ID L5JQ78_PTEAL Unreviewed; 376 AA.
AC L5JQ78;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 27-MAR-2024, entry version 43.
DE SubName: Full=Neurexin-3-alpha {ECO:0000313|EMBL:ELK01102.1};
GN ORFNames=PAL_GLEAN10020706 {ECO:0000313|EMBL:ELK01102.1};
OS Pteropus alecto (Black flying fox).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Chiroptera; Megachiroptera; Pteropodidae;
OC Pteropodinae; Pteropus.
OX NCBI_TaxID=9402 {ECO:0000313|EMBL:ELK01102.1, ECO:0000313|Proteomes:UP000010552};
RN [1] {ECO:0000313|Proteomes:UP000010552}
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 -!- FUNCTION: Neuronal cell surface protein that may be involved in cell
CC recognition and cell adhesion. May mediate intracellular signaling.
CC {ECO:0000256|ARBA:ARBA00043901}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00076}.
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DR EMBL; KB031153; ELK01102.1; -; Genomic_DNA.
DR AlphaFoldDB; L5JQ78; -.
DR STRING; 9402.L5JQ78; -.
DR eggNOG; KOG3514; Eukaryota.
DR InParanoid; L5JQ78; -.
DR Proteomes; UP000010552; Unassembled WGS sequence.
DR CDD; cd00054; EGF_CA; 1.
DR CDD; cd00110; LamG; 1.
DR Gene3D; 2.60.120.200; -; 2.
DR Gene3D; 2.10.25.10; Laminin; 1.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR000742; EGF-like_dom.
DR InterPro; IPR000152; EGF-type_Asp/Asn_hydroxyl_site.
DR InterPro; IPR001791; Laminin_G.
DR PANTHER; PTHR15036:SF57; NEUREXIN-3; 1.
DR PANTHER; PTHR15036; PIKACHURIN-LIKE PROTEIN; 1.
DR Pfam; PF00008; EGF; 1.
DR Pfam; PF02210; Laminin_G_2; 1.
DR SMART; SM00282; LamG; 1.
DR SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 2.
DR PROSITE; PS00010; ASX_HYDROXYL; 1.
DR PROSITE; PS50026; EGF_3; 1.
DR PROSITE; PS50025; LAM_G_DOMAIN; 1.
PE 4: Predicted;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW EGF-like domain {ECO:0000256|ARBA:ARBA00022536, ECO:0000256|PROSITE-
KW ProRule:PRU00076}; Glycoprotein {ECO:0000256|ARBA:ARBA00023207};
KW Heparan sulfate {ECO:0000256|ARBA:ARBA00023207};
KW Proteoglycan {ECO:0000256|ARBA:ARBA00023207};
KW Reference proteome {ECO:0000313|Proteomes:UP000010552};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT DOMAIN 71..263
FT /note="Laminin G"
FT /evidence="ECO:0000259|PROSITE:PS50025"
FT DOMAIN 267..304
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
SQ SEQUENCE 376 AA; 42244 MW; 84133519146BCBF1 CRC64;
MWKLYHLNSC RGLRGDSVQG GVGIYERGTC QVVYKNNDIR LELSRLARIG DTKMKIYGEV
VFKCENVATL DPINFETPEA YISLPKWNTK RMGSISFDFR TTEPNGLILF THGKPQERKD
ARSQKNTKVD FFAVELLDGN LYLLLDMGSG TIKVKATQKK ANDGEWYHVD IQRDGRSGTI
SVNSRRTPFT ASGESEILDL EGDMYLGGLP ENRAGLILPT ELWTAMLNYG YVGCIRDLFI
DGRSKNIRQL AEMQNAAGVK SSCSRMSAKQ CDSYPCKNNA VCKDGWNRFI CDCTGTGYWG
RTCEREASIL SYDGSMYMKI IMPMVMHTEA EDVSFRFMSQ RAYGLLVATT SRDSADTLRL
ELDGGRVKLM VNLGIV
//
