ID   PERI_XENLA              Reviewed;         456 AA.
AC   P48676;
DT   01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1996, sequence version 1.
DT   25-MAY-2022, entry version 96.
DE   RecName: Full=Peripherin;
DE   AltName: Full=Neuronal intermediate filament IF3;
GN   Name=prph; Synonyms=if3;
OS   Xenopus laevis (African clawed frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX   NCBI_TaxID=8355;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND DEVELOPMENTAL STAGE.
RX   PubMed=2632231; DOI=10.1242/dev.107.4.701;
RA   Sharpe C.R., Pluck A., Gurdon J.B.;
RT   "XIF3, a Xenopus peripherin gene, requires an inductive signal for enhanced
RT   expression in anterior neural tissue.";
RL   Development 107:701-714(1989).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 323-396.
RX   PubMed=3224553; DOI=10.1242/dev.103.2.269;
RA   Sharpe C.R.;
RT   "Developmental expression of a neurofilament-M and two vimentin-like genes
RT   in Xenopus laevis.";
RL   Development 103:269-277(1988).
CC   -!- FUNCTION: Class-III neuronal intermediate filament protein (By
CC       similarity). My form an independent structural network without the
CC       involvement of other neurofilaments or may cooperate with other
CC       neuronal intermediate filament proteins to form a filamentous network
CC       (By similarity). {ECO:0000250|UniProtKB:P15331,
CC       ECO:0000250|UniProtKB:P21807}.
CC   -!- SUBUNIT: Forms homodimers (in vitro) (By similarity). Homopolymerizes
CC       into a filamentous network (in vitro) (By similarity).
CC       {ECO:0000250|UniProtKB:P15331, ECO:0000250|UniProtKB:P21807}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC       {ECO:0000250|UniProtKB:P15331}. Cell projection, axon
CC       {ECO:0000250|UniProtKB:P15331}. Perikaryon
CC       {ECO:0000250|UniProtKB:P15331}.
CC   -!- DEVELOPMENTAL STAGE: Expressed predominantly in anterior and dorsal
CC       structures and most strongly in the brain of the tailbud (stage 26)
CC       embryo. {ECO:0000269|PubMed:2632231}.
CC   -!- SIMILARITY: Belongs to the intermediate filament family.
CC       {ECO:0000255|PROSITE-ProRule:PRU01188}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAA34591.1; Type=Frameshift; Evidence={ECO:0000305};
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DR   EMBL; X16570; CAA34591.1; ALT_FRAME; mRNA.
DR   PIR; A60090; A60090.
DR   AlphaFoldDB; P48676; -.
DR   SMR; P48676; -.
DR   Proteomes; UP000186698; Genome assembly.
DR   GO; GO:0030424; C:axon; IEA:UniProtKB-SubCell.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0043204; C:perikaryon; IEA:UniProtKB-SubCell.
DR   GO; GO:0045098; C:type III intermediate filament; IEA:InterPro.
DR   GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
DR   GO; GO:0045104; P:intermediate filament cytoskeleton organization; IEA:InterPro.
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   2: Evidence at transcript level;
KW   Cell projection; Coiled coil; Cytoplasm; Cytoskeleton;
KW   Intermediate filament; Phosphoprotein; Reference proteome.
FT   CHAIN           1..456
FT                   /note="Peripherin"
FT                   /id="PRO_0000063782"
FT   DOMAIN          88..397
FT                   /note="IF rod"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01188"
FT   REGION          1..90
FT                   /note="Head"
FT   REGION          1..55
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          91..123
FT                   /note="Coil 1A"
FT   REGION          124..134
FT                   /note="Linker 1"
FT   REGION          135..230
FT                   /note="Coil 1B"
FT   REGION          231..252
FT                   /note="Linker 2"
FT   REGION          253..395
FT                   /note="Coil 2"
FT   REGION          396..456
FT                   /note="Tail"
FT   REGION          411..456
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        420..456
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   456 AA;  51996 MW;  E31BD54C5498C5B0 CRC64;
     MSHSGLRSTS TSYRRTLGSS PVPSSYSSSS RLSTSRHFGS PSPGPSSRSS SSAFRVRSST
     PVRVSLDRVD FSVAEAVNQE FLTTRSNEKA ELQELNDRFA SFIEKVRYLE QQNAVLVTEI
     NQARSKEPTR ASDLCQQELR ELRKQLELLG KDRDHIQVER DNFAEDLAFL KQRLDEEVHK
     REDAENNLVL FRKDVDDATL SRLELERKIE SLMDEIEFLK KLHEEELNDV QVSVQAQPVH
     MEIEAAKQPD LTSALRDIRS QYETIAAKNV QESEDWYKSK FADLSDAANR NSEALRQAKQ
     DMNESRRQIQ SLTCEVDGLK GTNEALLRQM KNMEEQFGME AANYQDTIGG LEQEVQHMKE
     EMSRHLREYQ DLLNVKMALD IEIATYRKLL EGEESRIAVP IHSLTSLSIK SPAAPEIDPS
     TETHTRKTVA IKTIETRDGE QVVTESRKEQ SSEGEK