ID A0A3Q1AXW2_AMPOC Unreviewed; 1458 AA.
AC A0A3Q1AXW2;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE SubName: Full=Neurexin 1 {ECO:0000313|Ensembl:ENSAOCP00000005669.1};
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:ENSAOCP00000005669.1, ECO:0000313|Proteomes:UP000257160};
RN [1] {ECO:0000313|Ensembl:ENSAOCP00000005669.1}
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; ENSAOCT00000005915.1; ENSAOCP00000005669.1; ENSAOCG00000000563.1.
DR GeneTree; ENSGT00940000154292; -.
DR OMA; SCHVQSN; -.
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:SF49; AXOTACTIN; 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 Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 1384..1404
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 26..207
FT /note="Laminin G"
FT /evidence="ECO:0000259|PROSITE:PS50025"
FT DOMAIN 197..235
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 252..434
FT /note="Laminin G"
FT /evidence="ECO:0000259|PROSITE:PS50025"
FT DOMAIN 441..634
FT /note="Laminin G"
FT /evidence="ECO:0000259|PROSITE:PS50025"
FT DOMAIN 638..675
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 680..844
FT /note="Laminin G"
FT /evidence="ECO:0000259|PROSITE:PS50025"
FT DOMAIN 858..1033
FT /note="Laminin G"
FT /evidence="ECO:0000259|PROSITE:PS50025"
FT DOMAIN 1036..1073
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 1077..1279
FT /note="Laminin G"
FT /evidence="ECO:0000259|PROSITE:PS50025"
FT REGION 1283..1374
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1425..1458
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1283..1336
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1359..1374
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1425..1441
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1442..1458
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1458 AA; 160912 MW; 91F4DB27F1AFD64E CRC64;
VKNGLDLIKQ CVLLCLYLVQ YKIGTCLEFT GAEGQWARFP VWNACCESEM SFNLKTKSSH
GLLVYFDDEG FCDFLELLIL NGKLSLRFSI FCADPATVLS DTAVNDSQWH TVTIRRNFKN
TTLMVDNEIK WVEVKSKRRD MTVFSHLFVG GIPPELRSVA LRLTSAAVKD QPPFTGWITD
IKVNNTESVM INSEGVLKDL CGTANMCLNG GVCSLINNEP TCDCSQTGFQ GKDCSEGLAH
LMMGDQGKEE YVATFKGSEF FCYDLSLNPI QSSSDEITLS FKTLQRNGLM LHTGKSADYV
NLALKNGAVS LVINLGSGAF EALVEPVNGK FNDNDWHDVK VTRNLRQVTI SVDGILTTTG
YTQEDYTMLG SDDFFYVGGS PSTADLPGSP VSNNFMGCLK EVVYKNNDVR LELSRLAKQG
DPKMKIHGTV AFKCENVATL DPITFETPES FIILNKWNAK KTGSISFDFR TTEPNGLLLF
SHGKPKQQPK DSKSPQTLKV DFFAIEMLDG HLYLLLDMGS GTTKTKAVNK KVNDGEWYHV
DFQRDGRSGT ISINTLRTAY TAPGESEILD LDDNLYLGGL PENKMGLVFP TEVWTALLNY
GYVGCIRDLF IDGQSKDVRR LAEVQKAAGV KPSCSKEPPK QCLSNPCQNN GICREGWNRY
VCDCSGTGYL GRSCEREATV LSYDGSKFMK VQLPLVMHTE AEDVSLRFRS QRAYGILIAT
TSRDSADTLR LELESGRVRL TVNLGKGPET IFAGQNLNDN EWHTVRVFRR GKSLKLTVDD
LLPVEGQMAG DHTQLEFHNI ETGIVTEKRF MSMVPSNFIG HLQSLSFNGM AYIDLCKNGD
IDYCELNAMI GFKNIIADPV TFKSRSSYVT LTTLQAYYSM HLFFQFKTTS SDGLILYNSG
DGNDFIVVEL VKGYLHYVSD LGNGAHLIKG NSNKPLNDNH WHNVIISRDT NNLHTVKIDT
KITTQTTTGA KNLDLKGNLY IGGVAKEMYK ELPKLVHAKE GFQGCLASVD LNGRLPDLMS
DALDCVGQIE RGCEGPSTTC QEDSCANQGV CLQQWEGFSC DCSMTTFGGP LCNDAGTTYI
FGRDGGLITY TWPPNDRPST RADRLAIGFS THLKDAVLVR VDSSSGLGDF LKLHIEKGNI
AVVFNVGTDD INIEETSKFV NDGKYHIVKF TRSGGNATLQ VDDLPVIERY PTGNIDNERL
AIARQRIPYR LGRVVDEWLL DKGRQLTIFN SQTTIQIGGW ERDRSRSFQG QLSGLYYNGL
KVFNMAAEGD PNIKIQGSVR LVGESPSSIT PQSSTTANRS ETSTSIMEIT TTTASSRRVK
QTTPREPQQT TDDLLVASAE CPSDDEDIDP CEPSSGGLAN PTGAGTGYPG TSEVFRESSS
TTGMVVGIVA AAALCILILL YAMYKYRNRD EGSYHVDESR NYISNSAQSN GTVVKEKPVN
TAKTSGKNKK NKDKEYYV
//
