ID PERI_MOUSE Reviewed; 475 AA. AC P15331; O35688; O35689; DT 01-APR-1990, integrated into UniProtKB/Swiss-Prot. DT 15-JUL-1998, sequence version 2. DT 02-SEP-2026, entry version 174. DE RecName: Full=Peripherin; GN Name=Prph; Synonyms=Prph1; 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 [GENOMIC DNA]. RC STRAIN=BALB/cJ; TISSUE=Liver; RX PubMed=1294287; DOI=10.1016/0248-4900(92)90193-5; RA Karpov V., Landon F., Djabali K., Gros F., Portier M.M.; RT "Structure of the mouse gene encoding peripherin: a neuronal intermediate RT filament protein."; RL Biol. Cell 76:43-48(1992). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 5G). RC STRAIN=FVB/N; TISSUE=Colon; 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 OF 70-475, AND ALTERNATIVE SPLICING. RX PubMed=2767051; DOI=10.1002/j.1460-2075.1989.tb03564.x; RA Landon F., Lemonnier M., Benarous R., Huc C., Fiszman M., Gros F., RA Portier M.M.; RT "Multiple mRNAs encode peripherin, a neuronal intermediate filament RT protein."; RL EMBO J. 8:1719-1726(1989). RN [4] RP PROTEIN SEQUENCE OF 411-424. RC TISSUE=Brain; RA Lubec G., Yang J.W., Zigmond M.; RL Submitted (JUL-2007) to UniProtKB. RN [5] RP FUNCTION, SUBUNIT, AND SUBCELLULAR LOCATION. RX PubMed=10426285; DOI=10.1139/o99-003; RA Beaulieu J.M., Robertson J., Julien J.P.; RT "Interactions between peripherin and neurofilaments in cultured cells: RT disruption of peripherin assembly by the NF-M and NF-H subunits."; RL Biochem. Cell Biol. 77:41-45(1999). RN [6] RP INTERACTION WITH DST, AND SUBCELLULAR LOCATION. RX PubMed=9971739; DOI=10.1083/jcb.144.3.435; RA Leung C.L., Sun D., Liem R.K.; RT "The intermediate filament protein peripherin is the specific interaction RT partner of mouse BPAG1-n (dystonin) in neurons."; RL J. Cell Biol. 144:435-446(1999). RN [7] RP FUNCTION, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE. RX PubMed=12065660; DOI=10.1046/j.1471-4159.2002.00853.x; RA Lariviere R.C., Nguyen M.D., Ribeiro-da-Silva A., Julien J.P.; RT "Reduced number of unmyelinated sensory axons in peripherin null mice."; RL J. Neurochem. 81:525-532(2002). RN [8] RP FUNCTION, AND SUBCELLULAR LOCATION. RX PubMed=15322088; DOI=10.1074/jbc.m408139200; RA Gros-Louis F., Lariviere R., Gowing G., Laurent S., Camu W., Bouchard J.P., RA Meininger V., Rouleau G.A., Julien J.P.; RT "A frameshift deletion in peripherin gene associated with amyotrophic RT lateral sclerosis."; RL J. Biol. Chem. 279:45951-45956(2004). RN [9] RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY. RX PubMed=17899157; DOI=10.1007/s00418-007-0340-4; RA Barclay M., Noakes P.G., Ryan A.F., Julien J.P., Housley G.D.; RT "Neuronal expression of peripherin, a type III intermediate filament RT protein, in the mouse hindbrain."; RL Histochem. Cell Biol. 128:541-550(2007). RN [10] RP PHOSPHORYLATION AT SER-66, AND MUTAGENESIS OF SER-66. RX PubMed=17569669; DOI=10.1074/jbc.m611703200; RA Konishi H., Namikawa K., Shikata K., Kobatake Y., Tachibana T., Kiyama H.; RT "Identification of peripherin as a Akt substrate in neurons."; RL J. Biol. Chem. 282:23491-23499(2007). RN [11] RP SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE. RX PubMed=18709437; DOI=10.1007/s11248-008-9210-7; RA McLenachan S., Goldshmit Y., Fowler K.J., Voullaire L., Holloway T.P., RA Turnley A.M., Ioannou P.A., Sarsero J.P.; RT "Transgenic mice expressing the Peripherin-EGFP genomic reporter display RT intrinsic peripheral nervous system fluorescence."; RL Transgenic Res. 17:1103-1116(2008). RN [12] RP FUNCTION, SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE, AND DISRUPTION RP PHENOTYPE. RX PubMed=20132868; DOI=10.1016/j.neulet.2010.01.063; RA Barclay M., Julien J.P., Ryan A.F., Housley G.D.; RT "Type III intermediate filament peripherin inhibits neuritogenesis in type RT II spiral ganglion neurons in vitro."; RL Neurosci. Lett. 478:51-55(2010). RN [13] RP FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY. RX PubMed=22723690; DOI=10.1523/jneurosci.1081-12.2012; RA Yuan A., Sasaki T., Kumar A., Peterhoff C.M., Rao M.V., Liem R.K., RA Julien J.P., Nixon R.A.; RT "Peripherin is a subunit of peripheral nerve neurofilaments: implications RT for differential vulnerability of CNS and peripheral nervous system RT axons."; RL J. Neurosci. 32:8501-8508(2012). RN [14] RP FUNCTION, INTERACTION WITH RAB7A, SUBCELLULAR LOCATION, AND DEVELOPMENTAL RP STAGE. RX PubMed=23179371; DOI=10.1007/s00401-012-1063-8; RA Cogli L., Progida C., Thomas C.L., Spencer-Dene B., Donno C., Schiavo G., RA Bucci C.; RT "Charcot-Marie-Tooth type 2B disease-causing RAB7A mutant proteins show RT altered interaction with the neuronal intermediate filament peripherin."; RL Acta Neuropathol. 125:257-272(2013). CC -!- FUNCTION: Class-III neuronal intermediate filament protein (By CC similarity). May form an independent structural network without the CC involvement of other neurofilaments or may cooperate with the neuronal CC intermediate filament proteins NEFL, NEFH, NEFM and INA to form CC filamentous networks (PubMed:10426285, PubMed:15322088, CC PubMed:22723690). Assembly of the neuronal intermediate filaments may CC be regulated by RAB7A (PubMed:23179371). Plays a role in the CC development of unmyelinated sensory neurons (PubMed:12065660). May be CC involved in axon elongation and axon regeneration after injury (By CC similarity). Inhibits neurite extension in type II spiral ganglion CC neurons in the cochlea (PubMed:20132868). CC {ECO:0000250|UniProtKB:P21807, ECO:0000269|PubMed:10426285, CC ECO:0000269|PubMed:12065660, ECO:0000269|PubMed:15322088, CC ECO:0000269|PubMed:20132868, ECO:0000269|PubMed:22723690, CC ECO:0000269|PubMed:23179371}. CC -!- SUBUNIT: Forms homodimers (in vitro) (By similarity). Homopolymerizes CC into a filamentous network (in vitro) (PubMed:10426285). Forms CC heterodimers with NEFL, NEFM or NEFH (in vitro) (By similarity). CC Interacts with DST (via C-terminus) (PubMed:9971739). Interacts with CC RAB7A; the interaction is direct (PubMed:23179371). Interacts with CC PRKCE (via phorbol-ester/DAG-type 2 domain) (By similarity). CC {ECO:0000250|UniProtKB:P21807, ECO:0000250|UniProtKB:P41219, CC ECO:0000269|PubMed:10426285, ECO:0000269|PubMed:23179371, CC ECO:0000269|PubMed:9971739}. CC -!- INTERACTION: CC P15331; Q9EPM5: Sync; NbExp=3; IntAct=EBI-1634736, EBI-7424051; CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton CC {ECO:0000269|PubMed:10426285, ECO:0000269|PubMed:15322088, CC ECO:0000269|PubMed:18709437, ECO:0000269|PubMed:20132868, CC ECO:0000269|PubMed:22723690, ECO:0000269|PubMed:23179371, CC ECO:0000269|PubMed:9971739}. Cell projection, axon CC {ECO:0000269|PubMed:17899157, ECO:0000269|PubMed:18709437, CC ECO:0000269|PubMed:20132868, ECO:0000269|PubMed:22723690, CC ECO:0000269|PubMed:23179371}. Perikaryon {ECO:0000269|PubMed:17899157, CC ECO:0000269|PubMed:18709437, ECO:0000269|PubMed:20132868}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=3; CC Name=5g; CC IsoId=P15331-1; Sequence=Displayed; CC Name=3u; CC IsoId=P15331-2; Sequence=VSP_002466; CC Name=5b; CC IsoId=P15331-3; Sequence=VSP_002467; CC -!- TISSUE SPECIFICITY: Expressed in the sciatic nerve and at very low CC levels in the central nervous system (at protein level) CC (PubMed:22723690). Expressed in the spinal cord, in the sciatic nerve CC at the level of the dorsal root ganglion and in trigeminal nerves (at CC protein level) (PubMed:12065660). Expressed in the cranial nerves in CC the hindbrain, including the sensory and motor trigeminal neurons, the CC mesencephalic trigeminal neurons, the spinal trigeminal neurons, and in CC the facial nerve (at protein level) (PubMed:17899157). Expressed in the CC cerebellum, with expression in the inferior cerebellar peduncle and the CC lateral deep cerebellar nucleus (at protein level) (PubMed:17899157). CC Expressed in vestibulocochlear neurons, such as the anteroventral CC cochlear nucleus, the dorsal cochlear nucleus, the superficial granule CC cell layer and the granule cell lamina (at protein level) CC (PubMed:17899157). Expressed in glossopharyngeal, vagal and hypoglossal CC neurons (at protein level) (PubMed:17899157). Expressed in peripheral CC sensory neurons, in the dorsal root ganglia and the spinal cord, and to CC a lower extent in motor neurons (PubMed:18709437). Expressed in the CC optic tract of the central nervous system, especially in the lateral CC geniculate nucleus and the superior colliculus (PubMed:18709437). CC Expressed in neurons of the pineal stalk in the cortex CC (PubMed:18709437). Expressed in the spinal trigeminal tract of the CC midbrain, in the medulla and in the medial cerebellar peduncle CC (PubMed:18709437). {ECO:0000269|PubMed:12065660, CC ECO:0000269|PubMed:17899157, ECO:0000269|PubMed:18709437, CC ECO:0000269|PubMed:22723690}. CC -!- DEVELOPMENTAL STAGE: Expressed in the dorsal root ganglia and in the CC spinal cord at 9.5 dpc (PubMed:18709437). Expressed in the neurons that CC innervate the limb buds at 13 dpc (PubMed:18709437). Expressed in the CC dorsal root ganglia and the sciatic nerve at 13.5 dpc CC (PubMed:23179371). Expressed in type I and type II spiral ganglion CC neurons of the cochlea at postnatal days P1 to P7 (PubMed:20132868). CC {ECO:0000269|PubMed:18709437, ECO:0000269|PubMed:20132868, CC ECO:0000269|PubMed:23179371}. CC -!- PTM: Phosphorylated; phosphorylation increases after nerve injury in CC regenerating neurons. {ECO:0000250|UniProtKB:P21807}. CC -!- DISRUPTION PHENOTYPE: Mutant mice are viable, reproduce normally and do CC not exhibit gross morphological defects (PubMed:12065660). Increased CC levels of intermediate filament proteins Vim in the spinal cord and Ina CC in L5 ventral roots, and a reduction in the number of L5 unmyelinated CC sensory fibers (PubMed:12065660). More and longer type II spiral CC ganglion neuron neurites during cochlear neuritogenesis at P1 CC (PubMed:20132868). {ECO:0000269|PubMed:12065660, CC ECO:0000269|PubMed:20132868}. CC -!- SIMILARITY: Belongs to the intermediate filament family. CC {ECO:0000255|PROSITE-ProRule:PRU01188}. 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; X15475; CAA33502.1; -; mRNA. DR EMBL; BC046291; AAH46291.1; -; mRNA. DR EMBL; X59840; CAA42499.1; -; Genomic_DNA. DR EMBL; X59840; CAA42500.1; -; Genomic_DNA. DR EMBL; X59840; CAA42501.1; -; Genomic_DNA. DR CCDS; CCDS27813.1; -. [P15331-2] DR CCDS; CCDS49727.1; -. [P15331-1] DR PIR; S14887; S14887. DR AlphaFoldDB; P15331; -. DR SMR; P15331; -. DR FunCoup; P15331; 199. DR IntAct; P15331; 10. DR MINT; P15331; -. DR STRING; 10090.ENSMUSP00000049303; -. DR GlyGen; P15331; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; P15331; -. DR PhosphoSitePlus; P15331; -. DR jPOST; P15331; -. DR PaxDb; 10090-ENSMUSP00000049303; -. DR ProteomicsDB; 288030; -. [P15331-1] DR ProteomicsDB; 288031; -. [P15331-2] DR ProteomicsDB; 288032; -. [P15331-3] DR Pumba; P15331; -. DR ABCD; P15331; 1 sequenced antibody. DR AGR; MGI:97774; -. DR MGI; MGI:97774; Prph. DR eggNOG; ENOG502QPSH; Eukaryota. DR InParanoid; P15331; -. DR PhylomeDB; P15331; -. DR CD-CODE; CE726F99; Postsynaptic density. DR PRO; PR:P15331; -. DR Proteomes; UP000000589; Unplaced. DR RNAct; P15331; protein. DR GO; GO:0030424; C:axon; IDA:MGI. DR GO; GO:0044299; C:C-fiber; IDA:MGI. DR GO; GO:0005882; C:intermediate filament; IDA:MGI. DR GO; GO:0005883; C:neurofilament; IDA:MGI. DR GO; GO:0043025; C:neuronal cell body; ISO:MGI. DR GO; GO:0043204; C:perikaryon; EXP:UniProtKB. DR GO; GO:0001750; C:photoreceptor outer segment; IDA:MGI. DR GO; GO:0042622; C:photoreceptor outer segment membrane; IDA:MGI. DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central. DR GO; GO:0043195; C:terminal bouton; ISO:GO_Central. DR GO; GO:0045098; C:type III intermediate filament; IDA:MGI. DR GO; GO:0044877; F:protein-containing complex binding; ISO:GO_Central. DR GO; GO:0005200; F:structural constituent of cytoskeleton; IBA:GO_Central. DR GO; GO:0045104; P:intermediate filament cytoskeleton organization; IDA:MGI. DR GO; GO:0045109; P:intermediate filament organization; IBA:GO_Central. DR FunFam; 1.20.5.1160:FF:000001; Keratin type II; 1. DR FunFam; 1.20.5.170:FF:000002; Type I keratin KA11; 1. DR FunFam; 1.20.5.500:FF:000001; Type II keratin 23; 1. DR Gene3D; 1.20.5.170; -; 1. DR Gene3D; 1.20.5.500; Single helix bin; 1. DR Gene3D; 1.20.5.1160; Vasodilator-stimulated phosphoprotein; 1. DR InterPro; IPR018039; IF_conserved. DR InterPro; IPR039008; IF_rod_dom. DR InterPro; IPR006821; Intermed_filament_DNA-bd. DR InterPro; IPR050405; Intermediate_filament. DR InterPro; IPR002957; Keratin_I. DR PANTHER; PTHR45652; GLIAL FIBRILLARY ACIDIC PROTEIN; 1. DR PANTHER; PTHR45652:SF14; PERIPHERIN; 1. DR Pfam; PF00038; Filament; 1. DR Pfam; PF04732; Filament_head; 1. DR PRINTS; PR01248; TYPE1KERATIN. DR SMART; SM01391; Filament; 1. DR SUPFAM; SSF64593; Intermediate filament protein, coiled coil region; 2. DR PROSITE; PS00226; IF_ROD_1; 1. DR PROSITE; PS51842; IF_ROD_2; 1. PE 1: Evidence at protein level; KW Alternative splicing; Cell projection; Coiled coil; Cytoplasm; KW Cytoskeleton; Direct protein sequencing; Intermediate filament; Nitration; KW Phosphoprotein; Reference proteome. FT CHAIN 1..475 FT /note="Peripherin" FT /id="PRO_0000063780" FT DOMAIN 101..411 FT /note="IF rod" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01188" FT REGION 1..103 FT /note="Head" FT REGION 1..42 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 104..136 FT /note="Coil 1A" FT REGION 137..147 FT /note="Linker 1" FT REGION 148..243 FT /note="Coil 1B" FT REGION 244..266 FT /note="Linker 2" FT REGION 267..409 FT /note="Coil 2" FT REGION 410..475 FT /note="Tail" FT REGION 453..475 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 14..26 FT /note="Low complexity" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 24 FT /note="3'-nitrotyrosine" FT /evidence="ECO:0000250|UniProtKB:P21807" FT MOD_RES 35 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P21807" FT MOD_RES 57 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P21807" FT MOD_RES 66 FT /note="Phosphoserine; by PKB/AKT1" FT /evidence="ECO:0000269|PubMed:17569669" FT MOD_RES 383 FT /note="3'-nitrotyrosine" FT /evidence="ECO:0000250|UniProtKB:P21807" FT MOD_RES 475 FT /note="Phosphotyrosine" FT /evidence="ECO:0000250|UniProtKB:P21807" FT VAR_SEQ 294 FT /note="K -> KVREHWGNPGGPRVGRHWEWRCASQPGLSATAQ (in isoform FT 3u)" FT /evidence="ECO:0000305" FT /id="VSP_002466" FT VAR_SEQ 454..475 FT /note="KVVTESQKEQHSDLDKSSIHSY -> LLRPQPEL (in isoform 5b)" FT /evidence="ECO:0000305" FT /id="VSP_002467" FT MUTAGEN 66 FT /note="S->A: Abolishes phosphorylation by AKT." FT /evidence="ECO:0000269|PubMed:17569669" SQ SEQUENCE 475 AA; 54268 MW; 777300B08A312953 CRC64; MPSSASMSHH HSSGLRSSIS STSYRRTFGP PPSLSPGAFS YSSSSRFSSS RLLGSGSPSS SARLGSFRAP RAGALRLPSE RLDFSMAEAL NQEFLATRSN EKQELQELND RFANFIEKVR FLEQQNAALR GELSQARGQE PARADQLCQQ ELRELRRELE LLGRERDRVQ VERDGLAEDL AALKQRLEEE TRKREDAEHN LVLFRKDVDD ATLSRLELER KIESLMDEIE FLKKLHEEEL RDLQVSVESQ QVQQVEVEAT VKPELTAALR DIRAQYENIA AKNLQEAEEW YKSKYADLSD AANRNHEALR QAKQEMNESR RQIQSLTCEV DGLRGTNEAL LRQLRELEEQ FALEAGGYQA GAARLEEELR QLKEEMARHL REYQELLNVK MALDIEIATY RKLLEGEESR ISVPVHSFAS LSLKTTVPEM EPLQDSHSKK MVLIRTIETR DGEKVVTESQ KEQHSDLDKS SIHSY //