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Database: UniProt
Entry: A0A195FK63_9HYME
LinkDB: A0A195FK63_9HYME
Original site: A0A195FK63_9HYME 
ID   A0A195FK63_9HYME        Unreviewed;      1687 AA.
AC   A0A195FK63;
DT   05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2016, sequence version 1.
DT   27-MAR-2024, entry version 27.
DE   SubName: Full=Collagen alpha-2(XI) chain {ECO:0000313|EMBL:KYN40652.1};
GN   ORFNames=ALC56_04961 {ECO:0000313|EMBL:KYN40652.1};
OS   Trachymyrmex septentrionalis.
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Formicoidea;
OC   Formicidae; Myrmicinae; Trachymyrmex.
OX   NCBI_TaxID=34720 {ECO:0000313|EMBL:KYN40652.1, ECO:0000313|Proteomes:UP000078541};
RN   [1] {ECO:0000313|EMBL:KYN40652.1, ECO:0000313|Proteomes:UP000078541}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Tsep2-gDNA-1 {ECO:0000313|EMBL:KYN40652.1};
RC   TISSUE=Whole body {ECO:0000313|EMBL:KYN40652.1};
RA   Nygaard S., Hu H., Boomsma J., Zhang G.;
RT   "Trachymyrmex septentrionalis WGS genome.";
RL   Submitted (MAR-2016) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; KQ981522; KYN40652.1; -; Genomic_DNA.
DR   STRING; 34720.A0A195FK63; -.
DR   Proteomes; UP000078541; Unassembled WGS sequence.
DR   GO; GO:0005581; C:collagen trimer; IEA:UniProtKB-KW.
DR   GO; GO:0005201; F:extracellular matrix structural constituent; IEA:InterPro.
DR   GO; GO:0048856; P:anatomical structure development; IEA:UniProt.
DR   Gene3D; 2.60.120.1000; -; 1.
DR   Gene3D; 2.60.120.200; -; 1.
DR   InterPro; IPR008160; Collagen.
DR   InterPro; IPR013320; ConA-like_dom_sf.
DR   InterPro; IPR000885; Fib_collagen_C.
DR   InterPro; IPR001791; Laminin_G.
DR   InterPro; IPR048287; TSPN-like_N.
DR   PANTHER; PTHR24023; COLLAGEN ALPHA; 1.
DR   PANTHER; PTHR24023:SF1105; MULTIPLEXIN, ISOFORM R; 1.
DR   Pfam; PF01410; COLFI; 1.
DR   Pfam; PF01391; Collagen; 9.
DR   Pfam; PF02210; Laminin_G_2; 1.
DR   SMART; SM00038; COLFI; 1.
DR   SMART; SM00210; TSPN; 1.
DR   SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 1.
DR   PROSITE; PS51461; NC1_FIB; 1.
PE   4: Predicted;
KW   Collagen {ECO:0000313|EMBL:KYN40652.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000078541}.
FT   DOMAIN          1464..1687
FT                   /note="Fibrillar collagen NC1"
FT                   /evidence="ECO:0000259|PROSITE:PS51461"
FT   REGION          264..286
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          344..406
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          426..1301
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1318..1420
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        389..403
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        582..596
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        651..675
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        955..971
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1344..1358
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1687 AA;  172133 MW;  C979BFAF9D0C08D2 CRC64;
     MRLLDHTRGQ WRTLRSTWIM LLVHSLFLML LILSGLQRNA VDAALQDASK NVTDIIEAMG
     MQEQLFGVRR TESRCRDDTI AYDIMEAAIL MAPTNVLFPA GIPQDFSILV VAKPRANEST
     SEDYSTSVLF TIYGDSGEEQ LILSLGRDIK FLYSINPDDR NEPISFDVNT SDGQWHRLGV
     SIKGDAVTII LDCNRHITKK LRRNVEKTIA GILMIGQQLK GDLYLGSLEM LKIALNPDAA
     YEICTTFAPD CERESRYGLN YNSSFNEDDY EEENESEDDN RNFLPHGTIT NTINGLTSAT
     KNSTSYEVEI TTMVNVYNAE SNHQQNYGES TNNPYDEEYI KRYNTRGSPG LRGFPGPPGV
     PGPSGEKGEP GRDGLPGLPG VSGPPGNVFV VPSLNQQGNE KGPDSQAEML RQMISQHMLA
     MRGVEGPMGL TGVQGPDGPP GPQGQKGEPG SSGNPGREGR RGRPGRDGER GLSGLPGMKG
     EQGQIGLPGL PGDKGERGSS GKPGESGLPG HEGMQGEDGP PGLPGLPGEL GPRGFIGSRG
     FPGLPGNPGI PGNEGPPGIK GNVGPLGPPG APGQSGPTGS IGPPGPQGPP GPIGLVGPQG
     KPGIPGLSGA DGSPGLPGNP GILGTKGEQG PPGLQGPMGF PGVRGVKGDE GQRGLAGERG
     EKGDRGLEGE KGDTGAKGEP GTTGPQGIPG LEGLEGPKGF EGFRGETGPA GLPGEKGKIG
     LPGYAGYPGN PGEKGDKGQL GNQGASGDKG ERGNNGLQGE RGTTGPRGFR GTRGRRGAEG
     LPGSKGDTGQ PGPAGPSGEI GSPGVEGPRG FTGPSGPLGL DGKDGIPGPP GERGPTGESG
     SPGPPGIPGV IGLPGPPGEL GQPGEPGASG SPGAPGEIGI PGEQGKEGPP GPAGLTGLKG
     SPGPGGLPGF PGERGLSGLP GLPGLKGEMG PIGAQGLSGD KGIQGEPGKD GSPGPEGKQG
     HKGDEGSIGL KGEKGDPGPV GPIGRDGLPG QRGLPGPPGP VGSPGEDGDK GNVGPPGEKG
     FKGSQGDIGF PGPQGVQGPR GESGLVGSPG QKGPPGEIGQ RGSKGEDGPV GATGPAGSVG
     SSGLPGQSGV KGEVGDPGTI GPIGPIGIPG ERGPRGSKGL KGTDGPTGPE GRQGEKGDDG
     MQGAPGKPGL EGTQGERGLP GIKGEEGKLG LLGLPGLRGL TGPEGPKGDA GLPGLPGPPG
     EPGLMGAKGE PGKDGEDGRV GDPGVPGEDG LPGKEGLPGP PGKSGPEGPA GQQGNTGLPG
     EKGDIGLPGA PGFEGPVGPQ GPPGLSGLPG ERGLPGAAGE NGIVGMPGAV GAPGIIGPIG
     SKGQKGDKGR RGIKGYRGES GLIGIKGDHG KRGEKGDRGL PGTQGFKGNP GHPGQVGSRG
     EQGFVGLPGL PGPSGLKGNA GNEGMRGDVG PAGPPGPPGP PGLSIGQSDF DRIIPSIYRD
     QSARRKRDAF EDIDEEEMFD KKLSEIKKAF YNIRQELHLM RKPIGTRDNP ARTCRDLFYG
     HPDFKDGWYW IDPNLGMPDD AISVICNITN MGETCIFPDI HSSHMPSIPW RKEDNKTDWY
     SHLRGGFRIS YETIGIVQMN FLRLLSQEAY QNFTYTCTNS VAWYDGENRS YNLSLRLLGD
     NGDEFSYNNI RPHLIADECK SRSGKEETVF LIRTSKLQQL PLIDFYPVDY GLPQQAFGFK
     VGPVCFK
//
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