microvilli
CC organization and length. Plays a role in assembly of the complex (By
CC similarity). May play a role in cellular response to endoplasmic
CC reticulum stress (PubMed:22589549). {ECO:0000250|UniProtKB:Q8N8V4,
CC ECO:0000269|PubMed:22589549}.
CC -!- SUBUNIT: Part of the IMAC/intermicrovillar adhesion
CC complex/intermicrovillar tip-link complex composed of ANKS4B, MYO7B,
CC USH1C, CDHR2 and CDHR5 (By similarity). Interacts with USH1C; the
CC interaction is direct and is required for ANKS4B localization to the
CC tip of microvilli (PubMed:15461667, PubMed:26812017). Interacts with
CC MYO7B; the interaction is direct (PubMed:26812017). May interact with
CC HSPA5 (PubMed:22589549). {ECO:0000250|UniProtKB:Q8N8V4,
CC ECO:0000269|PubMed:15461667, ECO:0000269|PubMed:22589549,
CC ECO:0000269|PubMed:26812017}.
CC -!- SUBCELLULAR LOCATION: Cell projection, microvillus
CC {ECO:0000269|PubMed:26812018}. Note=Localizes at the tip of microvilli
CC (PubMed:26812018). May associate with endoplasmic reticulum membranes
CC (PubMed:22589549). {ECO:0000269|PubMed:22589549,
CC ECO:0000269|PubMed:26812018}.
CC -!- TISSUE SPECIFICITY: Cochlea, kidney, lung, liver, pancreas, salivary
CC gland and small intestine (at protein level). Expressed in kidney,
CC small intestine, pancreas, liver and colon. Not detected in heart,
CC spleen and brain. {ECO:0000269|PubMed:15461667,
CC ECO:0000269|PubMed:26812018}.
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DR EMBL; AF524030; AAM81375.1; -; mRNA.
DR EMBL; AK008229; BAB25545.1; -; mRNA.
DR EMBL; BC115784; AAI15785.1; -; mRNA.
DR EMBL; BC118013; AAI18014.1; -; mRNA.
DR CCDS; CCDS21793.1; -.
DR RefSeq; NP_082361.2; NM_028085.2.
DR PDB; 5F3X; X-ray; 2.65 A; B/D=345-423.
DR PDB; 5F3Y; X-ray; 3.41 A; B=252-352.
DR PDBsum; 5F3X; -.
DR PDBsum; 5F3Y; -.
DR AlphaFoldDB; Q8K3X6; -.
DR SMR; Q8K3X6; -.
DR BioGRID; 215131; 1.
DR IntAct; Q8K3X6; 1.
DR STRING; 10090.ENSMUSP00000033201; -.
DR iPTMnet; Q8K3X6; -.
DR PhosphoSitePlus; Q8K3X6; -.
DR jPOST; Q8K3X6; -.
DR MaxQB; Q8K3X6; -.
DR PaxDb; Q8K3X6; -.
DR PeptideAtlas; Q8K3X6; -.
DR PRIDE; Q8K3X6; -.
DR ProteomicsDB; 281773; -.
DR Antibodypedia; 50456; 66 antibodies from 16 providers.
DR DNASU; 72074; -.
DR Ensembl; ENSMUST00000033201; ENSMUSP00000033201; ENSMUSG00000030909.
DR GeneID; 72074; -.
DR KEGG; mmu:72074; -.
DR UCSC; uc009jmj.2; mouse.
DR CTD; 257629; -.
DR MGI; MGI:1919324; Anks4b.
DR VEuPathDB; HostDB:ENSMUSG00000030909; -.
DR eggNOG; KOG0504; Eukaryota.
DR GeneTree; ENSGT00390000017548; -.
DR HOGENOM; CLU_028071_1_0_1; -.
DR InParanoid; Q8K3X6; -.
DR OMA; EVIWDDE; -.
DR OrthoDB; 1344159at2759; -.
DR PhylomeDB; Q8K3X6; -.
DR TreeFam; TF324946; -.
DR BioGRID-ORCS; 72074; 1 hit in 72 CRISPR screens.
DR PRO; PR:Q8K3X6; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; Q8K3X6; protein.
DR Bgee; ENSMUSG00000030909; Expressed in jejunum and 31 other tissues.
DR Genevisible; Q8K3X6; MM.
DR GO; GO:0005903; C:brush border; IDA:UniProtKB.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IDA:MGI.
DR GO; GO:0005902; C:microvillus; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IDA:MGI.
DR GO; GO:1904970; P:brush border assembly; ISS:UniProtKB.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR GO; GO:1904106; P:protein localization to microvillus; ISS:UniProtKB.
DR GO; GO:0065003; P:protein-containing complex assembly; ISS:UniProtKB.
DR GO; GO:0034976; P:response to endoplasmic reticulum stress; IMP:MGI.
DR CDD; cd09587; SAM_HARP; 1.
DR Gene3D; 1.10.150.50; -; 1.
DR Gene3D; 1.25.40.20; -; 1.
DR InterPro; IPR037601; ANKS4B_SAM.
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; 1.
DR Pfam; PF00536; SAM_1; 1.
DR SMART; SM00248; ANK; 3.
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; 2.
PE 1: Evidence at protein level;
KW 3D-structure; ANK repeat; Cell projection; Coiled coil; Differentiation;
KW Reference proteome; Repeat.
FT CHAIN 1..423
FT /note="Ankyrin repeat and SAM domain-containing protein 4B"
FT /id="PRO_0000066997"
FT REPEAT 31..60
FT /note="ANK 1"
FT REPEAT 64..93
FT /note="ANK 2"
FT REPEAT 97..126
FT /note="ANK 3"
FT DOMAIN 357..409
FT /note="SAM"
FT REGION 1..251
FT /note="Mediates localization to microvilli"
FT /evidence="ECO:0000250|UniProtKB:Q8N8V4"
FT REGION 158..181
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 207..227
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 253..352
FT /note="Mediates interaction with MYO7B"
FT /evidence="ECO:0000269|PubMed:26812017"
FT REGION 303..335
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 130..169
FT /evidence="ECO:0000255"
FT COILED 301..335
FT /evidence="ECO:0000255"
FT MOTIF 421..423
FT /note="PDZ-binding; mediates interaction with USH1C"
FT /evidence="ECO:0000269|PubMed:15461667"
FT COMPBIAS 165..181
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 311..325
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 324
FT /note="E -> G (in Ref. 2; BAB25545)"
FT /evidence="ECO:0000305"
FT CONFLICT 332
FT /note="A -> E (in Ref. 2; BAB25545)"
FT /evidence="ECO:0000305"
FT STRAND 265..267
FT /evidence="ECO:0007829|PDB:5F3Y"
FT TURN 268..270
FT /evidence="ECO:0007829|PDB:5F3Y"
FT HELIX 353..360
FT /evidence="ECO:0007829|PDB:5F3X"
FT HELIX 364..366
FT /evidence="ECO:0007829|PDB:5F3X"
FT HELIX 367..372
FT /evidence="ECO:0007829|PDB:5F3X"
FT HELIX 377..381
FT /evidence="ECO:0007829|PDB:5F3X"
FT HELIX 385..390
FT /evidence="ECO:0007829|PDB:5F3X"
FT HELIX 395..413
FT /evidence="ECO:0007829|PDB:5F3X"
FT STRAND 421..423
FT /evidence="ECO:0007829|PDB:5F3X"
SQ SEQUENCE 423 AA; 47975 MW; 65886645CB15AB48 CRC64;
MSTRYHQAAS DSYLELLKEA TKRDLNLSDE DGMTPTLLAA YHGNLEALEI ICSRGGDPDK
CDIWGNTPLH YAASNGHTHC ISFLVNFGAN IFALDNDLKS PLDAAASREQ KECVALLDKA
ATVQNTMNPK RVTRLKEQAL KNARKQMKEC ERLQERHQNK MARTYSKEDS GTISSSHSTL
SRSFLSTTSA GRFGSLSKGI KDTFKIKSKK NKDTTEQLEK DGRSGQRPVM EVFREEEEDS
FPKDFKEKLH FSVEEDDDVQ HESILNRPGL GSIVFSRNRV LDFEDISDSK RELGFKMPSE
LFQRQGAAGT VEEEEEEEEE EEEEKREANG TAGDLPWDEE EVEWEEDAVD ATPLEVFLQS
QHLEEFLPIF MREQIDLEAL LLCSDEDLQN IHMQLGPRKK VLSAIDKRKQ VLQQPGQLVD
TSL
