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Database: UniProt
Entry: A0A3L8RV95_CHLGU
LinkDB: A0A3L8RV95_CHLGU
Original site: A0A3L8RV95_CHLGU 
ID   A0A3L8RV95_CHLGU        Unreviewed;       736 AA.
AC   A0A3L8RV95;
DT   13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT   13-FEB-2019, sequence version 1.
DT   24-JAN-2024, entry version 18.
DE   RecName: Full=Ig-like domain-containing protein {ECO:0000259|PROSITE:PS50835};
GN   ORFNames=DV515_00015516 {ECO:0000313|EMBL:RLV88244.1};
OS   Chloebia gouldiae (Gouldian finch) (Erythrura gouldiae).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Passeriformes; Passeroidea; Passeridae;
OC   Chloebia.
OX   NCBI_TaxID=44316 {ECO:0000313|EMBL:RLV88244.1, ECO:0000313|Proteomes:UP000276834};
RN   [1] {ECO:0000313|EMBL:RLV88244.1, ECO:0000313|Proteomes:UP000276834}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Red01 {ECO:0000313|EMBL:RLV88244.1};
RC   TISSUE=Muscle {ECO:0000313|EMBL:RLV88244.1};
RX   PubMed=30282656;
RA   Toomey M.B., Marques C.I., Andrade P., Araujo P.M., Sabatino S.,
RA   Gazda M.A., Afonso S., Lopes R.J., Corbo J.C., Carneiro M.;
RT   "A non-coding region near Follistatin controls head colour polymorphism in
RT   the Gouldian finch.";
RL   Proc. R. Soc. B 285:0-0(2018).
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:RLV88244.1}.
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DR   EMBL; QUSF01000189; RLV88244.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A3L8RV95; -.
DR   STRING; 44316.ENSEGOP00005014202; -.
DR   Ensembl; ENSEGOT00005016404; ENSEGOP00005014202; ENSEGOG00005011539.
DR   OMA; NGQHKAT; -.
DR   Proteomes; UP000276834; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   CDD; cd00063; FN3; 1.
DR   CDD; cd05764; IgI_SALM5_like; 1.
DR   Gene3D; 2.60.40.10; Immunoglobulins; 2.
DR   Gene3D; 3.80.10.10; Ribonuclease Inhibitor; 2.
DR   InterPro; IPR003961; FN3_dom.
DR   InterPro; IPR036116; FN3_sf.
DR   InterPro; IPR007110; Ig-like_dom.
DR   InterPro; IPR036179; Ig-like_dom_sf.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR013098; Ig_I-set.
DR   InterPro; IPR003599; Ig_sub.
DR   InterPro; IPR003598; Ig_sub2.
DR   InterPro; IPR001611; Leu-rich_rpt.
DR   InterPro; IPR003591; Leu-rich_rpt_typical-subtyp.
DR   InterPro; IPR032675; LRR_dom_sf.
DR   PANTHER; PTHR45842:SF10; LEUCINE-RICH REPEAT AND FIBRONECTIN TYPE-III DOMAIN-CONTAINING PROTEIN 5; 1.
DR   PANTHER; PTHR45842; SYNAPTIC ADHESION-LIKE MOLECULE SALM; 1.
DR   Pfam; PF07679; I-set; 1.
DR   Pfam; PF13855; LRR_8; 1.
DR   SMART; SM00409; IG; 1.
DR   SMART; SM00408; IGc2; 1.
DR   SMART; SM00369; LRR_TYP; 6.
DR   SUPFAM; SSF49265; Fibronectin type III; 1.
DR   SUPFAM; SSF48726; Immunoglobulin; 1.
DR   SUPFAM; SSF52058; L domain-like; 1.
DR   PROSITE; PS50835; IG_LIKE; 1.
DR   PROSITE; PS51450; LRR; 3.
PE   4: Predicted;
KW   Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW   Immunoglobulin domain {ECO:0000256|ARBA:ARBA00023319};
KW   Leucine-rich repeat {ECO:0000256|ARBA:ARBA00022614};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000276834};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   SIGNAL          1..17
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           18..736
FT                   /note="Ig-like domain-containing protein"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5018250661"
FT   TRANSMEM        525..551
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          287..373
FT                   /note="Ig-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50835"
FT   REGION          383..419
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          609..721
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        387..417
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        609..647
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        660..680
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        702..721
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   736 AA;  80453 MW;  F0E08679B4F1FB52 CRC64;
     MEKLLLFLLF IGIAVRAQIC PKRCVCQILS PNLATLCAKK GLLFVPPNID RRTVELRLAD
     NFVTNIKRKD FANMTSLVDL TLSRNTISFI TPHAFADLRN LRALHLNSNR LTKITNDMFS
     GLSNLHHLIL NNNQLTLISS TAFDDVLALE ELDLSYNNLE TIPWDAVEKM VSLHTLSLDH
     NMIDHIPKGT FSHLHKMTRL DVTSNKLQKL PPDPLFQRAQ VLATSGIISP STFALSFGGN
     PLHCNCELLW LRRLSREDDL ETCASPTLLS GRYFWSIPEE EFLCEPPLIT RHTHELRVLE
     GQRAALRCKA RGDPEPAIHW ISPEGKLISN ATRSTVYDNG TLDILITTVK DTGSFTCIAS
     NPAGEATQTV DLHIIKLPHL LNSTNHIHEP DPGSSDISTS TKSGSNTSSS NGDTKVSQDK
     KVVVAEATSS TALLKFNFQR NIPGIRMFQI QYNGTYDDSL VYRMIPPTSK TFLVNNLAAG
     TMYDLCVLAI YDDGITSLTA TRVVGCTQFT TEQDYVRCHF MQSQFLGGTM IIIIGGIIVA
     SVLVFIIILM IRYKVCNNNG QQKATKVSNV YSQTNGAQIQ GCSGVLSQSM SKQALGHEEG
     IQCCKAASDG VTQSPDTGSS QDSATTTSAL PPAWTSSTPL SQKQKRKSGP KPGSEAQGEA
     GGSSEPQNSN RNNSTALQLA SRPPDAAPAA HTYKRAQSKP KAGASLQDTS PSALPENAAT
     DVVTRQKTIR FQLSED
//
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