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Database: UniProt
Entry: H3AFI7_LATCH
LinkDB: H3AFI7_LATCH
Original site: H3AFI7_LATCH 
ID   H3AFI7_LATCH            Unreviewed;       825 AA.
AC   H3AFI7;
DT   18-APR-2012, integrated into UniProtKB/TrEMBL.
DT   18-APR-2012, sequence version 1.
DT   27-MAR-2024, entry version 69.
DE   RecName: Full=IF rod domain-containing protein {ECO:0000259|PROSITE:PS51842};
GN   Name=LOC102366449 {ECO:0000313|Ensembl:ENSLACP00000008408.1};
OS   Latimeria chalumnae (Coelacanth).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Coelacanthiformes; Coelacanthidae; Latimeria.
OX   NCBI_TaxID=7897 {ECO:0000313|Ensembl:ENSLACP00000008408.1, ECO:0000313|Proteomes:UP000008672};
RN   [1] {ECO:0000313|Proteomes:UP000008672}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Wild caught {ECO:0000313|Proteomes:UP000008672};
RA   Di Palma F., Alfoldi J., Johnson J., Berlin A., Gnerre S., Jaffe D.,
RA   MacCallum I., Young S., Walker B.J., Lander E., Lindblad-Toh K.;
RT   "The draft genome of Latimeria chalumnae.";
RL   Submitted (AUG-2011) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSLACP00000008408.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
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DR   EMBL; AFYH01157184; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   AlphaFoldDB; H3AFI7; -.
DR   STRING; 7897.ENSLACP00000008408; -.
DR   Ensembl; ENSLACT00000008476.1; ENSLACP00000008408.1; ENSLACG00000007444.1.
DR   eggNOG; KOG1216; Eukaryota.
DR   GeneTree; ENSGT00940000161685; -.
DR   HOGENOM; CLU_343449_0_0_1; -.
DR   InParanoid; H3AFI7; -.
DR   OMA; PEIKCHL; -.
DR   TreeFam; TF330122; -.
DR   Proteomes; UP000008672; Unassembled WGS sequence.
DR   Bgee; ENSLACG00000007444; Expressed in chordate pharynx and 2 other cell types or tissues.
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; IPR039008; IF_rod_dom.
DR   InterPro; IPR002957; Keratin_I.
DR   PANTHER; PTHR45652; GLIAL FIBRILLARY ACIDIC PROTEIN; 1.
DR   PANTHER; PTHR45652:SF10; NEUROFILAMENT MEDIUM POLYPEPTIDE ISOFORM X1; 1.
DR   Pfam; PF00038; Filament; 1.
DR   PRINTS; PR01248; TYPE1KERATIN.
DR   SMART; SM01391; Filament; 1.
DR   SUPFAM; SSF64593; Intermediate filament protein, coiled coil region; 2.
DR   PROSITE; PS51842; IF_ROD_2; 1.
PE   4: Predicted;
KW   Coiled coil {ECO:0000256|ARBA:ARBA00023054, ECO:0000256|SAM:Coils};
KW   Intermediate filament {ECO:0000256|ARBA:ARBA00022754};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008672}.
FT   DOMAIN          87..397
FT                   /note="IF rod"
FT                   /evidence="ECO:0000259|PROSITE:PS51842"
FT   REGION          1..30
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          496..521
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          536..825
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          105..222
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          255..368
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        536..743
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        752..786
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        787..801
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        802..825
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   825 AA;  93778 MW;  0C43D4E607F03E46 CRC64;
     MSYMDFLTTR PRRGAQGDHP RLQTRVPGSL SSGVPFPRLS SIPASANYIH RSNALLKREY
     ISPTFKPSDS LEFTQIVGDL NVPNVTEKEI LQKLNERFAG FIDNVHHLEV QNSNLEAEIE
     TLRCTQSSPS LAEFYEPYIR DLRELIQEVN SQKTQIQLAH QQLEEDLENW SQKCQAEAQI
     REDTEANVRA LKKETGDANL LKLELEKKAQ SLADEIVFLK KNHEEEVTEL MSQMQDPQVT
     YEMKGILKPN ITAALKDLRA QLEGHTNNNM QQAEELFKSR VAKLAKAAEI NNDALQTTRQ
     EIIEYRKQLQ SKSTELEAVR GTKESLEKQL DHLEERHDAE IAYFQNTIQQ LECELKDTKW
     EMANHLREYQ ELLNVKMALD VEIASYRRLL EGEENRITSV SGSFTAPIGL QEQVATYTAE
     EVAKQKTDPV KIEPQYKFVE EIITETTKEI EMTDIEECQG LPETETSLEE EKLSSDQPIE
     LEKVEETAKV VEALSEKVEE DQTEKHEEGK QETTCEAEEG KEEILAATAE VMREAQGEVL
     GDKTVEPKVE TMEHGESLPS MEEDKSVSEE IPKEREEKDE GDEKRATTGS KEGKEVHVDI
     EATKESEQGE EEEDKKEKQG DLESKLDATL EVKEKLGDHS KKEEEPLESI VGKEELITSD
     EEQEKSIDEV KEENVRLLKS EVSLTTVEKD EEEDKESSKK AEKKEDEETV AKGSEKCEDS
     KHVEKGEDSK SEGKQKEQTQ EAAIPPEEPR GQEAGKVQET SKEKAMEEYS KEAPKEPEEK
     SQEDIESQAE VSQAVQSAEE TQVRDQQEEA KSDLSDNGKK QVHGD
//
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