ID   RGP51_LYMST             Reviewed;         452 AA.
AC   Q6QUW1;
DT   02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   25-MAY-2022, entry version 60.
DE   RecName: Full=Retrograde protein of 51 kDa;
GN   Name=RGP51;
OS   Lymnaea stagnalis (Great pond snail) (Helix stagnalis).
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Gastropoda;
OC   Heterobranchia; Euthyneura; Panpulmonata; Hygrophila; Lymnaeoidea;
OC   Lymnaeidae; Lymnaea.
OX   NCBI_TaxID=6523;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=14973157; DOI=10.1074/mcp.m400004-mcp200;
RA   Perlson E., Medzihradszky K.F., Darula Z., Munno D.W., Syed N.I.,
RA   Burlingame A.L., Fainzilber M.;
RT   "Differential proteomics reveals multiple components in retrogradely
RT   transported axoplasm after nerve injury.";
RL   Mol. Cell. Proteomics 3:510-520(2004).
RN   [2]
RP   IDENTIFICATION BY MASS SPECTROMETRY, AND SULFATION AT SER-156.
RC   TISSUE=Nerve;
RX   PubMed=14752058; DOI=10.1074/mcp.m300140-mcp200;
RA   Medzihradszky K.F., Darula Z., Perlson E., Fainzilber M., Chalkley R.J.,
RA   Ball H., Greenbaum D., Bogyo M., Tyson D.R., Bradshaw R.A.,
RA   Burlingame A.L.;
RT   "O-sulfonation of serine and threonine: mass spectrometric detection and
RT   characterization of a new posttranslational modification in diverse
RT   proteins throughout the eukaryotes.";
RL   Mol. Cell. Proteomics 3:429-440(2004).
CC   -!- SIMILARITY: Belongs to the intermediate filament family.
CC       {ECO:0000255|PROSITE-ProRule:PRU01188}.
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DR   EMBL; AY524862; AAT01542.1; -; mRNA.
DR   AlphaFoldDB; Q6QUW1; -.
DR   SMR; Q6QUW1; -.
DR   PRIDE; Q6QUW1; -.
DR   GO; GO:0005882; C:intermediate filament; IEA:UniProtKB-KW.
DR   InterPro; IPR018039; IF_conserved.
DR   InterPro; IPR039008; IF_rod_dom.
DR   Pfam; PF00038; Filament; 2.
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   Coiled coil; Intermediate filament; Sulfation.
FT   CHAIN           1..452
FT                   /note="Retrograde protein of 51 kDa"
FT                   /id="PRO_0000349090"
FT   DOMAIN          72..424
FT                   /note="IF rod"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01188"
FT   REGION          1..75
FT                   /note="Head"
FT   REGION          1..50
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          76..111
FT                   /note="Coil 1A"
FT   REGION          112..121
FT                   /note="Linker 1"
FT   REGION          122..259
FT                   /note="Coil 1B"
FT   REGION          260..278
FT                   /note="Linker 12"
FT   REGION          279..424
FT                   /note="Coil 2"
FT   REGION          425..452
FT                   /note="Tail"
FT   COMPBIAS        1..15
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        16..50
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         156
FT                   /note="Sulfoserine"
FT                   /evidence="ECO:0000269|PubMed:14752058"
SQ   SEQUENCE   452 AA;  51481 MW;  B3F60C0DD7BE3BA4 CRC64;
     MQKGAKIEDE GRQSRIQSRN FIIQRSDPRT RGSSVYSSRS SSYNVRSSIS PGVYQQLSSS
     GITDFKGNRE KEKREMQNLN ERLASYIEKV HFLDAQVKKL EAENEALRNR KVEDLQPIRD
     AYENELRQAR KVIDELASSK GVAEGKLAGL QDEIGSLREL IVTYESQAKD YRKKIDSLGN
     QLGEFEGELQ SLRLRVGSLE DENAKLRELL EKVQEQNRRL RADLDTETAA HIEADCLAQT
     KTEEAEFYRD LLDQLELLKP EPIQIKGMDY ADFWKSELAK CVREINLAYD EKIDLIQQDC
     EAKYASQINQ LRSGNVKDGM QLQHSQEEVK KLRGQLQDKN AAYAELATRI ASLQAERDEL
     ARQLADIERE LEEQKLKYNR DVGDLESELT SVLAQLQHLM DAKMSLELEI ACYKKLLEGE
     ESRVGLRTLV EQAIGTQSKG SASLKDAIQS SS