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PERI_BOVIN
ID   PERI_BOVIN              Reviewed;         469 AA.
AC   A6QQJ3;
DT   08-MAR-2011, integrated into UniProtKB/Swiss-Prot.
DT   21-AUG-2007, sequence version 1.
DT   03-AUG-2022, entry version 88.
DE   RecName: Full=Peripherin;
GN   Name=PRPH;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Hereford; TISSUE=Ascending colon;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (JUL-2007) to the EMBL/GenBank/DDBJ databases.
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 (By similarity). Assembly of the neuronal
CC       intermediate filaments may be regulated by RAB7A (By similarity). Plays
CC       a role in the development of unmyelinated sensory neurons (By
CC       similarity). May be involved in axon elongation and axon regeneration
CC       after injury (By similarity). Inhibits neurite extension in type II
CC       spiral ganglion neurons in the cochlea (By similarity).
CC       {ECO:0000250|UniProtKB:P15331, ECO:0000250|UniProtKB:P21807}.
CC   -!- SUBUNIT: Forms homodimers (in vitro) (By similarity). Homopolymerizes
CC       into a filamentous network (in vitro) (By similarity). 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 (By similarity). Interacts with PRKCE
CC       (via phorbol-ester/DAG-type 2 domain) (By similarity).
CC       {ECO:0000250|UniProtKB:P15331, ECO:0000250|UniProtKB:P21807,
CC       ECO:0000250|UniProtKB:P41219}.
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   -!- PTM: Phosphorylated; phosphorylation increases after nerve injury in
CC       regenerating neurons. {ECO:0000250|UniProtKB:P21807}.
CC   -!- SIMILARITY: Belongs to the intermediate filament family.
CC       {ECO:0000255|PROSITE-ProRule:PRU01188}.
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DR   EMBL; BC149862; AAI49863.1; -; mRNA.
DR   RefSeq; NP_001095848.1; NM_001102378.1.
DR   AlphaFoldDB; A6QQJ3; -.
DR   SMR; A6QQJ3; -.
DR   STRING; 9913.ENSBTAP00000023744; -.
DR   PaxDb; A6QQJ3; -.
DR   PeptideAtlas; A6QQJ3; -.
DR   PRIDE; A6QQJ3; -.
DR   Ensembl; ENSBTAT00000023744; ENSBTAP00000023744; ENSBTAG00000017864.
DR   GeneID; 510082; -.
DR   KEGG; bta:510082; -.
DR   CTD; 5630; -.
DR   VEuPathDB; HostDB:ENSBTAG00000017864; -.
DR   VGNC; VGNC:33384; PRPH.
DR   eggNOG; ENOG502QPSH; Eukaryota.
DR   GeneTree; ENSGT00940000160203; -.
DR   HOGENOM; CLU_012560_7_4_1; -.
DR   InParanoid; A6QQJ3; -.
DR   OMA; THSRKMV; -.
DR   OrthoDB; 655109at2759; -.
DR   TreeFam; TF330122; -.
DR   Proteomes; UP000009136; Chromosome 5.
DR   Bgee; ENSBTAG00000017864; Expressed in conceptus and 51 other tissues.
DR   GO; GO:0030424; C:axon; IBA:GO_Central.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005882; C:intermediate filament; IBA:GO_Central.
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: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   2: Evidence at transcript level;
KW   Cell projection; Coiled coil; Cytoplasm; Cytoskeleton;
KW   Intermediate filament; Nitration; Phosphoprotein; Reference proteome.
FT   CHAIN           1..469
FT                   /note="Peripherin"
FT                   /id="PRO_0000405805"
FT   DOMAIN          96..406
FT                   /note="IF rod"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01188"
FT   REGION          1..98
FT                   /note="Head"
FT   REGION          1..60
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          99..131
FT                   /note="Coil 1A"
FT   REGION          132..142
FT                   /note="Linker 1"
FT   REGION          143..238
FT                   /note="Coil 1B"
FT   REGION          239..261
FT                   /note="Linker 2"
FT   REGION          262..404
FT                   /note="Coil 2"
FT   REGION          405..469
FT                   /note="Tail"
FT                   /evidence="ECO:0000250"
FT   REGION          447..469
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..21
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        28..54
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        447..463
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         16
FT                   /note="3'-nitrotyrosine"
FT                   /evidence="ECO:0000250|UniProtKB:P21807"
FT   MOD_RES         27
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P21807"
FT   MOD_RES         49
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P21807"
FT   MOD_RES         58
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P15331"
FT   MOD_RES         378
FT                   /note="3'-nitrotyrosine"
FT                   /evidence="ECO:0000250|UniProtKB:P21807"
FT   MOD_RES         469
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000250|UniProtKB:P21807"
SQ   SEQUENCE   469 AA;  53631 MW;  4889823E57A0501A CRC64;
     MSHPSGLRSS VSSTSYRRTF GPPPSLSPGA FSYSSSSRFS SSRLLGSASP GSSVRLGSFR
     GPRAGTGALL RLPSERLDFS MAEALNQEFL ATRSNEKQEL QELNDRFANF IEKVRFLEQQ
     NAALRGELNQ ARGQEPARAD QLCQQELREL RRELELLGRE RDRVQVERDG LAEDLAALKQ
     RLEEETRKRE DAEHNLVLFR KDVDDATLSR LELERKIESL MDEIEFLKKL HEEELRDLQL
     SVESQQVQHV EVEATVKPEL TAALRDIRAQ YESIAAKNLQ EAEEWYKSKY ADLSDAANRN
     HEALRQAKQE MNESRRQIQS LTCEVDGLRG TNEALLRQLR ELEEQFALEA GGYQAGAARL
     EEELRQLKEE MARHLREYQE LLNVKMALDI EIATYRKLLE GEESRISVPV HSFASLSIKT
     TVPEVEPPQE THSRKMVLIR TIETRDGEQV VTESQKEQHS ELDKSPQSY
 
 
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