NEST_MESAU
ID NEST_MESAU Reviewed; 1818 AA.
AC Q9Z1Q1;
DT 11-JAN-2011, integrated into UniProtKB/Swiss-Prot.
DT 11-JAN-2011, sequence version 2.
DT 25-MAY-2022, entry version 68.
DE RecName: Full=Nestin {ECO:0000312|EMBL:AAC98312.1};
DE Flags: Fragments;
GN Name=NES {ECO:0000250|UniProtKB:Q6P5H2};
OS Mesocricetus auratus (Golden hamster).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea;
OC Cricetidae; Cricetinae; Mesocricetus.
OX NCBI_TaxID=10036;
RN [1] {ECO:0000305, ECO:0000312|EMBL:AAC98312.1}
RP NUCLEOTIDE SEQUENCE [MRNA] OF 15-1818, PROTEIN SEQUENCE OF 1-14; 204-214;
RP 224-240; 505-520; 527-540 AND 752-769, AND SUBUNIT.
RC TISSUE=Kidney {ECO:0000269|PubMed:10092680};
RX PubMed=10092680; DOI=10.1074/jbc.274.14.9881;
RA Steinert P.M., Chou Y.H., Prahlad V., Parry D.A., Marekov L.N., Wu K.C.,
RA Jang S.I., Goldman R.D.;
RT "A high molecular weight intermediate filament-associated protein in BHK-21
RT cells is nestin, a type VI intermediate filament protein. Limited co-
RT assembly in vitro to form heteropolymers with type III vimentin and type IV
RT alpha-internexin.";
RL J. Biol. Chem. 274:9881-9890(1999).
CC -!- FUNCTION: Required for brain and eye development. Promotes the
CC disassembly of phosphorylated vimentin intermediate filaments (IF)
CC during mitosis and may play a role in the trafficking and distribution
CC of IF proteins and other cellular factors to daughter cells during
CC progenitor cell division. Required for survival, renewal and mitogen-
CC stimulated proliferation of neural progenitor cells (By similarity).
CC {ECO:0000250}.
CC -!- SUBUNIT: Interacts with FHOD3 (By similarity). Forms homodimers and
CC homotetramers in vitro. In mixtures with other intermediate filament
CC proteins such as vimentin and alpha-internexin, preferentially forms
CC heterodimers which can assemble to form intermediate filaments if
CC nestin does not exceed 25%. {ECO:0000250|UniProtKB:P21263,
CC ECO:0000269|PubMed:10092680}.
CC -!- PTM: Constitutively phosphorylated. This increases during mitosis when
CC the cytoplasmic intermediate filament network is reorganized (By
CC similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the intermediate filament family.
CC {ECO:0000255|PROSITE-ProRule:PRU01188}.
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DR EMBL; AF110498; AAC98312.1; -; mRNA.
DR PIR; T34518; T34518.
DR AlphaFoldDB; Q9Z1Q1; -.
DR SMR; Q9Z1Q1; -.
DR PRIDE; Q9Z1Q1; -.
DR Proteomes; UP000189706; Unplaced.
DR GO; GO:0005882; C:intermediate filament; IEA:UniProtKB-KW.
DR GO; GO:0019215; F:intermediate filament binding; IDA:UniProtKB.
DR GO; GO:0007420; P:brain development; ISS:UniProtKB.
DR GO; GO:0031076; P:embryonic camera-type eye development; ISS:UniProtKB.
DR GO; GO:0030844; P:positive regulation of intermediate filament depolymerization; ISS:UniProtKB.
DR GO; GO:2000179; P:positive regulation of neural precursor cell proliferation; ISS:UniProtKB.
DR InterPro; IPR018039; IF_conserved.
DR InterPro; IPR039008; IF_rod_dom.
DR InterPro; IPR031211; Nestin.
DR PANTHER; PTHR47051; PTHR47051; 4.
DR PROSITE; PS00226; IF_ROD_1; 1.
DR PROSITE; PS51842; IF_ROD_2; 1.
PE 1: Evidence at protein level;
KW Coiled coil; Developmental protein; Direct protein sequencing;
KW Intermediate filament; Isopeptide bond; Neurogenesis; Phosphoprotein;
KW Reference proteome; Ubl conjugation.
FT CHAIN <1..1818
FT /note="Nestin"
FT /id="PRO_0000403464"
FT DOMAIN <1..135
FT /note="IF rod"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01188"
FT REGION <1..>14
FT /note="Coil 1B"
FT /evidence="ECO:0000255"
FT REGION 15..17
FT /note="Linker 2"
FT /evidence="ECO:0000255"
FT REGION 18..135
FT /note="Coil 2B"
FT /evidence="ECO:0000255"
FT REGION 136..1818
FT /note="Tail"
FT /evidence="ECO:0000255"
FT REGION 266..309
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 336..355
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 377..451
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 480..787
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 866..900
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 945..998
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1134..1262
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1334..1818
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 377..395
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 396..447
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 487..692
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 707..787
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 866..893
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 979..998
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1134..1162
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1200..1220
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1334..1365
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1398..1418
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1613..1635
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1685..1709
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 133
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P48681"
FT MOD_RES 137
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P48681"
FT MOD_RES 160
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P48681"
FT MOD_RES 180
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P48681"
FT MOD_RES 210
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P48681"
FT MOD_RES 288
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P48681"
FT MOD_RES 390
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P48681"
FT MOD_RES 400
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P48681"
FT MOD_RES 448
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6P5H2"
FT MOD_RES 513
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P48681"
FT MOD_RES 591
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6P5H2"
FT MOD_RES 737
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6P5H2"
FT MOD_RES 803
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P48681"
FT MOD_RES 824
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6P5H2"
FT MOD_RES 915
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6P5H2"
FT MOD_RES 957
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P21263"
FT MOD_RES 1052
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P48681"
FT MOD_RES 1063
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P48681"
FT MOD_RES 1073
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P21263"
FT MOD_RES 1123
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P48681"
FT MOD_RES 1134
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P48681"
FT MOD_RES 1162
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P48681"
FT MOD_RES 1238
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P48681"
FT MOD_RES 1495
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P48681"
FT MOD_RES 1499
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P48681"
FT MOD_RES 1523
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6P5H2"
FT MOD_RES 1614
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P48681"
FT MOD_RES 1623
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P48681"
FT MOD_RES 1698
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P48681"
FT MOD_RES 1700
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P48681"
FT MOD_RES 1791
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6P5H2"
FT MOD_RES 1814
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P48681"
FT MOD_RES 1815
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P48681"
FT CROSSLNK 1043
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1); alternate"
FT /evidence="ECO:0000250|UniProtKB:P48681"
FT CROSSLNK 1043
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:P48681"
FT NON_CONS 14..15
FT /evidence="ECO:0000303|PubMed:10092680"
FT NON_TER 1
FT /evidence="ECO:0000312|EMBL:AAC98312.1"
SQ SEQUENCE 1818 AA; 200577 MW; 323AC1FF4B0AC4F0 CRC64;
WREKLEAEVQ RQNLYQERVA HMESSLGQAR ERLGRAVRGA REGRLELQQL QAERDGLQER
REALEQRLEG RWQDRLQATE KFQLAVEALE QEKQGLQSQI AQILEGGQQL AHLKMSLSLE
VATYRTLLEA ENSRLQTPGR SSQASLGFQD PKLKLRFLGT PENQHLGSVL PVLSPTPLPS
PLPDTLETPV TAFLKTQEFL QARIPTLAST PIPPMTEAPC LAKAEVRAQD APLSLLQTQG
ERQQAPEPLW AKATASVSTG VLTELEEAGG QQPGHFPEDA TASAPSLSPH HPVLEAKDGD
STESRGSSIF QEDEGQIWEL VEKEAAIELK VESSLAQETQ EDGLHTEEIQ DSQGPLQKET
LEALGEEPLM SLKIQNHETP GKENCNSLRS VDENQGTLKS PEEEKQTLLK SLEEKDVEVE
KTLEKGVPEL SKPLGKEDPR IEDQELMSPE GTLETLSFIG KRNEEVVRSS EEENIESLAA
FKKESQHPLG CPEEEIQRVE RLIEKEGQES LSSPEEEDQE TDRPLEKENG EPLKPVEEED
QLFETLIEKE GQESLSSPEE EDQETDRPLE KEEDQLVERL VEKEGQESLS SPEEEDQETD
RPLEKENGEP LKPVEEEDQL FETLIEKEGQ ESLSSPEEED QETDRPLEKE EDQLVERLVE
KEGQESLSSP EEEDQETDRP LEKEEDQLVE TLIEKQGQEC LSSPEEEDQE TDRPLEKEED
QRVERLIEKE GQESLSSPEE EDQETYRLLE KENGEPLKPV EEEDQRVERL IEKEDQESLS
SLKEEDQRIV KTLERENWES LRSLDENLDT VMPLESKNQK PLKSLEAEEE QRIVKPLEKV
SQDSIGSLEK ENVELLRSLE DDQITESLLK KGTQESLESH EDRNQETQDP QRFLEEEGQG
IVKQLEKENQ GFLGSLEEEK VVKRSLEREN HEPLSSVEKD WVTESLLERE SQDSGKSLEG
QEAFRCLGKE DPESLQFPEV QDQEIQRSLQ QETQQTLGAL GDEQMASEPP EKVGPELLKF
LGNGQEIVRS LEEQNQESLV SVKETSVETA KSSDMEDIEP LKSADEDLEI INSAGAQESL
WSMEVTRETT RPLEKEVQES LGFVGGNQEI LRPLERGNEE LGSLGKWNLE AVDSPEAVEE
GRQPLGEEAC LEMGEHQEPP RSLGEVEQGL PGSGNQQKWE DRAVENAAAD QGPTLGRTGI
ESEDEAELPL SGQGEKEEDA EERELQLDAM GEAWSLASSE PQEPRVPSEG GSAGAPQGLE
GQSEQVGVLG VPVGQGMPEV TEPLLQEDVA QAGKRDPIEL TLGSDAATRA GLGLEQEVAG
SGGSRHLARE EAIHPSLGEE SVEAKIAHDL EGPGKEPKEA GALESEISEL PRTSSDVLES
KGCKQSEPVL GWAVEEASVE ASDHEGSDAP EPRPSETEGD EGAQAALAPP GPKLMEPCSP
TPILKDAYEW QPQAEGTRET GRQLEGGSAS LERVEDEQEF GLGGIPEGLQ DWEESREESE
ADELGETLPD STPLGLYLRS PTSPKWDQAG EQRLSPQGEA RKEGWGPAVP AAQGLSNPPG
EEERGHDSDL SSEEFEDLGT EASLLPGLPK EVADHLGQVP PGPEPECWDQ GGESDGFADE
EESGEEGEEE EHEDGTESGA QWWGSGPSKV QHVTQRGDLQ EHESVGISGP WDDGWRGAAA
GISVTGLETE SQDSAEPSGS EVSESVSSEG EDQAPDHLDT PQGVTNVVPG AGDTFGISGQ
APNLESEHMN GRLENGLEQS EGQGVLDRHQ DQGHPSQQQE VGALKAPLLG SPVHRGPSQS
LEFPLSGADR DSWSSGED
