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Database: UniProt
Entry: Q3ZAL9_DROME
LinkDB: Q3ZAL9_DROME
Original site: Q3ZAL9_DROME 
ID   Q3ZAL9_DROME            Unreviewed;      1028 AA.
AC   Q3ZAL9;
DT   27-SEP-2005, integrated into UniProtKB/TrEMBL.
DT   27-SEP-2005, sequence version 1.
DT   27-MAR-2024, entry version 84.
DE   SubName: Full=IP13787p {ECO:0000313|EMBL:AAZ86771.1};
DE   Flags: Fragment;
GN   Name=CG33274-RA {ECO:0000313|EMBL:AAZ86771.1};
OS   Drosophila melanogaster (Fruit fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC   Drosophilidae; Drosophila; Sophophora.
OX   NCBI_TaxID=7227 {ECO:0000313|EMBL:AAZ86771.1};
RN   [1] {ECO:0000313|EMBL:AAZ86771.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Stapleton M., Carlson J., Chavez C., Frise E., George R., Pacleb J.,
RA   Park S., Wan K., Yu C., Celniker S.;
RL   Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; BT023850; AAZ86771.1; -; mRNA.
DR   AlphaFoldDB; Q3ZAL9; -.
DR   EnsemblMetazoa; FBtr0299840; FBpp0289118; FBgn0263219.
DR   VEuPathDB; VectorBase:FBgn0263219; -.
DR   Bgee; FBgn0263219; Expressed in central nervous system and 11 other cell types or tissues.
DR   ExpressionAtlas; Q3ZAL9; baseline and differential.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0009653; P:anatomical structure morphogenesis; IEA:UniProt.
DR   GO; GO:0030154; P:cell differentiation; IEA:UniProt.
DR   GO; GO:0048731; P:system development; IEA:UniProt.
DR   CDD; cd00063; FN3; 6.
DR   Gene3D; 2.60.40.10; Immunoglobulins; 7.
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; IPR003598; Ig_sub2.
DR   PANTHER; PTHR44170:SF30; FIBRONECTIN TYPE-III DOMAIN-CONTAINING PROTEIN; 1.
DR   PANTHER; PTHR44170; PROTEIN SIDEKICK; 1.
DR   Pfam; PF00041; fn3; 6.
DR   Pfam; PF07679; I-set; 1.
DR   PRINTS; PR00014; FNTYPEIII.
DR   SMART; SM00060; FN3; 6.
DR   SMART; SM00408; IGc2; 1.
DR   SUPFAM; SSF49265; Fibronectin type III; 3.
DR   SUPFAM; SSF48726; Immunoglobulin; 1.
DR   PROSITE; PS50853; FN3; 6.
DR   PROSITE; PS50835; IG_LIKE; 1.
PE   2: Evidence at transcript level;
KW   Immunoglobulin domain {ECO:0000256|ARBA:ARBA00023319};
KW   Membrane {ECO:0000256|SAM:Phobius}; Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        736..757
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          18..118
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   DOMAIN          123..229
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   DOMAIN          234..329
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   DOMAIN          333..428
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   DOMAIN          430..518
FT                   /note="Ig-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50835"
FT   DOMAIN          520..613
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   DOMAIN          614..709
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   REGION          797..816
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          872..1017
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        872..899
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        928..943
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        961..989
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1000..1014
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:AAZ86771.1"
SQ   SEQUENCE   1028 AA;  114914 MW;  BB51150ACF458884 CRC64;
     FGQDEMSIQL IVQEVPEQPK NLRINSQQSR SLQLTWSQPF AGNSPIEEYH IYYKQISDFF
     SPSDIWQNAE HLTIAGAQTV INIQQLRPAK AYHIRMSAEN KLGASEFSEV VQVTTLEEVP
     SGPPLAVRAE PKSSTEIFVT WDAPERDHWN GILLGYYVGY QMSLTPEDKE VNPTQGFSFK
     TVEVRSHFGG ETVLANLNKF TQYHVIVQAY TSQGSGPPSK EIAVQTMEDV PSSPPESPQC
     DVLGSTSIYI TWSPPDIDGQ NGKIKGYKVF YISVDELYET DPEVVKSTNQ YVTIENLRKY
     TNYTVWVLAY TKVGDGMKTK PFYCRTHEDV PSAPQAIKAI PASSSKIIIS WLPPDLPNGD
     ITGYTFYMSM LEGGREEGTH KRLLGPFVEM HETVRTQESA TYQFWLTAST KMGEGEKTQV
     VTVPPNNKVP ARIVSFSQRI VTPWKEHLEL PCRKVGAPAP VTIWRQDGHN METSARKTIA
     KNGTLYMKEC QASDAGNYTC SVENTWGKDE IVYNIVVKVP PEAPNLTVIN AYTDSLLLEW
     MDNSHGGSPI LGYVINYKRD NGDWEELQVD SKTTSHLLTN LWCGTRYQLY ITAYNKIGTG
     LPCDIVNSYT KGNPPVQPKH SQMITNNSTS VTCWLDSWGD GGCGILYFMI ESRVYGRSSW
     AVVSNHIPPT ERIYTVSDLV PGTKYQLKVT AHNNAGSTTA IYNFTTLSTQ GVIYNNDHST
     PVSHLSDLPF YANFKLLLPI CFSLLMLLAL IGAALFLRKR KLASQARLAS SSMSESPSLA
     NLQNKQNRDQ QYLAVRCNPG TSAPRGSNSN DSGSFGKAEG NEYIEDICPY ATFQLNKQTY
     SESSYSGNVY SGPYHSVRGS FVYHDVKPES YHSKEPEYTK VRRKVGRLRD PHSESQEYDT
     LGSESDNDVS ARALNSAKYR AQRDTQDETS SSSETTPTSM TRKSKPPFAA RKGGKPGTSG
     KRHVRSSSGY SSHNEETTFS ISNYPPNYQD HINPPARFSD ANDKTKTQTS PRMRANQKLH
     REAFQINV
//
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