ID L5LFJ9_MYODS Unreviewed; 1190 AA.
AC L5LFJ9;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 27-MAR-2024, entry version 41.
DE SubName: Full=Neural cell adhesion molecule L1-like protein {ECO:0000313|EMBL:ELK25099.1};
GN ORFNames=MDA_GLEAN10023266 {ECO:0000313|EMBL:ELK25099.1};
OS Myotis davidii (David's myotis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Chiroptera; Microchiroptera; Vespertilionidae;
OC Myotis.
OX NCBI_TaxID=225400 {ECO:0000313|EMBL:ELK25099.1, ECO:0000313|Proteomes:UP000010556};
RN [1] {ECO:0000313|Proteomes:UP000010556}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=23258410; DOI=10.1126/science.1230835;
RA Zhang G., Cowled C., Shi Z., Huang Z., Bishop-Lilly K.A., Fang X.,
RA Wynne J.W., Xiong Z., Baker M.L., Zhao W., Tachedjian M., Zhu Y., Zhou P.,
RA Jiang X., Ng J., Yang L., Wu L., Xiao J., Feng Y., Chen Y., Sun X.,
RA Zhang Y., Marsh G.A., Crameri G., Broder C.C., Frey K.G., Wang L.F.,
RA Wang J.;
RT "Comparative analysis of bat genomes provides insight into the evolution of
RT flight and immunity.";
RL Science 339:456-460(2013).
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004479}; Single-
CC pass type I membrane protein {ECO:0000256|ARBA:ARBA00004479}.
CC -!- SIMILARITY: Belongs to the immunoglobulin superfamily.
CC L1/neurofascin/NgCAM family. {ECO:0000256|ARBA:ARBA00008588}.
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DR EMBL; KB112367; ELK25099.1; -; Genomic_DNA.
DR AlphaFoldDB; L5LFJ9; -.
DR eggNOG; KOG3513; Eukaryota.
DR Proteomes; UP000010556; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR CDD; cd00063; FN3; 3.
DR CDD; cd00096; Ig; 1.
DR CDD; cd05731; Ig3_L1-CAM_like; 1.
DR CDD; cd04978; Ig4_L1-NrCAM_like; 1.
DR CDD; cd05845; IgI_2_L1-CAM_like; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 10.
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; IPR026966; Neurofascin/L1/NrCAM_C.
DR PANTHER; PTHR44170:SF51; NEURAL CELL ADHESION MOLECULE L1-LIKE PROTEIN ISOFORM X1; 1.
DR PANTHER; PTHR44170; PROTEIN SIDEKICK; 1.
DR Pfam; PF13882; Bravo_FIGEY; 1.
DR Pfam; PF00041; fn3; 3.
DR Pfam; PF07679; I-set; 1.
DR Pfam; PF13927; Ig_3; 4.
DR SMART; SM00060; FN3; 4.
DR SMART; SM00409; IG; 6.
DR SMART; SM00408; IGc2; 5.
DR SUPFAM; SSF49265; Fibronectin type III; 2.
DR SUPFAM; SSF48726; Immunoglobulin; 6.
DR PROSITE; PS50853; FN3; 3.
DR PROSITE; PS50835; IG_LIKE; 6.
PE 3: Inferred from homology;
KW Cell adhesion {ECO:0000256|ARBA:ARBA00022889};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Immunoglobulin domain {ECO:0000256|ARBA:ARBA00023319};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000010556};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}; Signal {ECO:0000256|SAM:SignalP};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT SIGNAL 1..24
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 25..1190
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003970161"
FT TRANSMEM 1064..1085
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 35..124
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 128..223
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 240..326
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 331..417
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 423..510
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 515..607
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 614..709
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 714..807
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 899..996
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT REGION 693..720
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 988..1009
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1094..1134
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1171..1190
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1094..1130
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1174..1190
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1190 AA; 130776 MW; F1F42B008E367724 CRC64;
MERLPGAGGA VFSLLSLLLH LASASEIPLS VPQVPTITKQ SKEQVAFPFD EYFQIECEAK
GNPEPRFTWT KDGKPFDLSD PRVIASNNSG TFRIPNEGQI AHFQGKYRCF ASNKLGVAMS
EEIEFIVPNV PKFPKEKIEP LEVEEGDPLV LPCNPPTGLP PLHIYWMNIE LEHIQQDERV
YMSQEGDLYF ANVEEHDSRN DYCCFAAFPR LRTIVQKMPM KLTVNSSNSI KQRKPSLLLP
PVARGPESAV TVLRGDTLVL ECFAEGLPTP QVGWEKVGGD LPKGRETKEN YGKMLKIENV
SYEDKGNYRC TANNFLGVAT HDFHVTVEEP PRWTKKPQSG VYSTRSSGIL LCEAEGEPEP
VIRWRVNGIP IEENPFAGDV VSPGEVSFTD LQPNHTAVYQ CEASNAHGTI LANANVDVVD
VRPLIETEDE ESYAAVAGSS AFLLCEFFAS PQAMVSWQKA DAARPLEGPR YHVHTNGTLQ
IREATVEDAG AYSCWVENAQ GKTAVTASLD IRNATRLQVS PRDPRVPRSH TLELHCESEC
DPHLKPSLRL TWSKGGAAFE TNGTEDGRIL IDGAHLTISN LTLEDQGVYT CSAHTALDSA
ANETHVTVLD VPDPPENLRL SERQNRSVRL TWDAGDSHNS NISGYVVEFE GNREEPGRWE
QLAAVPGGET TVLLTLAPYV RYQFRVIAAN EVGRSRPSRP SEHHETPPAA PDKNPQNVRV
QASQPKEMVI RWEPLKSTEQ NGPGLEYRVA WKPLGALGEW EEETVREHSL RVMTPAIYAP
YEVQVQALNH LGAGPQPQSV VLHSGEDYPD AAPVIHGVDV VNSTLAKINW WKTKSLADGR
SLPKEVSILR FPGQRSSGML PALDAFSEFH LTVLAFNAKG AGPESEPYVF QTPEGVPEQP
TFLKVIKVDK DTATLAWGPP RKLNGNLTGY LLQYQIINDT DEIGELNDVS ITAPSKPSWR
LSNLNATTKY KFYVRACTSR GCGKPVTEET ATLGESSRGP GKLPEGVNAT EKVHPPEVPE
PGAEHAVRLL PKNWVGNNSI FEDVIEARGR EYAGLYDDIA TQGWFIGLMG AIAVLTLVLL
TICFVKRSRG GKYSVKDKED LHPDPDVQSG KDETFGDYSD SDEKPLKGSL RSLTRDLPAT
ESADSLVPYG DGDHGLFSED GSFIGAYAGS KEKGSVESNG SSTATFPLRA
//
