PERI_MOUSE
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 03-AUG-2022, entry version 159.
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:22723690, PubMed:15322088,
CC PubMed:10426285). 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}.
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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 IntAct; P15331; 10.
DR MINT; P15331; -.
DR STRING; 10090.ENSMUSP00000049303; -.
DR iPTMnet; P15331; -.
DR PhosphoSitePlus; P15331; -.
DR UCD-2DPAGE; P15331; -.
DR jPOST; P15331; -.
DR MaxQB; P15331; -.
DR PRIDE; P15331; -.
DR ProteomicsDB; 288030; -. [P15331-1]
DR ProteomicsDB; 288031; -. [P15331-2]
DR ProteomicsDB; 288032; -. [P15331-3]
DR ABCD; P15331; 1 sequenced antibody.
DR MGI; MGI:97774; Prph.
DR eggNOG; ENOG502QPSH; Eukaryota.
DR InParanoid; P15331; -.
DR PhylomeDB; P15331; -.
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:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005882; C:intermediate filament; IDA:MGI.
DR GO; GO:0005883; C:neurofilament; IDA:MGI.
DR GO; GO:0043005; C:neuron projection; ISO:MGI.
DR GO; GO:0043025; C:neuronal cell body; ISO:MGI.
DR GO; GO:0043204; C:perikaryon; IEA:UniProtKB-SubCell.
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:MGI.
DR GO; GO:0045098; C:type III intermediate filament; ISO:MGI.
DR GO; GO:0044877; F:protein-containing complex binding; ISO:MGI.
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 InterPro; IPR018039; IF_conserved.
DR InterPro; IPR039008; IF_rod_dom.
DR InterPro; IPR006821; Intermed_filament_DNA-bd.
DR InterPro; IPR002957; Keratin_I.
DR InterPro; IPR027700; PRPH/Plasticin.
DR PANTHER; PTHR45652:SF14; PTHR45652:SF14; 1.
DR Pfam; PF00038; Filament; 1.
DR Pfam; PF04732; Filament_head; 1.
DR PRINTS; PR01248; TYPE1KERATIN.
DR SMART; SM01391; Filament; 1.
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 1..29
FT /note="Polar residues"
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
