ID A0A1U7SHY4_ALLSI Unreviewed; 651 AA.
AC A0A1U7SHY4;
DT 10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT 10-MAY-2017, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE SubName: Full=Amyloid-like protein 2 isoform X4 {ECO:0000313|RefSeq:XP_006032198.1};
GN Name=APLP2 {ECO:0000313|RefSeq:XP_006032198.1};
OS Alligator sinensis (Chinese alligator).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Crocodylia; Alligatoridae; Alligatorinae;
OC Alligator.
OX NCBI_TaxID=38654 {ECO:0000313|Proteomes:UP000189705, ECO:0000313|RefSeq:XP_006032198.1};
RN [1] {ECO:0000313|RefSeq:XP_006032198.1}
RP IDENTIFICATION.
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}.
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DR RefSeq; XP_006032198.1; XM_006032136.2.
DR AlphaFoldDB; A0A1U7SHY4; -.
DR GeneID; 102371069; -.
DR CTD; 334; -.
DR OrthoDB; 2907766at2759; -.
DR Proteomes; UP000189705; Unplaced.
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; cd21709; JMTM_APLP2; 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:SF14; AMYLOID BETA PRECURSOR LIKE PROTEIN 2; 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 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:UP000189705};
KW Signal {ECO:0000256|ARBA:ARBA00022729};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 582..604
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 1..154
FT /note="E1"
FT /evidence="ECO:0000259|PROSITE:PS51869"
FT DOMAIN 264..455
FT /note="E2"
FT /evidence="ECO:0000259|PROSITE:PS51870"
FT REGION 1..88
FT /note="GFLD subdomain"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01217"
FT REGION 96..154
FT /note="CuBD subdomain"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01217"
FT REGION 162..246
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 163..180
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 189..218
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 219..246
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 38..82
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01217"
FT DISULFID 63..70
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01217"
FT DISULFID 98..152
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01217"
FT DISULFID 109..139
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01217"
FT DISULFID 123..151
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01217"
SQ SEQUENCE 651 AA; 74906 MW; AFD06F8A26B31D73 CRC64;
MFCGKLNMHV NIQTGKWEPD TSGTKSCFGR KEEVLQYCQE IYPELQITNV VEANQPVSID
NWCKKGKKQC KDHTHIVVPY KCLVGEFVSD VLLVPEKCRF FHKERMDVCE SHQHWHTVAK
EACLTEGMIL HSYGMLLPCG VDQFHGTEYV CCPQTKIVDE ALSKEEEEED EDEDEDYDLY
KSEFPTEADV EDFTETAVEE DEEEDEEGEE EEEVVEDRDY YYDSYKVDDY NEETPTEPSS
DKSLSEKEII SDVKVPPTPV PTDDVDVYFE TPADDNEHAR FQKAKEQLEV RHHNRMDRVK
KEWEEAERQA KNLPKAERQT LIQHFQAMVK SLEKEAASEK QQLVETHLAR VEAMLNDRRR
IALENYLAAL QADPPRPHRI LQALKRYVRA ENKDRLHTIR HYQHVLAVDP EKAAQMKSQV
MTHLHVIEER MNQSLSLLYK VPYVAEEIQD EIDELLQEQR ADMDQFTSSI SESLVDVRVS
SEESEEIPLQ EGKPFRPFQV KTFPALPESE GSGIADLDGL IGAEEKVINS KNKVDENVVI
DETLDVKEMI FNAERVGGLV EEPDDDGSLG SFHDDFSFSS SALIGLLVIA VAIATVIVIS
LVMLRKRQYG TISHGIVEVD PMLTPEERHL SKMQNHGYEN PTYKYLEQMQ I
//
