ID A0A2U9CH67_SCOMX Unreviewed; 978 AA.
AC A0A2U9CH67;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 24-JAN-2024, entry version 21.
DE RecName: Full=Neurofilament medium polypeptide {ECO:0000256|ARBA:ARBA00015894};
DE AltName: Full=160 kDa neurofilament protein {ECO:0000256|ARBA:ARBA00030258};
DE AltName: Full=Neurofilament triplet M protein {ECO:0000256|ARBA:ARBA00032778};
GN ORFNames=SMAX5B_015193 {ECO:0000313|EMBL:AWP15066.1};
OS Scophthalmus maximus (Turbot) (Psetta maxima).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Carangaria; Pleuronectiformes; Pleuronectoidei; Scophthalmidae;
OC Scophthalmus.
OX NCBI_TaxID=52904 {ECO:0000313|EMBL:AWP15066.1, ECO:0000313|Proteomes:UP000246464};
RN [1] {ECO:0000313|EMBL:AWP15066.1, ECO:0000313|Proteomes:UP000246464}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Martinez P.;
RT "Integrating genomic resources of turbot (Scophthalmus maximus) in depth
RT evaluation of genetic and physical mapping variation across individuals.";
RL Submitted (DEC-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the intermediate filament family.
CC {ECO:0000256|RuleBase:RU000685}.
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DR EMBL; CP026258; AWP15066.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2U9CH67; -.
DR STRING; 52904.ENSSMAP00000030093; -.
DR Proteomes; UP000246464; Chromosome 16.
DR GO; GO:0005882; C:intermediate filament; IEA:UniProtKB-KW.
DR GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
DR Gene3D; 1.20.5.170; -; 1.
DR Gene3D; 1.20.5.500; Single helix bin; 1.
DR Gene3D; 1.20.5.1160; Vasodilator-stimulated phosphoprotein; 1.
DR InterPro; IPR018039; IF_conserved.
DR InterPro; IPR039008; IF_rod_dom.
DR InterPro; IPR006821; Intermed_filament_DNA-bd.
DR InterPro; IPR002957; Keratin_I.
DR PANTHER; PTHR45652; GLIAL FIBRILLARY ACIDIC PROTEIN; 1.
DR PANTHER; PTHR45652:SF3; NEUROFILAMENT MEDIUM POLYPEPTIDE; 1.
DR Pfam; PF00038; Filament; 1.
DR Pfam; PF04732; Filament_head; 1.
DR PRINTS; PR01248; TYPE1KERATIN.
DR SMART; SM01391; Filament; 1.
DR SUPFAM; SSF64593; Intermediate filament protein, coiled coil region; 2.
DR PROSITE; PS00226; IF_ROD_1; 1.
DR PROSITE; PS51842; IF_ROD_2; 1.
PE 3: Inferred from homology;
KW Coiled coil {ECO:0000256|ARBA:ARBA00023054, ECO:0000256|SAM:Coils};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Intermediate filament {ECO:0000256|ARBA:ARBA00022754,
KW ECO:0000256|RuleBase:RU000685};
KW Reference proteome {ECO:0000313|Proteomes:UP000246464}.
FT DOMAIN 95..406
FT /note="IF rod"
FT /evidence="ECO:0000259|PROSITE:PS51842"
FT REGION 25..53
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 465..915
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 957..978
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 204..249
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 297..377
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 468..495
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 511..554
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 562..576
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 588..610
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 611..625
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 626..692
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 697..724
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 725..739
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 806..900
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 959..978
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 978 AA; 107720 MW; C6F5B71533EBC19D CRC64;
MSYPADTIGS PFRRVMDTRS IGYGYGRTGS SSPSSGFRSQ SWSRASPGST VTASYKRSVN
MPVSRAYGSA ALGSADGGDY NQSSVLNGDY KRSNEKEQLQ GLNDRFVVYI DKVHYLEQQN
KQIEDEIQAL RQKQVSRSQL GDLYDQELQE LRSMLEQIHH DKTQIQLDTD HIEEDIQRLR
DRFDEEARIR EETEAIIRVL RKDMGDSELV KSEMEKKVQS LQDEIAFIRN NHEEEVSDLI
AQIQASQVTV ERKDLQKTDI TEALREIRCE LEGHSSQNLQ QVENWFMCRY SKLTEAAEHN
KDAIKSARDE ISDYRRQLQS KTVELESVRG TRESLERQLN DIEDRHNSDL ASLQETIHQL
DNELKSTKWE MARHLREYQD LLNVKMALDI EIAAYRKLLE GEETHFSTFP YRQTVTSHKI
SKPKSETPKL KVQHKFVEEI IEETRVEDEK SDIDESLAEI AQELSATLGG DEEEEEEKEG
DEAEAEGEEG AGEEEVVSAT EAKVSASAPT EGEEEEEEDE GKGGDEDEEG EGEGGEEEDK
EEEGEGEGED DGEKGDDAEA GHEVEGEEGG EEEEQVEETV LCSKAPESKA SPDKEKAGDK
ESSGGEEEAA EEPGAKEEGG DEDEDASTDK ASKSGDDKEE KEDVDKGKKE DAKKVKDEKA
DDKSEKEVEA KAEAPKTEAA KPEVKKEEAA KTQATKPVSL KPASPKSESP KSESPKSESP
KPASPKSESP KPGSPKPGSP KAESPKAESP KSESPKPGSP KAESPKSESP KAESPKAGSP
KAESPKAGSP KAESPKPSSP KAESPKTESP KPESPKAESP KAESPKAESP KAESPKAESP
KTETAKPDAP KAAEEKSEKK SDSTEDKKVE KNDVAMNGDI DKSSPEEEGK KDEGKDVDMV
ANGVDESPVK DDGSQKVVIT KTVETITTGE DGLQHVTKSI TVTETVKEME EMVQETLVST
KKTEKQSTQS IKQVTEGN
//
