ID   A4_DORPE                Reviewed;         612 AA.
AC   Q06BR2;
DT   16-OCT-2019, integrated into UniProtKB/Swiss-Prot.
DT   28-NOV-2006, sequence version 2.
DT   25-MAY-2022, entry version 51.
DE   RecName: Full=Amyloid-beta precursor-like protein {ECO:0000305};
DE   Flags: Precursor;
OS   Doryteuthis pealeii (Longfin inshore squid) (Loligo pealeii).
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Cephalopoda;
OC   Coleoidea; Decapodiformes; Teuthida; Myopsina; Loliginidae; Doryteuthis.
OX   NCBI_TaxID=1051067 {ECO:0000312|EMBL:ABI84193.2};
RN   [1] {ECO:0000312|EMBL:ABI84193.2}
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, AND TISSUE
RP   SPECIFICITY.
RC   TISSUE=Cervicothoracic ganglion {ECO:0000312|EMBL:ABI84193.2};
RX   PubMed=17062754; DOI=10.1073/pnas.0607527103;
RA   Satpute-Krishnan P., DeGiorgis J.A., Conley M.P., Jang M., Bearer E.L.;
RT   "A peptide zipcode sufficient for anterograde transport within amyloid
RT   precursor protein.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:16532-16537(2006).
RN   [2] {ECO:0000305}
RP   INTERACTION WITH KINESIN HEAVY CHAIN.
RX   PubMed=23011729; DOI=10.1088/1478-3975/9/5/055005;
RA   Seamster P.E., Loewenberg M., Pascal J., Chauviere A., Gonzales A.,
RA   Cristini V., Bearer E.L.;
RT   "Quantitative measurements and modeling of cargo-motor interactions during
RT   fast transport in the living axon.";
RL   Phys. Biol. 9:055005-055005(2012).
CC   -!- FUNCTION: Acts as a kinesin I membrane receptor, thereby playing a role
CC       in axonal anterograde transport of cargo towards synapes in axons.
CC       {ECO:0000269|PubMed:17062754}.
CC   -!- SUBUNIT: Interacts (via cytoplasmic domain) with kinesin heavy chain.
CC       {ECO:0000269|PubMed:23011729}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Single-pass type I
CC       membrane protein {ECO:0000255}. Cell projection, axon
CC       {ECO:0000269|PubMed:17062754}.
CC   -!- TISSUE SPECIFICITY: Expressed in the cervicothoracic ganglion (stellate
CC       ganglion) (at protein level). {ECO:0000269|PubMed:17062754}.
CC   -!- SIMILARITY: Belongs to the APP family. {ECO:0000255|PROSITE-
CC       ProRule:PRU01217, ECO:0000255|PROSITE-ProRule:PRU01218}.
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DR   EMBL; DQ913735; ABI84193.2; -; mRNA.
DR   AlphaFoldDB; Q06BR2; -.
DR   SMR; Q06BR2; -.
DR   GO; GO:0030424; C:axon; IEA:UniProtKB-SubCell.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0008201; F:heparin binding; IEA:InterPro.
DR   GO; GO:0046914; F:transition metal ion binding; IEA:InterPro.
DR   Gene3D; 1.20.120.770; -; 1.
DR   Gene3D; 2.30.29.30; -; 1.
DR   Gene3D; 3.30.1490.140; -; 1.
DR   Gene3D; 3.90.570.10; -; 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; PTHR23103; 2.
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; SSF109843; SSF109843; 1.
DR   SUPFAM; SSF56491; SSF56491; 1.
DR   SUPFAM; SSF89811; SSF89811; 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   1: Evidence at protein level;
KW   Cell membrane; Cell projection; Disulfide bond; Glycoprotein; Membrane;
KW   Signal; Transmembrane; Transmembrane helix.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000255"
FT   CHAIN           22..612
FT                   /note="Amyloid-beta precursor-like protein"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_5004165090"
FT   TOPO_DOM        22..542
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        543..563
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        564..612
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   DOMAIN          28..189
FT                   /note="E1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01217"
FT   DOMAIN          223..419
FT                   /note="E2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01218"
FT   REGION          28..122
FT                   /note="GFLD subdomain"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01217"
FT   REGION          130..189
FT                   /note="CuBD subdomain"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01217"
FT   REGION          251..276
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          437..490
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          598..612
FT                   /note="Required for the interaction with kinesin heavy
FT                   chain and for anterograde transport in axons"
FT                   /evidence="ECO:0000269|PubMed:17062754,
FT                   ECO:0000269|PubMed:23011729"
FT   MOTIF           599..604
FT                   /note="YENPXY motif"
FT                   /evidence="ECO:0000250|UniProtKB:P05067"
FT   COMPBIAS        443..457
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        473..490
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        99
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        108
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        150
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   DISULFID        38..60
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01217"
FT   DISULFID        71..116
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01217"
FT   DISULFID        96..103
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01217"
FT   DISULFID        132..187
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01217"
FT   DISULFID        143..173
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01217"
FT   DISULFID        157..186
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01217"
SQ   SEQUENCE   612 AA;  70322 MW;  1DE021080B851454 CRC64;
     MGPSVRPGFL VVVIGLQFVA ASMEVNSRKF EPMVAFICNK PAMHRVPSGW VPDDDPAKSC
     VKQPEEILEY CKKLYPDHDI TNVLQASYKV TIPNWCGFNV THCHKHGNHT VRPFRCLVGP
     FQSEALLVPE HCIFDHYHDP RVCNEFDQCN ETAMSKCSAR GMTTQSFAML WPCQEPGHFS
     GVEFVCCPKV SLIPESTEAP KSSPPTPAKT ENGLDDYTAY LKGDSKYMSK YANEHERFKA
     AEKVMQQFQR ERDTKMMKDW KAARDSVREK KKTDPKKAME LNKELTERYQ KIYHAYEQES
     IAEKKQLVNT HQQHIQSWLN NRKQVLMEKL QDALLAKPPK KSKIEKAATA YIKVEEKDKM
     HTYNHFQHLR DTDPEDAANI QDRVLEHLNL IDDRIRRVLD WLKRDPEIEK QVRPNIDKFM
     AKYKDINANS MKLLLRQEPT PKEAPVETQK AEDYSEEDEA AVTGTANKVK PTEARPEQQE
     DIKTPGFDSE TFEDERPAIA EQTIHDLPNH RKKGYIAHVQ QQPMIADEVS LDNLYANSHA
     NSVLGIAIGG VVVFIIIVVA VVMLKRRTQR QRVTHGFVEV DPAASPEERH VANMQMSGYE
     NPTYKYFEMQ NQ