ID A0A2Y9NL96_DELLE Unreviewed; 429 AA.
AC A0A2Y9NL96;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE SubName: Full=Neurexin 3 isoform X19 {ECO:0000313|RefSeq:XP_022432117.1};
GN Name=NRXN3 {ECO:0000313|RefSeq:XP_022432117.1};
OS Delphinapterus leucas (Beluga whale).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Whippomorpha; Cetacea; Odontoceti;
OC Monodontidae; Delphinapterus.
OX NCBI_TaxID=9749 {ECO:0000313|Proteomes:UP000248483, ECO:0000313|RefSeq:XP_022432117.1};
RN [1] {ECO:0000313|RefSeq:XP_022432117.1}
RP IDENTIFICATION.
RC TISSUE=Blood {ECO:0000313|RefSeq:XP_022432117.1};
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
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 -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004479}; Single-
CC pass type I membrane protein {ECO:0000256|ARBA:ARBA00004479}.
CC Presynaptic cell membrane {ECO:0000256|ARBA:ARBA00035005}; Single-pass
CC type I membrane protein {ECO:0000256|ARBA:ARBA00035005}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00122}.
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DR RefSeq; XP_022432117.1; XM_022576409.2.
DR AlphaFoldDB; A0A2Y9NL96; -.
DR Proteomes; UP000248483; Unplaced.
DR GO; GO:0042734; C:presynaptic membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0001525; P:angiogenesis; IEA:UniProtKB-KW.
DR CDD; cd00110; LamG; 1.
DR Gene3D; 2.60.120.200; -; 1.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR001791; Laminin_G.
DR InterPro; IPR003585; Neurexin-like.
DR InterPro; IPR027789; Syndecan/Neurexin_dom.
DR PANTHER; PTHR15036:SF57; NEUREXIN-3; 1.
DR PANTHER; PTHR15036; PIKACHURIN-LIKE PROTEIN; 1.
DR Pfam; PF02210; Laminin_G_2; 1.
DR Pfam; PF01034; Syndecan; 1.
DR SMART; SM00294; 4.1m; 1.
DR SMART; SM00282; LamG; 1.
DR SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 1.
DR PROSITE; PS50025; LAM_G_DOMAIN; 1.
PE 4: Predicted;
KW Glycoprotein {ECO:0000256|ARBA:ARBA00022974};
KW Heparan sulfate {ECO:0000256|ARBA:ARBA00023207};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Proteoglycan {ECO:0000256|ARBA:ARBA00022974};
KW Reference proteome {ECO:0000313|Proteomes:UP000248483};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}; Signal {ECO:0000256|SAM:SignalP};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT SIGNAL 1..35
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 36..429
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5015948218"
FT TRANSMEM 356..376
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 85..255
FT /note="Laminin G"
FT /evidence="ECO:0000259|PROSITE:PS50025"
FT REGION 44..65
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 289..313
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 398..429
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 289..312
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 411..429
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 429 AA; 46922 MW; 1A3071F6493BFFD7 CRC64;
MHLRIHARRS PPRRPAWTLG IWSLFWGCII SSVWSSSNVP FSSSSSSSPG SHSQHEHHFH
GSKHHSVPIS IYRSPVSLRG GHAGATYIFG KSGGLILYTW PANDRPSTRS DRLAVGFSTT
VKDGILVRID SAPGLGDFLQ LHIEQGKIGV VFNIGTVDIS IKEDRTPVND GKYHVVRFTR
NGGNATLQVD NWPVNEHYPT GRQLTIFNTQ AQIAIGGKDK GRLFQGQLSG LYYDGLKVLN
MAAENNPNIK INGSVRLVGE VPSILGTTQT TSMPPEMSTT VMETTTTMAT TTTRKNRSTA
SIQPTSDDLV SSAECSSDDE DFVECEPSTA NPTEPGVRRV PGASEVIRES SSTTGMVVGI
VAAAALCILI LLYAMYKYRN RDEGSYQVDE TRNYISNSAQ SNGTLLKEKQ QSSKSGHKKQ
KNKDKEYYV
//
