ID I3KG21_ORENI Unreviewed; 1468 AA.
AC I3KG21;
DT 11-JUL-2012, integrated into UniProtKB/TrEMBL.
DT 17-JUN-2020, sequence version 2.
DT 24-JAN-2024, entry version 74.
DE SubName: Full=Neurexin-1a {ECO:0000313|Ensembl:ENSONIP00000020066.2};
GN Name=LOC100697588 {ECO:0000313|Ensembl:ENSONIP00000020066.2};
OS Oreochromis niloticus (Nile tilapia) (Tilapia nilotica).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Cichlomorphae; Cichliformes; Cichlidae; African cichlids;
OC Pseudocrenilabrinae; Oreochromini; Oreochromis.
OX NCBI_TaxID=8128 {ECO:0000313|Ensembl:ENSONIP00000020066.2, ECO:0000313|Proteomes:UP000005207};
RN [1] {ECO:0000313|Ensembl:ENSONIP00000020066.2}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (JUL-2023) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004479}; Single-
CC pass type I membrane protein {ECO:0000256|ARBA:ARBA00004479}.
CC -!- SIMILARITY: Belongs to the neurexin family.
CC {ECO:0000256|ARBA:ARBA00010241}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00076}.
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DR RefSeq; XP_013124981.1; XM_013269527.2.
DR STRING; 8128.ENSONIP00000058773; -.
DR Ensembl; ENSONIT00000020083.2; ENSONIP00000020066.2; ENSONIG00000015930.2.
DR GeneID; 100697588; -.
DR KEGG; onl:100697588; -.
DR CTD; 565531; -.
DR eggNOG; KOG3514; Eukaryota.
DR GeneTree; ENSGT00940000154292; -.
DR HOGENOM; CLU_001710_0_1_1; -.
DR OrthoDB; 2999458at2759; -.
DR TreeFam; TF321302; -.
DR Proteomes; UP000005207; Unplaced.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0048856; P:anatomical structure development; IEA:UniProt.
DR CDD; cd00053; EGF; 1.
DR CDD; cd00054; EGF_CA; 1.
DR CDD; cd00110; LamG; 6.
DR Gene3D; 2.60.120.200; -; 6.
DR Gene3D; 2.10.25.10; Laminin; 3.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR000742; EGF-like_dom.
DR InterPro; IPR001791; Laminin_G.
DR InterPro; IPR003585; Neurexin-like.
DR InterPro; IPR027789; Syndecan/Neurexin_dom.
DR PANTHER; PTHR15036:SF82; -; 1.
DR PANTHER; PTHR15036; PIKACHURIN-LIKE PROTEIN; 1.
DR Pfam; PF00008; EGF; 1.
DR Pfam; PF02210; Laminin_G_2; 6.
DR Pfam; PF01034; Syndecan; 1.
DR SMART; SM00294; 4.1m; 1.
DR SMART; SM00181; EGF; 3.
DR SMART; SM00282; LamG; 6.
DR SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 6.
DR PROSITE; PS50026; EGF_3; 3.
DR PROSITE; PS50025; LAM_G_DOMAIN; 6.
PE 3: Inferred from homology;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW EGF-like domain {ECO:0000256|PROSITE-ProRule:PRU00076};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000005207};
KW 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..22
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 23..1468
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5025642179"
FT TRANSMEM 1395..1415
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 32..209
FT /note="Laminin G"
FT /evidence="ECO:0000259|PROSITE:PS50025"
FT DOMAIN 205..243
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 250..440
FT /note="Laminin G"
FT /evidence="ECO:0000259|PROSITE:PS50025"
FT DOMAIN 447..641
FT /note="Laminin G"
FT /evidence="ECO:0000259|PROSITE:PS50025"
FT DOMAIN 645..682
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 687..860
FT /note="Laminin G"
FT /evidence="ECO:0000259|PROSITE:PS50025"
FT DOMAIN 874..1049
FT /note="Laminin G"
FT /evidence="ECO:0000259|PROSITE:PS50025"
FT DOMAIN 1052..1089
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 1093..1294
FT /note="Laminin G"
FT /evidence="ECO:0000259|PROSITE:PS50025"
FT REGION 1299..1385
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1435..1468
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1299..1347
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1452..1468
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1468 AA; 160872 MW; 8113E2F85014CEDD CRC64;
MSVMAVCVWA AAPLLFLGLC LCSVGGQAQG EVLEFGGVSS QWGRFPVWNA CCESVLSFSL
RTHSQEGLLL YLDDEGFCDF LELLLLHGHL RLRFSIFCAE PAELQSGVAV SDGRWHAVRV
KRDWRNTSLE VDGRLEGWAE VKSKRRDMTV FSHTYMGGVS PELHSSPLRL TSPSVREHPA
FRGWITAVSI NGSLVTLDSS EGVTVTAGCG PDHQCQNGGV CNVVNDQAVC DCSDTGYQGN
DCSEAREEYV ATFKGSEYFC YDLSPNPIQS SSDEITLSFK TLQRNGLMLH TGKSADYVNL
ALKNGAVSLV INLGSGAFEA LVEPVNGKFN DNAWHDVKVT RNLRQHSGIG HAMVTISVDG
ILTTTGYTQE DYTMLGSDDF FYVGGSPSTA DLPGSPVSNN FMGCLKEVVY KNNDVRLELS
RLAKQGDPKM KVSGVVSFKC ESVATLDPVT FDTPESYVAL SKWTAKKAGS ISFDFRTTEP
NGLMLFSHGK PRQQQRKDPR TPPTVKVDFF AIEMLDGHLY LLLDMGSGTT KTKAIDRKVN
DGEWYHVDFQ RDGRSGTISV NSVRTAYTAP GDSEILDLDD TLYLGGLPED RAGLIFPTEV
WTALLNYGYV GCIRDLFVDG QSKDIRRLAE AQRAVGVKPS CSREPPKQCL SNPCQHNGIC
REGWNRYVCD CSGTGYLGRS CERDATILSY DGSKFMKVQL PVVMHTEAED VSLRFRSQRA
YGVLMATTSR NSADTLRLEL DGARVRLTVN LDCIRINCTA SKGPETIFAG SSLNDNEWHT
VRVVRRGKSL KLTVDDLQPV EGQMAGDHTQ LEFHNVETGI VTEKRFMPAV PSNFIGHLQG
LTLNGMPYID LCKNGDIDYC ELNAVIGYKS IVADPVTFRS RSSFVTLPTL QAYYSMHLFM
QFKTTSPDGL ILFNRGDGND FIVVELVKGY LHYISDLGNG AHLIKGNSNS PLNDNHWHNV
HISRDTNNLH TVKIDTKVTT QTTMGAKNLD LKGDLYIGGV SKEMYRDLPK LVHSREGFQG
CLATVDLNGR LPDLLADALA TMGQVERGCE GPSTTCQEDS CSNQGVCLQQ WEGFTCDCSM
TSYAGPLCND AGTTYIFGRD GGLVIYTWPP NERPSTRADR LSLGFSTQQK HAILLRVDSA
SGLGDYLQLQ IDKGNIRVVF NVGTDDINIE ESSKFVNDGK YHVIRFTRSG GNATLQLDDL
PVIERYPSGN IDNERLAIAR QRIPYRLGRV VDDWLLDKGR QLTIFNSQTT VRVGGGERGA
AMFQGQLAGL YYNGLRILNM AAEGHPHIKV EGSARLVGDM PSSSITPQSS AAAGGNRSDS
APSISDITTT TATNRKQGGT TKSSDDLLVA SAECPSDDED IDPCDPSSAR PPLPEVKMFP
GPSEVVRESS STTGMVVGIV AAAALCILIL LYAMYKYRNR DEGSYHVDES RNYISNSATQ
PNGSAKDKPL GIAKISKNKK NKDKEYYV
//