ZFY27_CHICK
ID ZFY27_CHICK Reviewed; 406 AA.
AC Q5ZL36;
DT 11-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 23-NOV-2004, sequence version 1.
DT 03-AUG-2022, entry version 94.
DE RecName: Full=Protrudin;
DE AltName: Full=Zinc finger FYVE domain-containing protein 27;
GN Name=ZFYVE27; ORFNames=RCJMB04_7p9;
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 [LARGE SCALE MRNA].
RC STRAIN=CB; TISSUE=Bursa of Fabricius;
RX PubMed=15642098; DOI=10.1186/gb-2004-6-1-r6;
RA Caldwell R.B., Kierzek A.M., Arakawa H., Bezzubov Y., Zaim J., Fiedler P.,
RA Kutter S., Blagodatski A., Kostovska D., Koter M., Plachy J., Carninci P.,
RA Hayashizaki Y., Buerstedde J.-M.;
RT "Full-length cDNAs from chicken bursal lymphocytes to facilitate gene
RT function analysis.";
RL Genome Biol. 6:R6.1-R6.9(2005).
CC -!- FUNCTION: Key regulator of RAB11-dependent vesicular trafficking during
CC neurite extension through polarized membrane transport. Promotes axonal
CC elongation and contributes to the establishment of neuronal cell
CC polarity. Involved in nerve growth factor-induced neurite formation in
CC VAPA-dependent manner. Contributes to both the formation and
CC stabilization of the tubular ER network. Involved in ER morphogenesis
CC by regulating the sheet-to-tubule balance and possibly the density of
CC tubule interconnections. {ECO:0000250|UniProtKB:Q3TXX3,
CC ECO:0000250|UniProtKB:Q5T4F4}.
CC -!- SUBUNIT: Can form homooligomers (monomers, dimers and tetramers).
CC {ECO:0000250|UniProtKB:Q5T4F4}.
CC -!- SUBCELLULAR LOCATION: Recycling endosome membrane
CC {ECO:0000250|UniProtKB:Q6P7B7}; Multi-pass membrane protein
CC {ECO:0000255}. Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:Q5T4F4}; Multi-pass membrane protein
CC {ECO:0000255}. Cell projection, growth cone membrane
CC {ECO:0000250|UniProtKB:Q3TXX3}; Multi-pass membrane protein
CC {ECO:0000255}. Note=Localizes to endoplasmic reticulum tubular network.
CC {ECO:0000250|UniProtKB:Q5T4F4}.
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DR EMBL; AJ719898; CAG31557.1; -; mRNA.
DR RefSeq; NP_001034393.1; NM_001039304.1.
DR AlphaFoldDB; Q5ZL36; -.
DR SMR; Q5ZL36; -.
DR STRING; 9031.ENSGALP00000042307; -.
DR PaxDb; Q5ZL36; -.
DR GeneID; 423839; -.
DR KEGG; gga:423839; -.
DR CTD; 118813; -.
DR VEuPathDB; HostDB:geneid_423839; -.
DR eggNOG; ENOG502QVKC; Eukaryota.
DR InParanoid; Q5ZL36; -.
DR PhylomeDB; Q5ZL36; -.
DR PRO; PR:Q5ZL36; -.
DR Proteomes; UP000000539; Unplaced.
DR GO; GO:0030424; C:axon; ISS:UniProtKB.
DR GO; GO:0030425; C:dendrite; ISS:UniProtKB.
DR GO; GO:0005783; C:endoplasmic reticulum; ISS:UniProtKB.
DR GO; GO:0071782; C:endoplasmic reticulum tubular network; ISS:UniProtKB.
DR GO; GO:0032584; C:growth cone membrane; ISS:UniProtKB.
DR GO; GO:0030176; C:integral component of endoplasmic reticulum membrane; ISS:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; ISS:UniProtKB.
DR GO; GO:0055038; C:recycling endosome membrane; ISS:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0043621; F:protein self-association; ISS:UniProtKB.
DR GO; GO:0071787; P:endoplasmic reticulum tubular network formation; ISS:UniProtKB.
DR GO; GO:0031175; P:neuron projection development; ISS:UniProtKB.
DR GO; GO:0048011; P:neurotrophin TRK receptor signaling pathway; ISS:UniProtKB.
DR GO; GO:0045773; P:positive regulation of axon extension; ISS:UniProtKB.
DR GO; GO:0072659; P:protein localization to plasma membrane; ISS:UniProtKB.
DR GO; GO:0016192; P:vesicle-mediated transport; ISS:UniProtKB.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR042405; Protrudin.
DR InterPro; IPR000306; Znf_FYVE.
DR InterPro; IPR017455; Znf_FYVE-rel.
DR InterPro; IPR011011; Znf_FYVE_PHD.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR14543; PTHR14543; 1.
DR Pfam; PF01363; FYVE; 1.
DR SMART; SM00064; FYVE; 1.
DR SUPFAM; SSF57903; SSF57903; 1.
DR PROSITE; PS50178; ZF_FYVE; 1.
PE 2: Evidence at transcript level;
KW Cell membrane; Cell projection; Endoplasmic reticulum; Endosome; Membrane;
KW Metal-binding; Reference proteome; Transmembrane; Transmembrane helix;
KW Zinc; Zinc-finger.
FT CHAIN 1..406
FT /note="Protrudin"
FT /id="PRO_0000245604"
FT TOPO_DOM 1..71
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q5T4F4"
FT TRANSMEM 72..92
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 93
FT /note="Lumenal"
FT /evidence="ECO:0000250|UniProtKB:Q5T4F4"
FT TRANSMEM 94..114
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 115..192
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q5T4F4"
FT INTRAMEM 193..213
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 214..406
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q5T4F4"
FT ZN_FING 339..405
FT /note="FYVE-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT REGION 1..210
FT /note="Sufficient for localization to endoplasmic reticulum
FT tubular network"
FT /evidence="ECO:0000250|UniProtKB:Q5T4F4"
FT REGION 1..97
FT /note="Sufficient for homooligomerization"
FT /evidence="ECO:0000250|UniProtKB:Q5T4F4"
FT REGION 239..295
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 248..262
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 275..295
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 345
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 348
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 361
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 364
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 369
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 372
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 397
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 400
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
SQ SEQUENCE 406 AA; 44926 MW; 55B890A8E9155144 CRC64;
MQAAERDGVA GGLEATAAVA ATGGGEASSE PPSPPKAASF DLLDLVRSYR RLELYLEPLR
DAAEGVRALL RWQRPLCSLL VCLGLNFLLL TLDQAAWYSV LALLVLLPAL LGYLQETYRV
RPSERELLRR KYHSVRREDL RRVQLSRQEA LAQVKCFLIQ LEGFLSGLCY NCEAVYRVLY
WENPTVSSQF YGALLGSVCI LYLLPLCWVM AILNSTLFLG NSQFYQVIKE LKASVEQSLG
TKPLESAPEP AKPLPTDAPP DRTPTPTSTE DLTPGSVEEA EEAEPDEEFK DAIEEDDEGS
QCSADFDLSL PDNGFMSKND VIRSKVSRLT ERLRKRYPSN NFGTCTGCGA TFSVLKKRRS
CSNCGNSFCS RCCSFKVPKA VMGATAPEAQ RETVFVCAQC NQMLIK
