PERI_RAT
ID PERI_RAT Reviewed; 468 AA.
AC P21807;
DT 01-MAY-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1991, sequence version 1.
DT 03-AUG-2022, entry version 141.
DE RecName: Full=Peripherin;
GN Name=Prph; Synonyms=Prph1;
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 [GENOMIC DNA], AND FUNCTION.
RX PubMed=2624740; DOI=10.1016/0896-6273(89)90228-6;
RA Thompson M.A., Ziff E.B.;
RT "Structure of the gene encoding peripherin, an NGF-regulated neuronal-
RT specific type III intermediate filament protein.";
RL Neuron 2:1043-1053(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=8575457;
RA Ho C.L., Chin S.S., Carnevale K., Liem R.K.;
RT "Translation initiation and assembly of peripherin in cultured cells.";
RL Eur. J. Cell Biol. 68:103-112(1995).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 8-468, AND FUNCTION.
RX PubMed=3339087; DOI=10.1083/jcb.106.1.181;
RA Leonard D.G., Gorham J.D., Cole P., Greene L.A., Ziff E.B.;
RT "A nerve growth factor-regulated messenger RNA encodes a new intermediate
RT filament protein.";
RL J. Cell Biol. 106:181-193(1988).
RN [4]
RP NUCLEOTIDE SEQUENCE OF 267-280.
RX PubMed=3418352; DOI=10.1111/j.1471-4159.1988.tb03104.x;
RA Aletta J.M., Angeletti R., Liem R.K., Purcell C., Shelanski M.L.,
RA Greene L.A.;
RT "Relationship between the nerve growth factor-regulated clone 73 gene
RT product and the 58-kilodalton neuronal intermediate filament protein
RT (peripherin).";
RL J. Neurochem. 51:1317-1320(1988).
RN [5]
RP NUCLEOTIDE SEQUENCE OF 296-468.
RX PubMed=3272173; DOI=10.1016/0896-6273(88)90189-4;
RA Parysek L.M., Chisholm R.L., Ley C.A., Goldman R.D.;
RT "A type III intermediate filament gene is expressed in mature neurons.";
RL Neuron 1:395-401(1988).
RN [6]
RP PROTEIN SEQUENCE OF 339-357 AND 404-417, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC STRAIN=Sprague-Dawley; TISSUE=Spinal cord;
RA Lubec G., Afjehi-Sadat L.;
RL Submitted (NOV-2006) to UniProtKB.
RN [7]
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND INDUCTION.
RX PubMed=2585054; DOI=10.1523/jneurosci.09-11-03766.1989;
RA Oblinger M.M., Wong J., Parysek L.M.;
RT "Axotomy-induced changes in the expression of a type III neuronal
RT intermediate filament gene.";
RL J. Neurosci. 9:3766-3775(1989).
RN [8]
RP SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND INDUCTION.
RX PubMed=2126481; DOI=10.1016/0006-8993(90)90832-v;
RA Troy C.M., Muma N.A., Greene L.A., Price D.L., Shelanski M.L.;
RT "Regulation of peripherin and neurofilament expression in regenerating rat
RT motor neurons.";
RL Brain Res. 529:232-238(1990).
RN [9]
RP FUNCTION, SUBUNIT, AND INDUCTION.
RX PubMed=7530776; DOI=10.1002/jnr.490390203;
RA Chadan S., Le Gall J.Y., Di Giamberardino L., Filliatreau G.;
RT "Axonal transport of type III intermediate filament protein peripherin in
RT intact and regenerating motor axons of the rat sciatic nerve.";
RL J. Neurosci. Res. 39:127-139(1994).
RN [10]
RP SUBUNIT, AND TISSUE SPECIFICITY.
RX PubMed=9388258; DOI=10.1074/jbc.272.49.31073;
RA Athlan E.S., Mushynski W.E.;
RT "Heterodimeric associations between neuronal intermediate filament
RT proteins.";
RL J. Biol. Chem. 272:31073-31078(1997).
RN [11]
RP PHOSPHORYLATION AT TYR-468.
RX PubMed=9453548; DOI=10.1046/j.1471-4159.1998.70020540.x;
RA Angelastro J.M., Ho C.L., Frappier T., Liem R.K., Greene L.A.;
RT "Peripherin is tyrosine-phosphorylated at its carboxyl-terminal tyrosine.";
RL J. Neurochem. 70:540-549(1998).
RN [12]
RP SUBCELLULAR LOCATION, TISSUE SPECIFICITY, INDUCTION, AND PHOSPHORYLATION.
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 [13]
RP NITRATION AT TYR-17 AND TYR-376, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=17268851; DOI=10.1007/s11064-006-9244-2;
RA Tedeschi G., Cappelletti G., Nonnis S., Taverna F., Negri A., Ronchi C.,
RA Ronchi S.;
RT "Tyrosine nitration is a novel post-translational modification occurring on
RT the neural intermediate filament protein peripherin.";
RL Neurochem. Res. 32:433-441(2007).
RN [14]
RP TISSUE SPECIFICITY, AND INDUCTION.
RX PubMed=19913522; DOI=10.1016/j.brainres.2009.11.011;
RA Reid A.J., Welin D., Wiberg M., Terenghi G., Novikov L.N.;
RT "Peripherin and ATF3 genes are differentially regulated in regenerating and
RT non-regenerating primary sensory neurons.";
RL Brain Res. 1310:1-7(2010).
RN [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-28 AND SER-50, 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).
CC -!- FUNCTION: Class-III neuronal intermediate filament protein
CC (PubMed:3339087, PubMed:2624740). My form an independent structural
CC network without the involvement of other neurofilaments or may
CC cooperate with the neuronal intermediate filament proteins NEFL, NEFH,
CC NEFM and INA to form a filamentous network (By similarity). Assembly of
CC the neuronal intermediate filaments may be regulated by RAB7A (By
CC similarity). Plays a role in the development of unmyelinated sensory
CC neurons (By similarity). May be involved in axon elongation and axon
CC regeneration after injury (PubMed:7530776, PubMed:2585054). Inhibits
CC neurite extension in type II spiral ganglion neurons in the cochlea (By
CC similarity). {ECO:0000250|UniProtKB:P15331, ECO:0000269|PubMed:2585054,
CC ECO:0000269|PubMed:2624740, ECO:0000269|PubMed:3339087,
CC ECO:0000269|PubMed:7530776}.
CC -!- SUBUNIT: Forms homodimers (in vitro) (PubMed:7530776, PubMed:9388258).
CC Homopolymerizes into a filamentous network (in vitro) (By similarity).
CC Forms heterodimers with NEFL, NEFM or NEFH (in vitro) (PubMed:9388258).
CC Interacts with DST (via C-terminus) (By similarity). Interacts with
CC RAB7A; the interaction is direct (By similarity). Interacts with PRKCE
CC (via phorbol-ester/DAG-type 2 domain) (By similarity).
CC {ECO:0000250|UniProtKB:P15331, ECO:0000250|UniProtKB:P41219,
CC ECO:0000269|PubMed:7530776, ECO:0000269|PubMed:9388258}.
CC -!- INTERACTION:
CC P21807; Q91ZU6: Dst; Xeno; NbExp=3; IntAct=EBI-446227, EBI-446159;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000269|PubMed:17569669}. Cell projection, axon
CC {ECO:0000269|PubMed:17569669}. Perikaryon {ECO:0000269|PubMed:17569669,
CC ECO:0000269|PubMed:2126481, ECO:0000269|PubMed:2585054}.
CC -!- TISSUE SPECIFICITY: Expressed in hypoglossal motor neurons (at protein
CC level) (PubMed:17569669, PubMed:2126481). Expressed in the small and
CC large sensory neurons of the dorsal root ganglion (at protein level)
CC (PubMed:2585054, PubMed:2126481, PubMed:9388258). Expressed in
CC cutaneous and muscular sensory neurons (PubMed:19913522).
CC {ECO:0000269|PubMed:17569669, ECO:0000269|PubMed:19913522,
CC ECO:0000269|PubMed:2126481, ECO:0000269|PubMed:2585054,
CC ECO:0000269|PubMed:9388258}.
CC -!- INDUCTION: Up-regulated in regenerating neurons after nerve injury.
CC {ECO:0000269|PubMed:17569669, ECO:0000269|PubMed:19913522,
CC ECO:0000269|PubMed:2126481, ECO:0000269|PubMed:2585054,
CC ECO:0000269|PubMed:7530776}.
CC -!- PTM: Phosphorylated; phosphorylation increases after nerve injury in
CC regenerating neurons. {ECO:0000269|PubMed:17569669}.
CC -!- SIMILARITY: Belongs to the intermediate filament family.
CC {ECO:0000255|PROSITE-ProRule:PRU01188}.
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DR EMBL; M26232; AAA41829.1; -; Genomic_DNA.
DR EMBL; AF031878; AAB87067.1; -; mRNA.
DR PIR; JN0016; JN0016.
DR AlphaFoldDB; P21807; -.
DR SMR; P21807; -.
DR IntAct; P21807; 3.
DR MINT; P21807; -.
DR STRING; 10116.ENSRNOP00000021010; -.
DR iPTMnet; P21807; -.
DR PhosphoSitePlus; P21807; -.
DR jPOST; P21807; -.
DR PaxDb; P21807; -.
DR PeptideAtlas; P21807; -.
DR PRIDE; P21807; -.
DR UCSC; RGD:3414; rat.
DR RGD; 3414; Prph.
DR eggNOG; ENOG502QPSH; Eukaryota.
DR InParanoid; P21807; -.
DR PhylomeDB; P21807; -.
DR PRO; PR:P21807; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0030424; C:axon; ISO:RGD.
DR GO; GO:0044299; C:C-fiber; ISO:RGD.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005882; C:intermediate filament; ISO:RGD.
DR GO; GO:0005883; C:neurofilament; ISO:RGD.
DR GO; GO:0043005; C:neuron projection; IDA:RGD.
DR GO; GO:0043025; C:neuronal cell body; IDA:MGI.
DR GO; GO:0043204; C:perikaryon; IEA:UniProtKB-SubCell.
DR GO; GO:0001750; C:photoreceptor outer segment; ISO:RGD.
DR GO; GO:0042622; C:photoreceptor outer segment membrane; ISO:RGD.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0043195; C:terminal bouton; IDA:RGD.
DR GO; GO:0045098; C:type III intermediate filament; IDA:RGD.
DR GO; GO:0044877; F:protein-containing complex binding; IDA:RGD.
DR GO; GO:0005200; F:structural constituent of cytoskeleton; IBA:GO_Central.
DR GO; GO:0045104; P:intermediate filament cytoskeleton organization; IMP:RGD.
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 Cell projection; Coiled coil; Cytoplasm; Cytoskeleton;
KW Direct protein sequencing; Intermediate filament; Nitration;
KW Phosphoprotein; Reference proteome.
FT CHAIN 1..468
FT /note="Peripherin"
FT /id="PRO_0000063781"
FT DOMAIN 94..404
FT /note="IF rod"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01188"
FT REGION 1..96
FT /note="Head"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 97..129
FT /note="Coil 1A"
FT REGION 130..140
FT /note="Linker 1"
FT REGION 141..236
FT /note="Coil 1B"
FT REGION 237..259
FT /note="Linker 2"
FT REGION 260..402
FT /note="Coil 2"
FT REGION 403..468
FT /note="Tail"
FT REGION 445..468
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 17
FT /note="3'-nitrotyrosine"
FT /evidence="ECO:0000269|PubMed:17268851"
FT MOD_RES 28
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 50
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 59
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P15331"
FT MOD_RES 376
FT /note="3'-nitrotyrosine"
FT /evidence="ECO:0000269|PubMed:17268851"
FT MOD_RES 468
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000269|PubMed:9453548"
FT CONFLICT 158..160
FT /note="ERD -> SAY (in Ref. 3)"
FT /evidence="ECO:0000305"
FT CONFLICT 291
FT /note="L -> K (in Ref. 3)"
FT /evidence="ECO:0000305"
FT CONFLICT 436
FT /note="L -> K (in Ref. 3)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 468 AA; 53550 MW; E42543338EBA5C05 CRC64;
MSHHSSGLRS SISSTSYRRT FGPPPSLSPG AFSYSSSSRF SSSRLLGSGS PSSSARLGSF
RAPRAGALRL PSERLDFSMA EALNQEFLAT RSNEKQELQE LNDRFANFIE KVRFLEQQNA
ALRGELSQAR GQEPARADQL CQQELRELRR ELELLGRERD RVQVERDGLA EDLGALKQRL
EEETRKREDA EHNLVLFRKD VDDATLSRLE LERKIESLMD EIEFLKKLHE EELRDLQVSV
ESQQVQQVEV EATVKPELTA ALRDIRAQYE NIAAKNLQEA EEWYKSKYAD LSDAANRNHE
ALRQAKQEMN ESRRQIQSLT CEVDGLRGTN EALLRQLREL EEQFALEAGG YQAGAARLEE
ELRQLKEEMA RHLREYQELL NVKMALDIEI ATYRKLLEGE ESRISVPVHS FASLSLKTTV
PEVEPPQDSH SRKMVLIRTI ETRDGEKVVT ESQKEQHSEL DKSSIHSY
