ID A0A1S3N8E9_SALSA Unreviewed; 734 AA.
AC A0A1S3N8E9;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE SubName: Full=Amyloid-like protein 1 isoform X2 {ECO:0000313|RefSeq:XP_014011758.1};
GN Name=LOC106577862 {ECO:0000313|RefSeq:XP_014011758.1};
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_014011758.1};
RN [1] {ECO:0000313|RefSeq:XP_014011758.1}
RP IDENTIFICATION.
RC TISSUE=Muscle {ECO:0000313|RefSeq:XP_014011758.1};
RG RefSeq;
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 APP family. {ECO:0000256|PROSITE-
CC ProRule:PRU01217}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU01217}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR RefSeq; XP_014011758.1; XM_014156283.1.
DR AlphaFoldDB; A0A1S3N8E9; -.
DR GeneID; 106577862; -.
DR OrthoDB; 2907766at2759; -.
DR Proteomes; UP000087266; Chromosome ssa02.
DR GO; GO:0012505; C:endomembrane system; IEA:UniProt.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0008201; F:heparin binding; IEA:UniProtKB-UniRule.
DR GO; GO:0046914; F:transition metal ion binding; IEA:InterPro.
DR CDD; cd21708; JMTM_APLP1; 1.
DR Gene3D; 6.10.250.1670; -; 1.
DR Gene3D; 1.20.120.770; Amyloid precursor protein, E2 domain; 1.
DR Gene3D; 3.30.1490.140; Amyloidogenic glycoprotein, copper-binding domain; 1.
DR Gene3D; 3.90.570.10; Amyloidogenic glycoprotein, heparin-binding domain; 1.
DR Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1.
DR InterPro; IPR036669; Amyloid_Cu-bd_sf.
DR InterPro; IPR008155; Amyloid_glyco.
DR InterPro; IPR011178; Amyloid_glyco_Cu-bd.
DR InterPro; IPR024329; Amyloid_glyco_E2_domain.
DR InterPro; IPR008154; Amyloid_glyco_extra.
DR InterPro; IPR015849; Amyloid_glyco_heparin-bd.
DR InterPro; IPR036454; Amyloid_glyco_heparin-bd_sf.
DR InterPro; IPR019745; Amyloid_glyco_intracell_CS.
DR InterPro; IPR019543; APP_amyloid_C.
DR InterPro; IPR019744; APP_CUBD_CS.
DR InterPro; IPR036176; E2_sf.
DR InterPro; IPR011993; PH-like_dom_sf.
DR PANTHER; PTHR23103; ALZHEIMER'S DISEASE BETA-AMYLOID RELATED; 1.
DR PANTHER; PTHR23103:SF13; AMYLOID BETA PRECURSOR LIKE PROTEIN 1; 1.
DR Pfam; PF10515; APP_amyloid; 1.
DR Pfam; PF12924; APP_Cu_bd; 1.
DR Pfam; PF12925; APP_E2; 1.
DR Pfam; PF02177; APP_N; 1.
DR PRINTS; PR00203; AMYLOIDA4.
DR SMART; SM00006; A4_EXTRA; 1.
DR SUPFAM; SSF56491; A heparin-binding domain; 1.
DR SUPFAM; SSF89811; Amyloid beta a4 protein copper binding domain (domain 2); 1.
DR SUPFAM; SSF109843; CAPPD, an extracellular domain of amyloid beta A4 protein; 1.
DR PROSITE; PS00319; APP_CUBD; 1.
DR PROSITE; PS51869; APP_E1; 1.
DR PROSITE; PS51870; APP_E2; 1.
DR PROSITE; PS00320; APP_INTRA; 1.
PE 3: Inferred from homology;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Copper {ECO:0000256|ARBA:ARBA00023008};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW ProRule:PRU01217}; Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000087266};
KW Signal {ECO:0000256|ARBA:ARBA00022729, 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..23
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 24..734
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5010259137"
FT TRANSMEM 666..688
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 35..195
FT /note="E1"
FT /evidence="ECO:0000259|PROSITE:PS51869"
FT DOMAIN 358..549
FT /note="E2"
FT /evidence="ECO:0000259|PROSITE:PS51870"
FT REGION 35..130
FT /note="GFLD subdomain"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01217"
FT REGION 138..195
FT /note="CuBD subdomain"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01217"
FT REGION 198..359
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 565..627
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 373..436
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 219..239
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 242..293
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 315..351
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 606..620
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 80..124
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01217"
FT DISULFID 105..112
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01217"
FT DISULFID 151..181
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01217"
SQ SEQUENCE 734 AA; 83642 MW; 2AA5190331226AA4 CRC64;
MGHSVLPILM VVLSHCMWGN VEALAMAEVN GPGPLVAEPQ IAMFCGRQLL HMNPETGQWE
PDPQGRQGCF TEPNQILSYC QEMYPALQIS HVEESSSPVT IPAWCKKGWG HCQTRPFIVM
PYRCQVGEYV SEALLVPDRC RFLHQEQMDA CESYVYWHNI AKEACTADSL ELHSYGMLLP
CGERFRGVEY VCCPGRGGSS GRGETEGGDV LPAGPQALTP QVKVNTGVKV TTPTPSPSPD
TDVDEADMEE EDDELVEENE QVVDEEEEEA VEDDEEEEEE EEEEEEEEEE QQQQQEVAAA
VKDPEEYEYS IDSGPYQASD YTDSFYYEKG QGQTGRNPST SPPQTRGDSL PTPRPTDGVD
VYFEMPGDDS EHANFLRAKM DLEERRMKRI NEIMKEWAEA DNQSKNLPKS DRQALNEHFQ
SVLQTLEEQV AGERQRLVET HLARVVATLN NNRRLALESY LTAVQAEPPQ PERVLQALKR
YMAAEQKDRR HTLRHYQHIE AVDPQKAEQM KFQVYTHLHV IEERMNQSLA LLYKVPALAE
ELHDDIQELV KAERGDISEL MTTSFSETRT TEELLPAESE EEKDDEEEEE RAFQNRPYPP
RIDPQPNTKK ASTDEYDYAT SERSPTYEYE EKINTSVELK QVVYKSPEIQ TDELQPDALE
TFNRGAMVGL LVVAVAIAMV MVISLLLVRR KPYGTISHGI VEVDPMLTPE ERQLNKMQNH
GYENPTYKFF EQMN
//
