GenomeNet

Database: UniProt
Entry: G1Q5Q5_MYOLU
LinkDB: G1Q5Q5_MYOLU
Original site: G1Q5Q5_MYOLU 
ID   G1Q5Q5_MYOLU            Unreviewed;       376 AA.
AC   G1Q5Q5;
DT   19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT   19-OCT-2011, sequence version 1.
DT   27-MAR-2024, entry version 69.
DE   RecName: Full=C-type lectin domain-containing protein {ECO:0000259|PROSITE:PS50041};
OS   Myotis lucifugus (Little brown bat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Chiroptera; Microchiroptera; Vespertilionidae;
OC   Myotis.
OX   NCBI_TaxID=59463 {ECO:0000313|Ensembl:ENSMLUP00000019038.1, ECO:0000313|Proteomes:UP000001074};
RN   [1] {ECO:0000313|Ensembl:ENSMLUP00000019038.1, ECO:0000313|Proteomes:UP000001074}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=21993624; DOI=10.1038/nature10530;
RA   Lindblad-Toh K., Garber M., Zuk O., Lin M.F., Parker B.J., Washietl S.,
RA   Kheradpour P., Ernst J., Jordan G., Mauceli E., Ward L.D., Lowe C.B.,
RA   Holloway A.K., Clamp M., Gnerre S., Alfoldi J., Beal K., Chang J.,
RA   Clawson H., Cuff J., Di Palma F., Fitzgerald S., Flicek P., Guttman M.,
RA   Hubisz M.J., Jaffe D.B., Jungreis I., Kent W.J., Kostka D., Lara M.,
RA   Martins A.L., Massingham T., Moltke I., Raney B.J., Rasmussen M.D.,
RA   Robinson J., Stark A., Vilella A.J., Wen J., Xie X., Zody M.C., Baldwin J.,
RA   Bloom T., Chin C.W., Heiman D., Nicol R., Nusbaum C., Young S.,
RA   Wilkinson J., Worley K.C., Kovar C.L., Muzny D.M., Gibbs R.A., Cree A.,
RA   Dihn H.H., Fowler G., Jhangiani S., Joshi V., Lee S., Lewis L.R.,
RA   Nazareth L.V., Okwuonu G., Santibanez J., Warren W.C., Mardis E.R.,
RA   Weinstock G.M., Wilson R.K., Delehaunty K., Dooling D., Fronik C.,
RA   Fulton L., Fulton B., Graves T., Minx P., Sodergren E., Birney E.,
RA   Margulies E.H., Herrero J., Green E.D., Haussler D., Siepel A., Goldman N.,
RA   Pollard K.S., Pedersen J.S., Lander E.S., Kellis M.;
RT   "A high-resolution map of human evolutionary constraint using 29 mammals.";
RL   Nature 478:476-482(2011).
RN   [2] {ECO:0000313|Ensembl:ENSMLUP00000019038.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- SUBUNIT: Oligomeric complex of 4 set of homotrimers.
CC       {ECO:0000256|ARBA:ARBA00011267}.
CC   -!- SIMILARITY: Belongs to the SFTPD family.
CC       {ECO:0000256|ARBA:ARBA00007899}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AAPE02041800; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   AlphaFoldDB; G1Q5Q5; -.
DR   STRING; 59463.ENSMLUP00000019038; -.
DR   Ensembl; ENSMLUT00000029561.1; ENSMLUP00000019038.1; ENSMLUG00000027676.1.
DR   eggNOG; KOG4297; Eukaryota.
DR   GeneTree; ENSGT00940000155748; -.
DR   HOGENOM; CLU_049894_3_0_1; -.
DR   InParanoid; G1Q5Q5; -.
DR   OMA; QGSKGYM; -.
DR   TreeFam; TF330481; -.
DR   Proteomes; UP000001074; Unassembled WGS sequence.
DR   GO; GO:0005581; C:collagen trimer; IEA:UniProtKB-KW.
DR   GO; GO:0030246; F:carbohydrate binding; IEA:UniProtKB-KW.
DR   Gene3D; 3.10.100.10; Mannose-Binding Protein A, subunit A; 1.
DR   Gene3D; 1.20.5.360; SFTPD helical domain; 1.
DR   InterPro; IPR001304; C-type_lectin-like.
DR   InterPro; IPR016186; C-type_lectin-like/link_sf.
DR   InterPro; IPR018378; C-type_lectin_CS.
DR   InterPro; IPR008160; Collagen.
DR   InterPro; IPR016187; CTDL_fold.
DR   InterPro; IPR015097; Surfac_D-trimer.
DR   PANTHER; PTHR37456:SF4; COLLAGEN ALPHA-1(XIII) CHAIN ISOFORM X2; 1.
DR   PANTHER; PTHR37456; SI:CH211-266K2.1; 1.
DR   Pfam; PF01391; Collagen; 2.
DR   Pfam; PF00059; Lectin_C; 1.
DR   Pfam; PF09006; Surfac_D-trimer; 1.
DR   SMART; SM00034; CLECT; 1.
DR   SUPFAM; SSF56436; C-type lectin-like; 1.
DR   SUPFAM; SSF57944; Triple coiled coil domain of C-type lectins; 1.
DR   PROSITE; PS00615; C_TYPE_LECTIN_1; 1.
DR   PROSITE; PS50041; C_TYPE_LECTIN_2; 1.
PE   3: Inferred from homology;
KW   Calcium {ECO:0000256|ARBA:ARBA00022837};
KW   Collagen {ECO:0000256|ARBA:ARBA00023119};
KW   Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW   Lectin {ECO:0000256|ARBA:ARBA00022734};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001074};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           21..376
FT                   /note="C-type lectin domain-containing protein"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5003418009"
FT   DOMAIN          260..375
FT                   /note="C-type lectin"
FT                   /evidence="ECO:0000259|PROSITE:PS50041"
FT   REGION          44..221
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        71..118
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        182..198
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   376 AA;  38033 MW;  BBF3C874CF5E0246 CRC64;
     KAMLLLSVLV LLTQPPRSRG AEVTTLPQKP LIDACTLVMC SPVENGLPGR DGQDGKDGPR
     GEKGDPGSPG APGPMGMPGP AGPVGPKGDN GPPGEPGPKG DSGPRGPPGP PGVPGPAGPE
     GPSGMQGNVG PQGKPGPKGE PGPKGEVGAP GVQGSAGPRG PPGFRGENGA PGERGAPGFP
     GEAGPAGPPG PQGPPGARGP PGLKGDRGDP GERGPKGESG LPDIAALRQQ VEALQGQVGR
     LQGAFLQYKK VELFPNGRGV GQKVFKSAGF QKPFQEAQQV CVQAGGQLPS PRNAAENEAL
     KQLVEIENKG AAFLSMTDSQ TEGKFIYPGG ESLVYSNWAS GEPSNYRDME DCAEMYTNGQ
     WNDGPCGEKR LVVCEF
//
DBGET integrated database retrieval system