ID A0A1S3RL94_SALSA Unreviewed; 1063 AA.
AC A0A1S3RL94;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE SubName: Full=Neural cell adhesion molecule 1-like isoform X8 {ECO:0000313|RefSeq:XP_014053018.1};
GN Name=LOC106603640 {ECO:0000313|RefSeq:XP_014053018.1};
OS Salmo salar (Atlantic salmon).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Protacanthopterygii; Salmoniformes;
OC Salmonidae; Salmoninae; Salmo.
OX NCBI_TaxID=8030 {ECO:0000313|Proteomes:UP000087266, ECO:0000313|RefSeq:XP_014053018.1};
RN [1] {ECO:0000313|RefSeq:XP_014053018.1}
RP IDENTIFICATION.
RC TISSUE=Muscle {ECO:0000313|RefSeq:XP_014053018.1};
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- FUNCTION: This protein is a cell adhesion molecule involved in neuron-
CC neuron adhesion, neurite fasciculation, outgrowth of neurites, etc.
CC {ECO:0000256|ARBA:ARBA00003000}.
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DR RefSeq; XP_014053018.1; XM_014197543.1.
DR AlphaFoldDB; A0A1S3RL94; -.
DR GeneID; 106603640; -.
DR OrthoDB; 5233206at2759; -.
DR Proteomes; UP000087266; Chromosome ssa04.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0007155; P:cell adhesion; IEA:InterPro.
DR CDD; cd00063; FN3; 2.
DR CDD; cd00096; Ig; 2.
DR Gene3D; 2.60.40.10; Immunoglobulins; 7.
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; IPR009138; Neural_cell_adh.
DR PANTHER; PTHR12231; CTX-RELATED TYPE I TRANSMEMBRANE PROTEIN; 1.
DR PANTHER; PTHR12231:SF239; NEURAL CELL ADHESION MOLECULE 1; 1.
DR Pfam; PF00041; fn3; 2.
DR Pfam; PF07679; I-set; 4.
DR Pfam; PF13927; Ig_3; 1.
DR PRINTS; PR01838; NCAMFAMILY.
DR SMART; SM00060; FN3; 2.
DR SMART; SM00409; IG; 5.
DR SMART; SM00408; IGc2; 5.
DR SUPFAM; SSF49265; Fibronectin type III; 1.
DR SUPFAM; SSF48726; Immunoglobulin; 5.
DR PROSITE; PS50853; FN3; 2.
DR PROSITE; PS50835; IG_LIKE; 5.
PE 4: Predicted;
KW Immunoglobulin domain {ECO:0000256|ARBA:ARBA00023319};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000087266};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}; Signal {ECO:0000256|SAM:SignalP};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..1063
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5010211954"
FT TRANSMEM 740..763
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 20..108
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 113..197
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 209..297
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 302..405
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 410..487
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 503..599
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 627..723
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT REGION 792..837
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 853..991
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1003..1063
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 792..818
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 821..837
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 853..917
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 942..988
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1021..1045
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1048..1063
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1063 AA; 115209 MW; B44E0211D225DF70 CRC64;
MLQTMDQIWA LLFFGYAASL QVEITPMQGE ISVGESKFFL CEVVGDAKDI DWFAPNGEKL
LPNRQDIIVN RNDESSSTLT IYNADVDNAG VYKCVAKNAD KESEGTVNVK IFQKITFKNA
PSPQEFNEGD DADIICDVVS SPPASIIWKH KGSKIQVTKD VRFKIMGNNH LQIRGIKKTD
EGAYTCEARV MARGEIDLKI IKVIVNVLPS IRTRQSEVNA TADINQSVML ACDADGFPEP
TVTWARNNIV LESDDKYSLN DDGSELIIKD VKKVDEGDYT CIARNKAGEK EEEVSLNVFV
QPKITYLDNQ TASELEEQIT LTCEASGDPT PTITWSFGRR FFTEGEQASW TRPETFESLD
GNVMVRSHAR VSSLTLKYVQ FTDAGQYLCT ARNSIGQDQQ TMYLEVRYAP KIQGSVTVYT
WERNAANISC EVLAHPGASV VWFRDGQQLP STNTTNVKIY NTPAVSHLEV TPDSQNDFGS
YNCTATNLIG TESKEFLLIQ ADVPSAPAIE RVEPFSSTAV VEFEEPDASG GVAILKYRAE
WRMKGQDWTG REYDAEDGLS MITIVGLKPE TFYEVKMSAI NGKGEGESST PLNFKTEPVR
YTFTISSVTP TFIPSTSAAL SEYAEGEPSP PKLEGKLQTM GNALKVNWIK QDDGGSPIKH
YLIRYRAKHV SDWKPEIRLP HGSEYVVLSS LDWNTEYEVY VVAENQQGKS QPGTISFRTA
AEPTAIPDTM TSGSGLGTGA IVGILIVVFV LLLVGVDVTC YFLNKCGFLM CIAVNFCGKS
GPGAKNKDIE EGKAAFMKDE SKEPIVEVRT EDRTPNHEGG GPTEPNETTP LTEPEPTADT
TATVVDLLPS IATNSDPVTE SFSTAQNSPA SETTTLTSST AAPTLAPTEA KTAPNSTPAP
IIQSSTPKAS TPAAQPAAQS DVAPLVDLSE TPKAMPLSDS KPATPATASL EPAKATSNLP
SAKANAVSQS QPEPVQSTPA SDSQNKDLQI DCLAKDVFDT LGKSSEAPAD STAAPAPAKD
DGKIMTEDKS KAPEMETEVK KAQTEVKTIP NEAAQTNGNE SKA
//
