APLP1_HUMAN » Amyloid-like protein 1

APLP1_HUMAN » Amyloid-like protein 1
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Topology in Plasma membrane
Topologyextracellular side
cytoplasmic side
APLP1_HUMAN » Amyloid-like protein 1 » APLP; APLP-1;
Hydrophobic Thickness 30.0 ± 2.0 Å
Tilt Angle 1 ± 0°
ΔGtransfer -28.1 kcal/mol
ΔGfold -10.5 kcal/mol
Links UniProtKB, Pfam, Interpro, iHOP, STRING, HGNC, HMDB
Topology Out
TM Segments 580-603 (579-607)
Pathways none
PDB 3q7g (A/B=285-494), 3q7l (A/B=285-494), 3qmk (A/B=285-494), 3pmr (A/B=285-499), 4rda (A/B=290-495), 4rd9 (A/B=292-494)
OPM none
Complexes

APLP1:APLP1_HUMAN

Interactions

A4, Complex: A4:APLP1

APLP1, Complex: Homodimer of amyloid-like protein 1, PDBID: 3PMR

APLP2, Complex: APLP1:APLP2

APRIO, Complex: APLP1:APRIO.PRIO, PubMed

DQA1, Complex: APLP1:DQA1, PubMed

PCDA4, Complex: APLP1:PCDA4, PubMed

STX5, Complex: APLP1:STX5, PubMed

Domains

AA: 53-154, PDBID: 1MWP, Subunit A, Seq Identity:42%, Amyloid A4 N-terminal heparin-binding

AA: 155-211, PDBID: 1OWT, Subunit A, Seq Identity:62%, Copper-binding of amyloid precursor, CuBD

AA: 285-467, PDBID: 3PMR, Subunit A, Seq Identity:100%, E2 domain of amyloid precursor protein

AA: 596-647, PDBID: 1M7E, Subunit F, Seq Identity:52%, beta-amyloid precursor protein C-terminus

UniProt annotation for APLP1_HUMAN » Amyloid-like protein 1
FUNCTION: May play a role in postsynaptic function. The C-terminal gamma-secretase processed fragment, ALID1, activates transcription activation through APBB1 (Fe65) binding (By similarity). Couples to JIP signal transduction through C-terminal binding. May interact with cellular G-protein signaling pathways. Can regulate neurite outgrowth through binding to components of the extracellular matrix such as heparin and collagen I.

FUNCTION: The gamma-CTF peptide, C30, is a potent enhancer of neuronal apoptosis.

SUBUNIT: Monomer and homodimer. Heparin binding promotes homodimerization. Binds, via its C-terminus, to the PID domain of several cytoplasmic proteins, including APBB and APBA family members, MAPK8IP1 and Dab1 (By similarity). Binding to Dab1 inhibits its serine phosphorylation (By similarity). Interacts with CPEB1. Interacts (via NPXY motif) with DAB2 (via PID domain); the interaction is impaired by tyrosine phosphorylation of the NPXY motif. Interacts (via NPXY motif) with DAB1 (By similarity).

TISSUE SPECIFICITY: Expressed in the cerebral cortex where it is localized to the postsynaptic density (PSD).

DOMAIN: The NPXY sequence motif found in many tyrosine- phosphorylated proteins is required for the specific binding of the PID domain. However, additional amino acids either N- or C- terminal to the NPXY motif are often required for complete interaction. The NPXY site is also involved in clathrin-mediated endocytosis.

MISCELLANEOUS: Binds zinc and copper in the extracellular domain. Zinc-binding increases heparin binding. No Cu(2+) reducing activity with copper-binding.

UniProt features for APLP1_HUMAN » Amyloid-like protein 1
SIGNAL 1 38 Potential.
CHAIN 39 650 Amyloid-like protein 1.
PEPTIDE 621 650 C30 (By similarity).
REGION 158 178 Copper-binding (By similarity).
REGION 204 211 Zinc-binding.
REGION 285 305 O-glycosylated at three sites.
REGION 310 342 Heparin-binding (By similarity).
REGION 410 441 Heparin-binding (By similarity).
REGION 442 459 Collagen-binding (By similarity).
REGION 632 649 Interaction with DAB1 (By similarity).
REGION 636 650 Interaction with DAB2 (By similarity).
MOTIF 604 615 Basolateral sorting signal (By similarity).
MOTIF 640 643 Clathrin-binding (Potential).
MOTIF 640 643 NPXY motif; contains endocytosis signal.
SITE 167 167 Required for Cu(2+) reduction (By similarity).
SITE 620 621 Cleavage; by caspase-3 (By similarity).
Amino Acid Sequence for APLP1_HUMAN » Amyloid-like protein 1
MGPASPAARG LSRRPGQPPL PLLLPLLLLL LRAQPAIGSL AGGSPGAAEA PGSAQVAGLC GRLTLHRDLR TGRWEPDPQR SRRCLRDPQR VLEYCRQMYP ELQIARVEQA TQAIPMERWC GGSRSGSCAH PHHQVVPFRC LPGEFVSEAL LVPEGCRFLH QERMDQCESS TRRHQEAQEA CSSQGLILHG SGMLLPCGSD RFRGVEYVCC PPPGTPDPSG TAVGDPSTRS WPPGSRVEGA EDEEEEESFP QPVDDYFVEP PQAEEEEETV PPPSSHTLAV VGKVTPTPRP TDGVDIYFGM PGEISEHEGF LRAKMDLEER RMRQINEVMR EWAMADNQSK NLPKADRQAL NEHFQSILQT LEEQVSGERQ RLVETHATRV IALINDQRRA ALEGFLAALQ ADPPQAERVL LALRRYLRAE QKEQRHTLRH YQHVAAVDPE KAQQMRFQVH THLQVIEERV NQSLGLLDQN PHLAQELRPQ IQELLHSEHL GPSELEAPAP GGSSEDKGGL QPPDSKDDTP MTLPKGSTEQ DAASPEKEKM NPLEQYERKV NASVPRGFPF HSSEIQRDEL APAGTGVSRE AVSGLLIMGA GGGSLIVLSM LLLRRKKPYG AISHGVVEVD PMLTLEEQQL RELQRHGYEN PTYRFLEERP