ID A0A3Q1FDF4_9TELE Unreviewed; 1279 AA.
AC A0A3Q1FDF4;
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=Neuronal cell adhesion molecule-like {ECO:0000313|Ensembl:ENSAPOP00000013927.1};
GN Name=NRCAM {ECO:0000313|Ensembl:ENSAPOP00000013927.1};
OS Acanthochromis polyacanthus (spiny chromis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Pomacentridae; Acanthochromis.
OX NCBI_TaxID=80966 {ECO:0000313|Ensembl:ENSAPOP00000013927.1, ECO:0000313|Proteomes:UP000257200};
RN [1] {ECO:0000313|Ensembl:ENSAPOP00000013927.1}
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 immunoglobulin superfamily.
CC L1/neurofascin/NgCAM family. {ECO:0000256|ARBA:ARBA00008588}.
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DR AlphaFoldDB; A0A3Q1FDF4; -.
DR Ensembl; ENSAPOT00000022212.1; ENSAPOP00000013927.1; ENSAPOG00000016917.1.
DR GeneTree; ENSGT00940000155419; -.
DR Proteomes; UP000257200; 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; IPR026966; Neurofascin/L1/NrCAM_C.
DR PANTHER; PTHR44170:SF15; NEURONAL CELL ADHESION MOLECULE; 1.
DR PANTHER; PTHR44170; PROTEIN SIDEKICK; 1.
DR Pfam; PF13882; Bravo_FIGEY; 1.
DR Pfam; PF00041; fn3; 4.
DR Pfam; PF07679; I-set; 4.
DR Pfam; PF13927; Ig_3; 2.
DR PRINTS; PR00014; FNTYPEIII.
DR SMART; SM00060; FN3; 5.
DR SMART; SM00409; IG; 6.
DR SMART; SM00408; IGc2; 6.
DR SUPFAM; SSF49265; Fibronectin type III; 3.
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};
KW Reference proteome {ECO:0000313|Proteomes:UP000257200};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}; Signal {ECO:0000256|SAM:SignalP};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT SIGNAL 1..21
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 22..1279
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5018744942"
FT TRANSMEM 1141..1162
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 32..119
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 130..220
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 253..341
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 346..434
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 440..527
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 531..618
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 635..730
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 732..829
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 834..936
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 940..1036
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT REGION 1198..1279
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1198..1226
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1279 AA; 142638 MW; 0CAB3268DC269849 CRC64;
MERRRMEAVL LVLFLGHLVT ALDVPLDLPQ PPTITQESPK DYIIDPRENI IIHCEAKGKP
HPSFSWTRNG THFDVDNDPN VNMKAHSGTL VVDISREKVE NYEGVYQCTA RNKHGTAVSN
NIVVRQSRSP LWSKEKIKPI VVQEGVSLVL PCRPPAGLPP PIIFWMDNNF QRLPQSRRVS
QSLNGDLYFS NVRREDSRND YICYARFPHT QTIQQKQPIN VRVLNLDAIN DTMADFYNDT
DLFSEAPVDE RRPTFLIPSG TSSTKMVLRG HVLEMECIAE GLPTPEISWT KISGDLPAGR
TFFLHYNKTL RIVDVSESDA ADYRCTAKNQ LGAVHHTIRV SVKAAPYWIS GPPRNLVLAP
GENGTLTCMA SGTPKPSVTW AMNGIPIENS PKDVSRKVED DTIIFTGVQT GSSAVYQCNI
SNDYGYLLSN AFVNVLSEPP RVLTPANKVY QVIKNHQAMI DCASFGSPIP KITWFKGSRS
MSLDGDYYIT HNNGTLEIYV AQAQNSGKYT CVARNSLGIY ENHVHLEVKE PTRILKQPEY
KVVQRGRSVV FECKVKHDPS LIPTMTWLKD DGELPDDERL IVDNDSLTIT EVTENDAGVY
TCIMNTTLDH DSATAELTVV EATPTPAVIH EHPDPPTDLE LTDQKKRSVQ LTWTPGDEHN
SPIQKFLIQY EDSLHHRGHW HNLTEVPGTR TTAHLKLSPY VHYTFRVLAL NAIGPSRPSF
PSRMYRTDPA APDENPTGVE GFGTEHNNLV ISWKPLSGFQ ANGPGLHYKV MWRQKALDSD
WTTVTVANNS KFVVVGTPTF VPYELKVQAV NDHGEGPEPK IAEGYSGEDL PIAAPENVQA
IIVNSTLAKV HWDPVPFHLI RGHLKGYKVY YWRKHSLHKH NPDHMEKDIL TFSGNHTHGM
LPGLHPFSLY SFNVRVFNGK GEGPPSPTQQ FKMPEGVPGP PTSLLVSNPN LDSLTLEWGP
PHDRNGHITG YTLKYQPVNN SNELGPLEEV ALAANETSIT LPNLKYSTRY KFYLSAKTVT
GPGPDITQEV VPVMDEASPF GNVSYAVGDD GALISWEYWG LEKNVYVEYV VKDSEGEEEW
QKELVNGSQN FMLKGLKEGL SYRVRLVTKG HQDQLLHCSE ELLVTVPAVA SRQVDIATQG
WFIGLMCAIA LLILILLIIC FIQRNKGGKY PVKEKEDAHT DPEFQPMKDD DCTFVEYSDN
EDHKPLKGSR TPSNGTVKRD DSDDSLVDYG EGGDGQFNED GSFIGQYSGK SASRDTAEGH
ESSEAPSPIN AMNSLNSFV
//
