ID A0A3Q1C974_AMPOC Unreviewed; 1496 AA.
AC A0A3Q1C974;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE SubName: Full=Neurexin 1 {ECO:0000313|Ensembl:ENSAOCP00000023235.1};
OS Amphiprion ocellaris (Clown anemonefish).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Pomacentridae; Amphiprion.
OX NCBI_TaxID=80972 {ECO:0000313|Ensembl:ENSAOCP00000023235.1, ECO:0000313|Proteomes:UP000257160};
RN [1] {ECO:0000313|Ensembl:ENSAOCP00000023235.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-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 Ensembl; ENSAOCT00000005989.1; ENSAOCP00000023235.1; ENSAOCG00000000563.1.
DR GeneTree; ENSGT00940000154292; -.
DR Proteomes; UP000257160; Unplaced.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0048856; P:anatomical structure development; IEA:UniProt.
DR CDD; cd00054; EGF_CA; 2.
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:SF51; NEUREXIN-1; 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:UP000257160};
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..27
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 28..1496
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5018648472"
FT TRANSMEM 1422..1442
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 27..208
FT /note="Laminin G"
FT /evidence="ECO:0000259|PROSITE:PS50025"
FT DOMAIN 198..236
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 273..463
FT /note="Laminin G"
FT /evidence="ECO:0000259|PROSITE:PS50025"
FT DOMAIN 470..663
FT /note="Laminin G"
FT /evidence="ECO:0000259|PROSITE:PS50025"
FT DOMAIN 667..704
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 709..882
FT /note="Laminin G"
FT /evidence="ECO:0000259|PROSITE:PS50025"
FT DOMAIN 896..1071
FT /note="Laminin G"
FT /evidence="ECO:0000259|PROSITE:PS50025"
FT DOMAIN 1074..1111
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 1115..1317
FT /note="Laminin G"
FT /evidence="ECO:0000259|PROSITE:PS50025"
FT REGION 1321..1412
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1463..1496
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1321..1374
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1397..1412
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1463..1479
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1480..1496
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1496 AA; 164989 MW; 07FDBA5120DF1862 CRC64;
MVLQKPHGAH IIWVGLLICC FVEIGTCLEF TGAEGQWARF PVWNACCESE MSFNLKTKSS
HGLLVYFDDE GFCDFLELLI LNGKLSLRFS IFCADPATVL SDTAVNDSQW HTVTIRRNFK
NTTLMVDNEI KWVEVKSKRR DMTVFSHLFV GGIPPELRSV ALRLTSAAVK DQPPFTGWIT
DIKVNNTESV MINSEGVLKD LCGTANMCLN GGVCSLINNE PTCDCSQTGF QGKDCSEGLA
HLMMGDQGKS KGQRGEAWLL RSLLSIQGKE EYVATFKGSE FFCYDLSLNP IQSSSDEITL
SFKTLQRNGL MLHTGKSADY VNLALKNGAV SLVINLGSGA FEALVEPVNG KFNDNDWHDV
KVTRNLRQHS GIGHAMVTIS VDGILTTTGY TQEDYTMLGS DDFFYVGGSP STADLPGSPV
SNNFMGCLKE VVYKNNDVRL ELSRLAKQGD PKMKIHGTVA FKCENVATLD PITFETPESF
IILNKWNAKK TGSISFDFRT TEPNGLLLFS HGKPKQQPKD SKSPQTLKVD FFAIEMLDGH
LYLLLDMGSG TTKTKAVNKK VNDGEWYHVD FQRDGRSGTI SINTLRTAYT APGESEILDL
DDNLYLGGLP ENKMGLVFPT EVWTALLNYG YVGCIRDLFI DGQSKDVRRL AEVQKAAGVK
PSCSKEPPKQ CLSNPCQNNG ICREGWNRYV CDCSGTGYLG RSCEREATVL SYDGSKFMKV
QLPLVMHTEA EDVSLRFRSQ RAYGILIATT SRDSADTLRL ELESGRVRLT VNLDCIRINC
TSSKGPETIF AGQNLNDNEW HTVRVFRRGK SLKLTVDDLL PVEGQMAGDH TQLEFHNIET
GIVTEKRFMS MVPSNFIGHL QSLSFNGMAY IDLCKNGDID YCELNAMIGF KNIIADPVTF
KSRSSYVTLT TLQAYYSMHL FFQFKTTSSD GLILYNSGDG NDFIVVELVK GYLHYVSDLG
NGAHLIKGNS NKPLNDNHWH NVIISRDTNN LHTVKIDTKI TTQTTTGAKN LDLKGNLYIG
GVAKEMYKEL PKLVHAKEGF QGCLASVDLN GRLPDLMSDA LDCVGQIERG CEGPSTTCQE
DSCANQGVCL QQWEGFSCDC SMTTFGGPLC NDAGTTYIFG RDGGLITYTW PPNDRPSTRA
DRLAIGFSTH LKDAVLVRVD SSSGLGDFLK LHIEKGNIAV VFNVGTDDIN IEETSKFVND
GKYHIVKFTR SGGNATLQVD DLPVIERYPT GNIDNERLAI ARQRIPYRLG RVVDEWLLDK
GRQLTIFNSQ TTIQIGGWER DRSRSFQGQL SGLYYNGLKV FNMAAEGDPN IKIQGSVRLV
GESPSSITPQ SSTTANRSET STSIMEITTT TASSRRVKQT TPREPQQTTD DLLVASAECP
SDDEDIDPCE PSSGGLANPT GAGTGYPGTS EVFRESSSTT GMVVGIVAAA ALCILILLYA
MYKYRNRDEG SYHVDESRNY ISNSAQSNGT VVKEKPVNTA KTSGKNKKNK DKEYYV
//
