ID   A0A3B3RCV2_9TELE        Unreviewed;       798 AA.
AC   A0A3B3RCV2;
DT   05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 1.
DT   27-MAR-2024, entry version 24.
DE   SubName: Full=Neuroligin-2-like {ECO:0000313|Ensembl:ENSPKIP00000016482.1};
OS   Paramormyrops kingsleyae.
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Osteoglossocephala;
OC   Osteoglossomorpha; Osteoglossiformes; Mormyridae; Paramormyrops.
OX   NCBI_TaxID=1676925 {ECO:0000313|Ensembl:ENSPKIP00000016482.1, ECO:0000313|Proteomes:UP000261540};
RN   [1] {ECO:0000313|Ensembl:ENSPKIP00000016482.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2023) to UniProtKB.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004251};
CC       Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004251}.
CC   -!- SIMILARITY: Belongs to the type-B carboxylesterase/lipase family.
CC       {ECO:0000256|ARBA:ARBA00005964}.
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DR   AlphaFoldDB; A0A3B3RCV2; -.
DR   Ensembl; ENSPKIT00000040976.1; ENSPKIP00000016482.1; ENSPKIG00000002770.1.
DR   GeneTree; ENSGT00940000160598; -.
DR   Proteomes; UP000261540; Unplaced.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0042043; F:neurexin family protein binding; IEA:InterPro.
DR   GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR   GO; GO:0007416; P:synapse assembly; IEA:UniProt.
DR   Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1.
DR   InterPro; IPR029058; AB_hydrolase.
DR   InterPro; IPR002018; CarbesteraseB.
DR   InterPro; IPR019819; Carboxylesterase_B_CS.
DR   InterPro; IPR000460; Nlgn.
DR   PANTHER; PTHR43903; NEUROLIGIN; 1.
DR   PANTHER; PTHR43903:SF3; NEUROLIGIN-2; 1.
DR   Pfam; PF00135; COesterase; 1.
DR   PRINTS; PR01090; NEUROLIGIN.
DR   SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
DR   PROSITE; PS00941; CARBOXYLESTERASE_B_2; 1.
PE   3: Inferred from homology;
KW   Cell adhesion {ECO:0000256|ARBA:ARBA00022889};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        655..678
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          20..581
FT                   /note="Carboxylesterase type B"
FT                   /evidence="ECO:0000259|Pfam:PF00135"
FT   REGION          598..649
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        633..648
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   798 AA;  89314 MW;  FD52F5489E94204F CRC64;
     MCGFMGRGGG GGVDALGKYP MVTTNYGKLR GIKKDLNNEI LGPVEQYLGV PYATPPIGDR
     RFQPPEAPGS WQDVRNATQF APVCPQNIHG VLPEIMLPVW FTDNLDIVAG YIQNQSEDCL
     YLNIYVPTED GPLTKKHDES SMNRPRDEDI RDRRKKAVML FIHGGSYMEG TGNMFDASVL
     AAYGNVIVVT MNYRLGVLGF LSTGDQSAKG NYGLLDQIQA LRWLNENIGH FGGDPERITI
     FGSGAGASCV NLLILSHHSE GLFQRAIAQS GSAISSWSVN YQPLKYTKIL ARKVGCSFGE
     TANMVECLRR KNFRELVDQD IQPARYHIAF GPVVDGDVVP DDPEILMQQG EFLNYDILIG
     VNQGEGLKFV DDGGSEGEEG ISAAAFDYTI SNFVDNLYGY PEGKDILRET IKFMYTDWAD
     RDNGEMRRKT LLALFTDHQW VAPAVATAKL HAEFQSPVYF YTFYHHCQTE TRPEWADAAH
     GDEIPYVFGV PMVGATDLFP CNFSKNDIML SAVVMTYWTN FAKTGDPNLP VPQDTKFIHT
     KPNRFEEVIW TKFNSKDKQY LHIGLKPRVR DNYRANKVAF WLELVPHLHS LHDVYVSSTT
     TRLPPGTPRG GGKGSGPRTT RHPIPTFPPD PDPDGSERPR HSPFPDDTRD YSTELSVTVA
     VGASLLFLNI LAFAALYYKR DKRHEMRRRL SPQHGPANDL AHSQEEEIMS MQMKHSEHDP
     HHDLEPLRPH EILRPACPPD YTLTLRRAPD DMPLMPPNTI TMISSTVAAM QPLHAFNTYP
     APVGHNNTLP HPHSTTRV
//