ID   AMPH_CHICK              Reviewed;         682 AA.
AC   P50478;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   03-AUG-2022, entry version 122.
DE   RecName: Full=Amphiphysin;
GN   Name=AMPH;
OS   Gallus gallus (Chicken).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC   Phasianinae; Gallus.
OX   NCBI_TaxID=9031;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=Tetra-hybrid; TISSUE=Forebrain;
RX   PubMed=1628617; DOI=10.1002/j.1460-2075.1992.tb05317.x;
RA   Lichte B., Veh R.W., Meyer H.E., Kilimann M.W.;
RT   "Amphiphysin, a novel protein associated with synaptic vesicles.";
RL   EMBO J. 11:2521-2530(1992).
CC   -!- FUNCTION: May participate in mechanisms of regulated exocytosis in
CC       synapses and certain endocrine cell types. May control the properties
CC       of the membrane associated cytoskeleton.
CC   -!- SUBUNIT: Heterodimer with BIN1. Binds SH3GLB1 (By similarity).
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle, synaptic
CC       vesicle membrane; Peripheral membrane protein; Cytoplasmic side.
CC       Cytoplasm, cytoskeleton.
CC   -!- TISSUE SPECIFICITY: Is abundant in the forebrain and cerebellum. It is
CC       also found in the adrenal gland, anterior and posterior pituitary.
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DR   EMBL; X60422; CAA42953.1; -; mRNA.
DR   PIR; S22700; S22700.
DR   RefSeq; NP_001004398.1; NM_001004398.1.
DR   AlphaFoldDB; P50478; -.
DR   SMR; P50478; -.
DR   ELM; P50478; -.
DR   STRING; 9031.ENSGALP00000018798; -.
DR   PaxDb; P50478; -.
DR   GeneID; 420761; -.
DR   KEGG; gga:420761; -.
DR   CTD; 273; -.
DR   VEuPathDB; HostDB:geneid_420761; -.
DR   eggNOG; KOG3771; Eukaryota.
DR   InParanoid; P50478; -.
DR   OrthoDB; 1366218at2759; -.
DR   PhylomeDB; P50478; -.
DR   PRO; PR:P50478; -.
DR   Proteomes; UP000000539; Unplaced.
DR   GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR   GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR   GO; GO:0044306; C:neuron projection terminus; IDA:AgBase.
DR   GO; GO:0008021; C:synaptic vesicle; IDA:AgBase.
DR   GO; GO:0030672; C:synaptic vesicle membrane; IEA:UniProtKB-SubCell.
DR   CDD; cd12140; SH3_Amphiphysin_I; 1.
DR   Gene3D; 1.20.1270.60; -; 1.
DR   InterPro; IPR027267; AH/BAR_dom_sf.
DR   InterPro; IPR003005; Amphiphysin.
DR   InterPro; IPR003017; Amphiphysin_1.
DR   InterPro; IPR035470; Amphiphysin_I_SH3.
DR   InterPro; IPR004148; BAR_dom.
DR   InterPro; IPR036028; SH3-like_dom_sf.
DR   InterPro; IPR001452; SH3_domain.
DR   PANTHER; PTHR46514:SF2; PTHR46514:SF2; 1.
DR   Pfam; PF03114; BAR; 1.
DR   Pfam; PF14604; SH3_9; 1.
DR   PRINTS; PR01251; AMPHIPHYSIN.
DR   PRINTS; PR01252; AMPHIPHYSIN1.
DR   PRINTS; PR00452; SH3DOMAIN.
DR   SMART; SM00721; BAR; 1.
DR   SMART; SM00326; SH3; 1.
DR   SUPFAM; SSF103657; SSF103657; 1.
DR   SUPFAM; SSF50044; SSF50044; 1.
DR   PROSITE; PS51021; BAR; 1.
DR   PROSITE; PS50002; SH3; 1.
PE   2: Evidence at transcript level;
KW   Coiled coil; Cytoplasm; Cytoplasmic vesicle; Cytoskeleton; Membrane;
KW   Reference proteome; SH3 domain; Synapse.
FT   CHAIN           1..682
FT                   /note="Amphiphysin"
FT                   /id="PRO_0000192950"
FT   DOMAIN          24..240
FT                   /note="BAR"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00361"
FT   DOMAIN          609..682
FT                   /note="SH3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT   REGION          244..310
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          446..470
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          501..530
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          561..606
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          10..84
FT                   /evidence="ECO:0000255"
FT   COILED          144..191
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        287..309
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        507..527
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        563..600
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   682 AA;  75205 MW;  61617F494F38EB20 CRC64;
     MADMKTGIFA KNVQKRLNRA QEKVLQKLGK ADETKDEQFE EYVQNFKRQE AEGSRLQREL
     RAYLAAIKGM QDASKKLTES LHEVYEPDWY GREDVKMIGE KCDELWEDFH QKLVDGSLLT
     LDTYLGQFPD IKTRIAKRSR KLVDYDSARH HLEALQSSKR KDEGRITKAE EEFQKAQKVF
     EEFNTDLQEE LPSLWSRRVG FYVNTFKNVS SLEAKFHKEI ALLCHKLYEV MTKLGDQHAD
     KAFTIQGAPS DSGPLRIAKT PSPPEEVSPL PSPTASPNHM LAPASPAPAR PKSPTQLRKG
     PPVPPLPKLT PTKELQQENI INLFDDNFVP EINVTTPSQN EIPETKKVES LLDLDFDPFK
     PEVVSTGVTH SPMSQTLPWD LWTTTSELVQ PASSTAFNGF AQDTTAFAVQ SNENVTETLT
     EAEEAPLGEL KVEETPTAAV VEKEAILAEP DEPTEQAAES IEAGDKETTG IAEKESEVVS
     AAGGAVAVED SVVVAAGAGE GAVRTEQEAA AEGDKPQGEE KDVDVSQEKV SSIPSVVIEP
     ASNNEGEGEE HHVIMNESKD AAAEMGTQGT DSETSQIGSE QKATEEIQTT PSQDQPASAG
     DTASDMPPGF LFKVEVLHDF EAANSDELNL KRGDIVLVIP SETTADQEAG WLTGIKESEW
     LQYRDANSYK GLFPENFTRH LE