ID A0A3B3B4H5_ORYME Unreviewed; 1175 AA.
AC A0A3B3B4H5;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE SubName: Full=Neurofascin homolog (chicken) a {ECO:0000313|Ensembl:ENSOMEP00000000496.1};
OS Oryzias melastigma (Marine medaka).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Beloniformes; Adrianichthyidae; Oryziinae;
OC Oryzias.
OX NCBI_TaxID=30732 {ECO:0000313|Ensembl:ENSOMEP00000000496.1, ECO:0000313|Proteomes:UP000261560};
RN [1] {ECO:0000313|Ensembl:ENSOMEP00000000496.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-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 immunoglobulin superfamily.
CC L1/neurofascin/NgCAM family. {ECO:0000256|ARBA:ARBA00008588}.
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DR AlphaFoldDB; A0A3B3B4H5; -.
DR Ensembl; ENSOMET00000015757.1; ENSOMEP00000000496.1; ENSOMEG00000001388.1.
DR GeneTree; ENSGT00940000157024; -.
DR Proteomes; UP000261560; Unplaced.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR CDD; cd00063; FN3; 4.
DR Gene3D; 2.60.40.10; Immunoglobulins; 10.
DR InterPro; IPR003961; FN3_dom.
DR InterPro; IPR036116; FN3_sf.
DR InterPro; IPR007110; Ig-like_dom.
DR InterPro; IPR036179; Ig-like_dom_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR013098; Ig_I-set.
DR InterPro; IPR003599; Ig_sub.
DR InterPro; IPR003598; Ig_sub2.
DR InterPro; IPR013151; Immunoglobulin.
DR InterPro; IPR026966; Neurofascin/L1/NrCAM_C.
DR PANTHER; PTHR44170:SF12; NEUROFASCIN; 1.
DR PANTHER; PTHR44170; PROTEIN SIDEKICK; 1.
DR Pfam; PF13882; Bravo_FIGEY; 1.
DR Pfam; PF00041; fn3; 3.
DR Pfam; PF07679; I-set; 4.
DR Pfam; PF00047; ig; 1.
DR Pfam; PF13927; Ig_3; 1.
DR SMART; SM00060; FN3; 4.
DR SMART; SM00409; IG; 6.
DR SMART; SM00408; IGc2; 6.
DR SUPFAM; SSF49265; Fibronectin type III; 2.
DR SUPFAM; SSF48726; Immunoglobulin; 6.
DR PROSITE; PS50853; FN3; 4.
DR PROSITE; PS50835; IG_LIKE; 6.
PE 3: Inferred from homology;
KW Cell adhesion {ECO:0000256|ARBA:ARBA00022889};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Immunoglobulin domain {ECO:0000256|ARBA:ARBA00023319};
KW Membrane {ECO:0000256|SAM:Phobius}; Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Signal {ECO:0000256|SAM:SignalP}; Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT SIGNAL 1..24
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 25..1175
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5017336169"
FT TRANSMEM 1046..1067
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 41..134
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 143..224
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 244..332
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 337..426
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 432..519
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 523..610
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 632..727
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 732..825
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 830..934
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 938..1034
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT REGION 711..738
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1078..1175
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1078..1105
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1106..1120
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1146..1160
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1161..1175
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1175 AA; 131719 MW; 24637859D5E18F4B CRC64;
MLGRGVYVAL TLVLFLLLWQ EAGLIEVPLD SKIQQNMKQP PTIIKQSVKD YIVDPRDNII
IECEAKGNPI PTFSWKRNGK FFNIGSNPTV TMRKRSGTLE IGIRLGERPE DYEGEYQCFA
RNDHGMAMSN KILLRVSKAP LWPKEVLEPL LVTEGSSLVL PCNPPPGLPP PQIFWIDSNM
NPIPQNERVS MGQNGDLYFS NVLVQDAERD YSCNARFNFT QTIQQKNPFT LRVQTSRKVA
ESRPTFLTPS GIQSSKMVLR DKELLLECIA AGLPTPSITW FKKGAELPAR KVKFEKNNKV
LRMLSVSEED AGDYVCTANN NVGMIRHTIS VEVKAAPYWL DKPTNLILAP DEHGRLVCRA
NGKPKPTIQW FVDGEPLEAK ISEGDQRRAL LGDTIIFRSV EIGTSAVYQC NASNQHGYLL
ANAFVSVLDM RPMMLGPKNQ HIQVIENNHT FLDCPYFGSP IPDLRWFKNG QGSGLDGGQY
RVYVNGSLEI RRARREDEGT YTCVATNMLG AAENQVHLEV KEPTRIVQAP VHQSAVRGTT
ARFDCKVNSD PTLPVTVTWT KDDKPLDLRW RLKKDKESLT IPNVNEGDAG TYTCMAKSAI
DQDSVSARLT VLEDDSLHPS LSSALPPGRP DPPMDLDLSD PAARSVRLTW IPGNDHKSPI
TGFLVQFEED RWEPGRWQNL TSFSGDLNSV VLQLAPFVNY QFRVIAVNSV GQSDPSRPSP
RYKTSGAAPD AIPRGLRGWG TRKDNMEISW EPLQDLERNG LNLQYHVWWR RKDSGEQWNS
GSTPLSSYVV HNTDTYVPYE IRIQASNEFG PGPESNVVIG YSGEDKPTEA PRQLRVSKVN
STKAHVHWKA VNMSSIRGEF KEYRLYYSRE SSLVPGLVVK EETKNKGFYT TAEEPSGILT
GLVPFSKYKM FMVVANNRFE SPPSNTVEFT TREGVPDAPR FFKINRRTLD TLYLEWDRPL
EPNGILVGYQ LKYQAVNSSG SSRSKILTFQ HNVTEFTLRL PDRSARYKLF LSALTQQGSG
EVYAEESPHF SNEAYIDQVD IATKGWFIGL MCGIALIILI LLIVCFIKRS RGGKYPVRDK
KDLPLDPVDH KDQDGSFDYH SDEDNKPLQG SQTSLDGNVK ESDDSLVDYG DGGDGQFNED
GSFIGQYTVK KDKDETEGNE SSEATSPVNA IYSLA
//
