ID A0A341CFE3_NEOAA Unreviewed; 697 AA.
AC A0A341CFE3;
DT 10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT 10-OCT-2018, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE SubName: Full=Amyloid-like protein 2 isoform X2 {ECO:0000313|RefSeq:XP_024612617.1};
GN Name=APLP2 {ECO:0000313|RefSeq:XP_024612617.1};
OS Neophocaena asiaeorientalis asiaeorientalis (Yangtze finless porpoise)
OS (Neophocaena phocaenoides subsp. asiaeorientalis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Whippomorpha; Cetacea; Odontoceti;
OC Phocoenidae; Neophocaena.
OX NCBI_TaxID=1706337 {ECO:0000313|Proteomes:UP000252040, ECO:0000313|RefSeq:XP_024612617.1};
RN [1] {ECO:0000313|RefSeq:XP_024612617.1}
RP IDENTIFICATION.
RC TISSUE=Meat {ECO:0000313|RefSeq:XP_024612617.1};
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}.
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DR RefSeq; XP_024612617.1; XM_024756849.1.
DR AlphaFoldDB; A0A341CFE3; -.
DR Proteomes; UP000252040; 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:0004867; F:serine-type endopeptidase inhibitor activity; IEA:InterPro.
DR GO; GO:0046914; F:transition metal ion binding; IEA:InterPro.
DR CDD; cd21709; JMTM_APLP2; 1.
DR CDD; cd22607; Kunitz_ABPP-like; 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; 4.10.410.10; Pancreatic trypsin inhibitor Kunitz 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; IPR002223; Kunitz_BPTI.
DR InterPro; IPR036880; Kunitz_BPTI_sf.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR020901; Prtase_inh_Kunz-CS.
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 Pfam; PF00014; Kunitz_BPTI; 1.
DR PRINTS; PR00203; AMYLOIDA4.
DR PRINTS; PR00759; BASICPTASE.
DR SMART; SM00006; A4_EXTRA; 1.
DR SMART; SM00131; KU; 1.
DR SUPFAM; SSF56491; A heparin-binding domain; 1.
DR SUPFAM; SSF89811; Amyloid beta a4 protein copper binding domain (domain 2); 1.
DR SUPFAM; SSF57362; BPTI-like; 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.
DR PROSITE; PS00280; BPTI_KUNITZ_1; 1.
DR PROSITE; PS50279; BPTI_KUNITZ_2; 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 Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000252040};
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 628..650
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 1..152
FT /note="E1"
FT /evidence="ECO:0000259|PROSITE:PS51869"
FT DOMAIN 256..306
FT /note="BPTI/Kunitz inhibitor"
FT /evidence="ECO:0000259|PROSITE:PS50279"
FT DOMAIN 319..510
FT /note="E2"
FT /evidence="ECO:0000259|PROSITE:PS51870"
FT REGION 1..86
FT /note="GFLD subdomain"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01217"
FT REGION 94..152
FT /note="CuBD subdomain"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01217"
FT REGION 158..191
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 162..188
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 63..70
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01217"
FT DISULFID 96..150
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01217"
FT DISULFID 107..137
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01217"
FT DISULFID 121..149
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01217"
SQ SEQUENCE 697 AA; 79961 MW; D467463E8283BBBE CRC64;
MFCGKLNMHV NIQTGEWEPD PTGTRSCFGT KEEVLQYCQE MYPELQITNV MEANQAVSVD
NWCRRDKKQC KTHIVIPFKC LVGEFVSDVL LVPEKCQFFH KERMEVCENH QHWHTVVKEA
CLTQGMTLYS YGMLLPCGVD QFHGTEYVCC PQTKVVESAV SKEEEEDDEE DDEEDDEEDD
EEEDYDIYKS EFPTEADLED FTEAAVDEGE EEVVEDRNYY YDAFKGDGRH EESPTQPSRH
GTAAEKEISH GVRAVCSQEA LTGPCRAVMP RWYFDLSKGK CVRFIYGGCG GNRNNFESEE
YCMAVCKVMI PPTPLPTNDV DVYFETSADD NEHARFQKAK EQLEIRHRHR MDRVKKEWEE
AELQAKNLPK AERQTLIQHF QAMVKALEKE AASEKQQLVE THLARVEAML NDRRRVALEN
YLAALQSDPP RPHRILQALR RYVRAENKDR LHTIRHYQHV LAVDPEKAAQ MKSQVMTHLH
VIEERRNQSL SLLYKVPYVA QEIQEEIDEL LQEQRADMDQ FTASISETPV DVRVSSEESD
EVLPFHPLHP FPSLPENEGS ALGEQEGGLI GAEEKVINSK KKVDENMVID ETLDVKEMIL
NAERVGGLEE GPESVGPLRE DFSLSSSALI GLLVIAVAIA TVIVISLVML RKRQYGTISH
GIVEVDPMLT PEERHLNKMQ NHGYENPTYK YLEQMQI
//
