PERI_HUMAN
ID PERI_HUMAN Reviewed; 470 AA.
AC P41219; Q8N577;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 31-OCT-2006, sequence version 2.
DT 03-AUG-2022, entry version 185.
DE RecName: Full=Peripherin;
DE AltName: Full=Neurofilament 4;
GN Name=PRPH; Synonyms=NEF4, PRPH1;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND ALTERNATIVE SPLICING (ISOFORM 2).
RC TISSUE=Placenta;
RX PubMed=7806235; DOI=10.1006/geno.1994.1410;
RA Foley J., Ley C.A., Parysek L.M.;
RT "The structure of the human peripherin gene (PRPH) and identification of
RT potential regulatory elements.";
RL Genomics 22:456-461(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16541075; DOI=10.1038/nature04569;
RA Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y.,
RA Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C.,
RA Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C.,
RA Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R.,
RA Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E.,
RA Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y.,
RA Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G.,
RA Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H.,
RA Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S.,
RA Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M.,
RA Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H.,
RA Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q.,
RA Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V.,
RA Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E.,
RA Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K.,
RA Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D.,
RA Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R.,
RA David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E.,
RA D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N.,
RA Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N.,
RA Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R.,
RA Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S.,
RA LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H.,
RA Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P.,
RA Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G.,
RA Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E.,
RA Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S.,
RA Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O.,
RA Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J.,
RA Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A.,
RA Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M.,
RA Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I.,
RA Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A.,
RA Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y.,
RA Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A.,
RA Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F.,
RA Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L.,
RA Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G.,
RA Gibbs R.A.;
RT "The finished DNA sequence of human chromosome 12.";
RL Nature 440:346-351(2006).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain;
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 INTERACTION WITH PRKCE, AND SUBCELLULAR LOCATION.
RX PubMed=18408015; DOI=10.1074/jbc.m710436200;
RA Sunesson L., Hellman U., Larsson C.;
RT "Protein kinase Cepsilon binds peripherin and induces its aggregation,
RT which is accompanied by apoptosis of neuroblastoma cells.";
RL J. Biol. Chem. 283:16653-16664(2008).
RN [5]
RP TISSUE SPECIFICITY.
RX PubMed=21088854; DOI=10.1007/s00441-010-1081-6;
RA Liu W., Kinnefors A., Bostroem M., Rask-Andersen H.;
RT "Expression of peripherin in human cochlea.";
RL Cell Tissue Res. 342:345-351(2010).
RN [6]
RP INTERACTION WITH RAB7A.
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).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [8]
RP INVOLVEMENT IN ALS, VARIANT ALS TYR-141, CHARACTERIZATION OF VARIANT ALS
RP TYR-141, FUNCTION, SUBUNIT, AND SUBCELLULAR LOCATION.
RX PubMed=15446584; DOI=10.1111/j.1750-3639.2004.tb00066.x;
RA Leung C.L., He C.Z., Kaufmann P., Chin S.S., Naini A., Liem R.K.,
RA Mitsumoto H., Hays A.P.;
RT "A pathogenic peripherin gene mutation in a patient with amyotrophic
RT lateral sclerosis.";
RL Brain Pathol. 14:290-296(2004).
RN [9]
RP INVOLVEMENT IN ALS, 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 [10]
RP VARIANTS ALS PRO-133 AND TYR-141.
RX PubMed=20363051; DOI=10.1016/j.neurobiolaging.2010.02.011;
RA Corrado L., Carlomagno Y., Falasco L., Mellone S., Godi M., Cova E.,
RA Cereda C., Testa L., Mazzini L., D'Alfonso S.;
RT "A novel peripherin gene (PRPH) mutation identified in one sporadic
RT amyotrophic lateral sclerosis patient.";
RL Neurobiol. Aging 32:552.E1-552.E6(2011).
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 a
CC filamentous network (PubMed:15446584, PubMed:15322088). Assembly of the
CC 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 (By similarity). Inhibits neurite extension
CC in type II spiral ganglion neurons in the cochlea (By similarity).
CC {ECO:0000250|UniProtKB:P15331, ECO:0000250|UniProtKB:P21807,
CC ECO:0000269|PubMed:15322088, ECO:0000269|PubMed:15446584}.
CC -!- SUBUNIT: Forms homodimers (in vitro) (By similarity). Homopolymerizes
CC into a filamentous network (in vitro) (PubMed:15446584). Forms
CC heterodimers with NEFL, NEFM or NEFH (in vitro) (By similarity).
CC Interacts with DST (via C-terminus) (By similarity). Interacts with
CC RAB7A; the interaction is direct (PubMed:23179371). Interacts with
CC PRKCE (via phorbol-ester/DAG-type 2 domain) (PubMed:18408015).
CC {ECO:0000250|UniProtKB:P15331, ECO:0000250|UniProtKB:P21807,
CC ECO:0000269|PubMed:15446584, ECO:0000269|PubMed:18408015,
CC ECO:0000269|PubMed:23179371}.
CC -!- INTERACTION:
CC P41219; Q86TN1: ARNT2; NbExp=3; IntAct=EBI-752074, EBI-25844820;
CC P41219; Q8WXF7: ATL1; NbExp=3; IntAct=EBI-752074, EBI-2410266;
CC P41219; Q8WUW1: BRK1; NbExp=3; IntAct=EBI-752074, EBI-2837444;
CC P41219; Q96HB5: CCDC120; NbExp=3; IntAct=EBI-752074, EBI-744556;
CC P41219; Q16543: CDC37; NbExp=3; IntAct=EBI-752074, EBI-295634;
CC P41219; Q7Z7K6: CENPV; NbExp=3; IntAct=EBI-752074, EBI-1210604;
CC P41219; Q9UNS2: COPS3; NbExp=3; IntAct=EBI-752074, EBI-350590;
CC P41219; P02489: CRYAA; NbExp=3; IntAct=EBI-752074, EBI-6875961;
CC P41219; Q8WUE5: CT55; NbExp=3; IntAct=EBI-752074, EBI-6873363;
CC P41219; P26196: DDX6; NbExp=3; IntAct=EBI-752074, EBI-351257;
CC P41219; P17661: DES; NbExp=6; IntAct=EBI-752074, EBI-1055572;
CC P41219; Q8TC29: ENKUR; NbExp=3; IntAct=EBI-752074, EBI-9246952;
CC P41219; Q96KS9: FAM167A; NbExp=3; IntAct=EBI-752074, EBI-10290462;
CC P41219; A0A0C3SFZ9: FCHO1; NbExp=3; IntAct=EBI-752074, EBI-11977403;
CC P41219; Q99871: HAUS7; NbExp=3; IntAct=EBI-752074, EBI-395719;
CC P41219; Q8IY31-2: IFT20; NbExp=3; IntAct=EBI-752074, EBI-11742277;
CC P41219; Q0VD86: INCA1; NbExp=3; IntAct=EBI-752074, EBI-6509505;
CC P41219; Q8N5Z5: KCTD17; NbExp=3; IntAct=EBI-752074, EBI-743960;
CC P41219; Q6ZU52: KIAA0408; NbExp=3; IntAct=EBI-752074, EBI-739493;
CC P41219; Q5T5P2-6: KIAA1217; NbExp=3; IntAct=EBI-752074, EBI-10188326;
CC P41219; Q9BVG8-5: KIFC3; NbExp=3; IntAct=EBI-752074, EBI-14069005;
CC P41219; Q6P597: KLC3; NbExp=3; IntAct=EBI-752074, EBI-1643885;
CC P41219; P02533: KRT14; NbExp=3; IntAct=EBI-752074, EBI-702178;
CC P41219; P08779: KRT16; NbExp=3; IntAct=EBI-752074, EBI-356410;
CC P41219; P08727: KRT19; NbExp=6; IntAct=EBI-752074, EBI-742756;
CC P41219; P35900: KRT20; NbExp=6; IntAct=EBI-752074, EBI-742094;
CC P41219; Q2M2I5: KRT24; NbExp=3; IntAct=EBI-752074, EBI-2952736;
CC P41219; Q7Z3Y8: KRT27; NbExp=3; IntAct=EBI-752074, EBI-3044087;
CC P41219; Q15323: KRT31; NbExp=3; IntAct=EBI-752074, EBI-948001;
CC P41219; Q14525: KRT33B; NbExp=3; IntAct=EBI-752074, EBI-1049638;
CC P41219; O95678: KRT75; NbExp=3; IntAct=EBI-752074, EBI-2949715;
CC P41219; O95447: LCA5L; NbExp=3; IntAct=EBI-752074, EBI-8473670;
CC P41219; Q96BZ8: LENG1; NbExp=3; IntAct=EBI-752074, EBI-726510;
CC P41219; Q8TBB1: LNX1; NbExp=6; IntAct=EBI-752074, EBI-739832;
CC P41219; Q8IV03: LURAP1L; NbExp=3; IntAct=EBI-752074, EBI-12898559;
CC P41219; Q96A72: MAGOHB; NbExp=3; IntAct=EBI-752074, EBI-746778;
CC P41219; Q13562: NEUROD1; NbExp=3; IntAct=EBI-752074, EBI-3908303;
CC P41219; O15381-5: NVL; NbExp=3; IntAct=EBI-752074, EBI-18577082;
CC P41219; Q9UBU9: NXF1; NbExp=3; IntAct=EBI-752074, EBI-398874;
CC P41219; Q9HBE1-4: PATZ1; NbExp=3; IntAct=EBI-752074, EBI-11022007;
CC P41219; O14813: PHOX2A; NbExp=3; IntAct=EBI-752074, EBI-25844430;
CC P41219; O75925: PIAS1; NbExp=3; IntAct=EBI-752074, EBI-629434;
CC P41219; O75928-2: PIAS2; NbExp=3; IntAct=EBI-752074, EBI-348567;
CC P41219; Q8WWB5: PIH1D2; NbExp=3; IntAct=EBI-752074, EBI-10232538;
CC P41219; Q96KQ4: PPP1R13B; NbExp=3; IntAct=EBI-752074, EBI-1105153;
CC P41219; Q96T49: PPP1R16B; NbExp=3; IntAct=EBI-752074, EBI-10293968;
CC P41219; Q6NYC8: PPP1R18; NbExp=3; IntAct=EBI-752074, EBI-2557469;
CC P41219; P54646: PRKAA2; NbExp=3; IntAct=EBI-752074, EBI-1383852;
CC P41219; P25786: PSMA1; NbExp=3; IntAct=EBI-752074, EBI-359352;
CC P41219; P57052: RBM11; NbExp=3; IntAct=EBI-752074, EBI-741332;
CC P41219; Q9ULX5: RNF112; NbExp=3; IntAct=EBI-752074, EBI-25829984;
CC P41219; Q96D59: RNF183; NbExp=3; IntAct=EBI-752074, EBI-743938;
CC P41219; Q96GQ5: RUSF1; NbExp=3; IntAct=EBI-752074, EBI-8636004;
CC P41219; Q8N6K7-2: SAMD3; NbExp=3; IntAct=EBI-752074, EBI-11528848;
CC P41219; Q96GM5: SMARCD1; NbExp=3; IntAct=EBI-752074, EBI-358489;
CC P41219; Q13573: SNW1; NbExp=3; IntAct=EBI-752074, EBI-632715;
CC P41219; Q15560: TCEA2; NbExp=3; IntAct=EBI-752074, EBI-710310;
CC P41219; Q8TDR4: TCP10L; NbExp=6; IntAct=EBI-752074, EBI-3923210;
CC P41219; Q86WV5: TEN1; NbExp=3; IntAct=EBI-752074, EBI-2562799;
CC P41219; Q969K7: TMEM54; NbExp=3; IntAct=EBI-752074, EBI-3922833;
CC P41219; Q5W5X9-3: TTC23; NbExp=3; IntAct=EBI-752074, EBI-9090990;
CC P41219; Q9UGJ1-2: TUBGCP4; NbExp=3; IntAct=EBI-752074, EBI-10964469;
CC P41219; Q495M9: USH1G; NbExp=3; IntAct=EBI-752074, EBI-8601749;
CC P41219; P08670: VIM; NbExp=4; IntAct=EBI-752074, EBI-353844;
CC P41219; Q15007-2: WTAP; NbExp=3; IntAct=EBI-752074, EBI-25840023;
CC P41219; Q53FD0-2: ZC2HC1C; NbExp=3; IntAct=EBI-752074, EBI-14104088;
CC P41219; Q9NQZ6: ZC4H2; NbExp=3; IntAct=EBI-752074, EBI-747993;
CC P41219; Q96NC0: ZMAT2; NbExp=3; IntAct=EBI-752074, EBI-2682299;
CC P41219; Q9UNY5: ZNF232; NbExp=3; IntAct=EBI-752074, EBI-749023;
CC P41219; Q8N0Y2-2: ZNF444; NbExp=3; IntAct=EBI-752074, EBI-12010736;
CC P41219; Q7Z3I7: ZNF572; NbExp=3; IntAct=EBI-752074, EBI-10172590;
CC P41219; PRO_0000449633 [P0DTD1]: rep; Xeno; NbExp=3; IntAct=EBI-752074, EBI-25492395;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000269|PubMed:15322088, ECO:0000269|PubMed:15446584,
CC ECO:0000269|PubMed:18408015}. Cell projection, axon
CC {ECO:0000250|UniProtKB:P15331}. Perikaryon
CC {ECO:0000250|UniProtKB:P15331}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P41219-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P41219-2; Sequence=VSP_021159;
CC -!- TISSUE SPECIFICITY: Expressed in the neurons of the outer hair cells in
CC the organ of Corti and to a lesser extent in type I spiral ganglion
CC cells. {ECO:0000269|PubMed:21088854}.
CC -!- PTM: Phosphorylated; phosphorylation increases after nerve injury in
CC regenerating neurons. {ECO:0000250|UniProtKB:P21807}.
CC -!- DISEASE: Amyotrophic lateral sclerosis (ALS) [MIM:105400]: A
CC neurodegenerative disorder affecting upper motor neurons in the brain
CC and lower motor neurons in the brain stem and spinal cord, resulting in
CC fatal paralysis. Sensory abnormalities are absent. The pathologic
CC hallmarks of the disease include pallor of the corticospinal tract due
CC to loss of motor neurons, presence of ubiquitin-positive inclusions
CC within surviving motor neurons, and deposition of pathologic
CC aggregates. The etiology of amyotrophic lateral sclerosis is likely to
CC be multifactorial, involving both genetic and environmental factors.
CC The disease is inherited in 5-10% of the cases.
CC {ECO:0000269|PubMed:15322088, ECO:0000269|PubMed:15446584,
CC ECO:0000269|PubMed:20363051}. Note=Disease susceptibility may be
CC associated with variants affecting the gene represented in this entry.
CC -!- MISCELLANEOUS: [Isoform 2]: Gene prediction based on similarity to
CC orthologs. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the intermediate filament family.
CC {ECO:0000255|PROSITE-ProRule:PRU01188}.
CC -!- WEB RESOURCE: Name=Wikipedia; Note=Peripherin entry;
CC URL="https://en.wikipedia.org/wiki/Peripherin";
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; L14565; AAA60190.1; -; Genomic_DNA.
DR EMBL; AC125611; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC032703; AAH32703.1; -; mRNA.
DR CCDS; CCDS8783.1; -. [P41219-1]
DR PIR; A55185; A55185.
DR RefSeq; NP_006253.2; NM_006262.3. [P41219-1]
DR RefSeq; XP_005269082.1; XM_005269025.1. [P41219-2]
DR AlphaFoldDB; P41219; -.
DR SMR; P41219; -.
DR BioGRID; 111614; 176.
DR IntAct; P41219; 90.
DR MINT; P41219; -.
DR STRING; 9606.ENSP00000257860; -.
DR GlyGen; P41219; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; P41219; -.
DR MetOSite; P41219; -.
DR PhosphoSitePlus; P41219; -.
DR SwissPalm; P41219; -.
DR BioMuta; PRPH; -.
DR DMDM; 118585871; -.
DR EPD; P41219; -.
DR jPOST; P41219; -.
DR MassIVE; P41219; -.
DR MaxQB; P41219; -.
DR PaxDb; P41219; -.
DR PeptideAtlas; P41219; -.
DR PRIDE; P41219; -.
DR ProteomicsDB; 55423; -. [P41219-1]
DR ProteomicsDB; 55424; -. [P41219-2]
DR Antibodypedia; 3724; 497 antibodies from 39 providers.
DR DNASU; 5630; -.
DR Ensembl; ENST00000257860.9; ENSP00000257860.4; ENSG00000135406.14. [P41219-1]
DR GeneID; 5630; -.
DR KEGG; hsa:5630; -.
DR MANE-Select; ENST00000257860.9; ENSP00000257860.4; NM_006262.4; NP_006253.2.
DR UCSC; uc001rtu.4; human. [P41219-1]
DR CTD; 5630; -.
DR DisGeNET; 5630; -.
DR GeneCards; PRPH; -.
DR HGNC; HGNC:9461; PRPH.
DR HPA; ENSG00000135406; Tissue enhanced (brain, intestine).
DR MalaCards; PRPH; -.
DR MIM; 105400; phenotype.
DR MIM; 170710; gene.
DR neXtProt; NX_P41219; -.
DR OpenTargets; ENSG00000135406; -.
DR Orphanet; 803; Amyotrophic lateral sclerosis.
DR PharmGKB; PA33816; -.
DR VEuPathDB; HostDB:ENSG00000135406; -.
DR eggNOG; ENOG502QPSH; Eukaryota.
DR GeneTree; ENSGT00940000160203; -.
DR HOGENOM; CLU_012560_7_4_1; -.
DR InParanoid; P41219; -.
DR OMA; THSRKMV; -.
DR OrthoDB; 655109at2759; -.
DR PhylomeDB; P41219; -.
DR TreeFam; TF330122; -.
DR PathwayCommons; P41219; -.
DR SignaLink; P41219; -.
DR SIGNOR; P41219; -.
DR BioGRID-ORCS; 5630; 17 hits in 1071 CRISPR screens.
DR GeneWiki; Peripherin; -.
DR GenomeRNAi; 5630; -.
DR Pharos; P41219; Tbio.
DR PRO; PR:P41219; -.
DR Proteomes; UP000005640; Chromosome 12.
DR RNAct; P41219; protein.
DR Bgee; ENSG00000135406; Expressed in dorsal root ganglion and 143 other tissues.
DR ExpressionAtlas; P41219; baseline and differential.
DR Genevisible; P41219; HS.
DR GO; GO:0030424; C:axon; IBA:GO_Central.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0005882; C:intermediate filament; IBA:GO_Central.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0043204; C:perikaryon; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0045098; C:type III intermediate filament; IBA:GO_Central.
DR GO; GO:0005200; F:structural constituent of cytoskeleton; IBA:GO_Central.
DR GO; GO:0005198; F:structural molecule activity; NAS:ProtInc.
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; Amyotrophic lateral sclerosis; Cell projection;
KW Coiled coil; Cytoplasm; Cytoskeleton; Disease variant;
KW Intermediate filament; Neurodegeneration; Nitration; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..470
FT /note="Peripherin"
FT /id="PRO_0000063779"
FT DOMAIN 97..407
FT /note="IF rod"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01188"
FT REGION 1..99
FT /note="Head"
FT REGION 100..132
FT /note="Coil 1A"
FT REGION 133..143
FT /note="Linker 1"
FT REGION 144..239
FT /note="Coil 1B"
FT REGION 240..262
FT /note="Linker 2"
FT REGION 263..405
FT /note="Coil 2"
FT REGION 406..470
FT /note="Tail"
FT REGION 447..470
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 450..470
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 17
FT /note="3'-nitrotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P21807"
FT MOD_RES 28
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P21807"
FT MOD_RES 50
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P21807"
FT MOD_RES 59
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P15331"
FT MOD_RES 379
FT /note="3'-nitrotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P21807"
FT MOD_RES 470
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P21807"
FT VAR_SEQ 449
FT /note="E -> EQ (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_021159"
FT VARIANT 133
FT /note="R -> P (in ALS; unknown pathological significance;
FT dbSNP:rs267607528)"
FT /evidence="ECO:0000269|PubMed:20363051"
FT /id="VAR_083259"
FT VARIANT 141
FT /note="D -> Y (in ALS; unknown pathological significance;
FT leads to filamentous aggregate formation;
FT dbSNP:rs58599399)"
FT /evidence="ECO:0000269|PubMed:15446584,
FT ECO:0000269|PubMed:20363051"
FT /id="VAR_083260"
FT CONFLICT 68
FT /note="G -> R (in Ref. 1; AAA60190)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 470 AA; 53651 MW; 4ABEAB96088719D6 CRC64;
MSHHPSGLRA GFSSTSYRRT FGPPPSLSPG AFSYSSSSRF SSSRLLGSAS PSSSVRLGSF
RSPRAGAGAL LRLPSERLDF SMAEALNQEF LATRSNEKQE LQELNDRFAN FIEKVRFLEQ
QNAALRGELS QARGQEPARA DQLCQQELRE LRRELELLGR ERDRVQVERD GLAEDLAALK
QRLEEETRKR EDAEHNLVLF RKDVDDATLS RLELERKIES LMDEIEFLKK LHEEELRDLQ
VSVESQQVQQ VEVEATVKPE LTAALRDIRA QYESIAAKNL QEAEEWYKSK YADLSDAANR
NHEALRQAKQ EMNESRRQIQ SLTCEVDGLR GTNEALLRQL RELEEQFALE AGGYQAGAAR
LEEELRQLKE EMARHLREYQ ELLNVKMALD IEIATYRKLL EGEESRISVP VHSFASLNIK
TTVPEVEPPQ DSHSRKTVLI KTIETRNGEV VTESQKEQRS ELDKSSAHSY
