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Database: UniProt
Entry: A0A091CUF9_FUKDA
LinkDB: A0A091CUF9_FUKDA
Original site: A0A091CUF9_FUKDA 
ID   A0A091CUF9_FUKDA        Unreviewed;      1455 AA.
AC   A0A091CUF9;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   27-MAR-2024, entry version 32.
DE   SubName: Full=Keratin, type II cytoskeletal 1 {ECO:0000313|EMBL:KFO21255.1};
GN   ORFNames=H920_17303 {ECO:0000313|EMBL:KFO21255.1};
OS   Fukomys damarensis (Damaraland mole rat) (Cryptomys damarensis).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Hystricomorpha; Bathyergidae;
OC   Fukomys.
OX   NCBI_TaxID=885580 {ECO:0000313|EMBL:KFO21255.1, ECO:0000313|Proteomes:UP000028990};
RN   [1] {ECO:0000313|EMBL:KFO21255.1, ECO:0000313|Proteomes:UP000028990}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   TISSUE=Liver {ECO:0000313|EMBL:KFO21255.1};
RA   Gladyshev V.N., Fang X.;
RT   "The Damaraland mole rat (Fukomys damarensis) genome and evolution of
RT   African mole rats.";
RL   Submitted (NOV-2013) to the EMBL/GenBank/DDBJ databases.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC   -!- SIMILARITY: Belongs to the intermediate filament family.
CC       {ECO:0000256|RuleBase:RU000685}.
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DR   EMBL; KN124398; KFO21255.1; -; Genomic_DNA.
DR   STRING; 885580.ENSFDAP00000011128; -.
DR   eggNOG; ENOG502QQIF; Eukaryota.
DR   Proteomes; UP000028990; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0045095; C:keratin filament; IEA:InterPro.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
DR   Gene3D; 1.20.5.170; -; 3.
DR   Gene3D; 1.20.5.500; Single helix bin; 2.
DR   Gene3D; 1.20.5.1160; Vasodilator-stimulated phosphoprotein; 3.
DR   InterPro; IPR018039; IF_conserved.
DR   InterPro; IPR039008; IF_rod_dom.
DR   InterPro; IPR032444; Keratin_2_head.
DR   InterPro; IPR003054; Keratin_II.
DR   InterPro; IPR018159; Spectrin/alpha-actinin.
DR   PANTHER; PTHR45616; GATA-TYPE DOMAIN-CONTAINING PROTEIN; 1.
DR   PANTHER; PTHR45616:SF33; KERATIN, TYPE II CYTOSKELETAL 1; 1.
DR   Pfam; PF00038; Filament; 4.
DR   Pfam; PF16208; Keratin_2_head; 3.
DR   PRINTS; PR01276; TYPE2KERATIN.
DR   SMART; SM01391; Filament; 3.
DR   SMART; SM00150; SPEC; 2.
DR   SUPFAM; SSF64593; Intermediate filament protein, coiled coil region; 8.
DR   PROSITE; PS00226; IF_ROD_1; 3.
DR   PROSITE; PS51842; IF_ROD_2; 3.
PE   3: Inferred from homology;
KW   Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW   Coiled coil {ECO:0000256|ARBA:ARBA00023054, ECO:0000256|SAM:Coils};
KW   Intermediate filament {ECO:0000256|ARBA:ARBA00022754,
KW   ECO:0000256|RuleBase:RU000685}; Keratin {ECO:0000256|ARBA:ARBA00022744};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136};
KW   Reference proteome {ECO:0000313|Proteomes:UP000028990}.
FT   DOMAIN          140..453
FT                   /note="IF rod"
FT                   /evidence="ECO:0000259|PROSITE:PS51842"
FT   DOMAIN          665..978
FT                   /note="IF rod"
FT                   /evidence="ECO:0000259|PROSITE:PS51842"
FT   DOMAIN          1198..1455
FT                   /note="IF rod"
FT                   /evidence="ECO:0000259|PROSITE:PS51842"
FT   COILED          216..243
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          351..424
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          720..810
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          876..956
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          1281..1434
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   1455 AA;  158402 MW;  12A1180928C162F0 CRC64;
     MPLEFQLDSG LPTNANLQRN TVNAEHDGEG TLKDTNAKLH DLKVALQQAR EDLARDLSPS
     PSDLGPSPIF PDGWHSSSKA VGKTDLVEKP LIHRASNFGP GGFGPSYPPG GIREVTINQS
     LLEPLHLEVD PEIQRIKIQE REQIKVLNNK FASFIDKVRF LEQQNQVLQT KWELLQQVDT
     TTQNSNLESF FESYISGLQK KVDFLNNEQM RKNSEIRSMQ DTVEDYKSKY EEEINKRTSA
     ENDFVVLKKD VDAAYVSKTD LESKVDTLLG EVNFLKYLFQ MELSQMQTHI SDTNVILSMD
     NNRTLDLDSI IEAVQAEYEL IVQRSKDEAE MLYQTKYQEL QISAGRQGDD LKNTKMEIAE
     LNRNIQRLQA EIGSVKKQIE QMHSAISDAE ERGQQALEDA KQKLQDMDEA LQQSKESLAR
     LLRDYQAMLG AKLSLDVEIA TYRKLLECEE SRMSGEMQNQ VSISVESNQV TLSGGAAGGS
     GGYGGGGGYS GGGGNFGANM SRQYSSRSLC RSGGKGFSSG SAGLVSFQRR STSSVRRSGG
     GGGRFSGGFC GSGGGGGGFG SRSLINLGGS KSISINVAGG GSRSGFGYGG GVFGGGVFGG
     GVFGGGGLGG GNFGSGGGFG GGGYGGGFGP VCPPGGIQEV TINQSLLQPL NVEIDPEIQK
     IKSQEREQIK TLNNQFASFI DKVRFLEQQN QVLQTKWELL QQVDTSTRSF SLEPYFEAYI
     SDLRKQVDRL RSDQSRMDSE LKTMQDMVED YRNKYEDEIN KRTNAENEFV TIKKDVDSAY
     MNKVDLQAKV DNLRQEIDFL TALYEAELSQ MQTHISETSV ILSMDNNRSL DLDSIIAEVK
     AQYEDIAQRS KAEAEALYQT KYEELQVTAG KHGDSVKTSK MEISELNRVI QRLRSEIDSV
     KKQISQLHQS IADAEQRGEN ALKDAQNKLN ELEDALQQAK EDLARLLRDY QELMNVKLAL
     DVEIATYRTL LEGEESRMSG ECSANVSMSL ALIRNLQVSS LYKAIMSCQN SCKSRGGVGG
     GGGRRGGGGG GGGFRGFSSG SAIVSGGSRR STSSFSCLSR HGGGGGGRGG GCGAGGFGSQ
     SVVSLGGSKS ISICVAGRGG SFGSGGGFGG RGGSFGGFGG GSSFGGGSGF GGGGFVGGSV
     GGGRFGGGGG PGGFGGPGGF GPGGILGGGI HEVSVNQSLL QPLDVKVDPE IQNIKSQERE
     QIKALNNKFA SFIDKVRFLE QQNQVLKTKW DLLQQLDVRS RTTNLEPLFQ TYISLLLKQV
     DTLSSERTAQ DSELNHMHDL VEDYKKKFED EINKRTAAEN DFVTLKKDVD NGYTIKVALQ
     ANVEALAQEI DFLRRLYEEY EELQLVAGKH GDSLREIKME ISELNRMIQR LQGEISHVKK
     QCKCVQDAIA EAEQRGEHAI KDAQQKLIDL EEALQQARED LARLLRDYQE LMSTKLSLDI
     EIATYRKLLE GEECR
//
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