ZFY27_PONAB
ID ZFY27_PONAB Reviewed; 411 AA.
AC Q5R7K2;
DT 11-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 76.
DE RecName: Full=Protrudin;
DE AltName: Full=Zinc finger FYVE domain-containing protein 27;
GN Name=ZFYVE27;
OS Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain cortex;
RG The German cDNA consortium;
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
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. Acts as an adapter protein that facilitates
CC the interaction of KIF5A with VAPA, VAPB, SURF4, RAB11A, RAB11B and
CC RTN3 and the ZFYVE27-KIF5A complex contributes to the transport of
CC these proteins in neurons. Can induce formation of neurite-like
CC membrane protrusions in non-neuronal cells in a KIF5A/B-dependent
CC manner. {ECO:0000250|UniProtKB:Q3TXX3, ECO:0000250|UniProtKB:Q5T4F4}.
CC -!- SUBUNIT: Can form homooligomers (monomers, dimers and tetramers).
CC Interacts with RAB11A (GDP-bound form); regulates RAB11A. Interacts
CC with FKBP8; may negatively regulate ZFYVE27 phosphorylation. Interacts
CC with VAPA (via MSP domain); may regulate ZFYVE27 retention in the
CC endoplasmic reticulum and its function in cell projections formation.
CC Interacts with VAPB (via MSP domain). Interacts with RAB11B (GDP-bound
CC form), REEP1, REEP5, ATL1, ATL2, ATL3, SPAST, SURF4, KIF5A, KIF5B,
CC KIF5C and RTN3. {ECO:0000250|UniProtKB:Q3TXX3,
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 at both dendrites and axons. Localizes to
CC endoplasmic reticulum tubular network. {ECO:0000250|UniProtKB:Q3TXX3,
CC ECO:0000250|UniProtKB:Q5T4F4}.
CC -!- PTM: Phosphorylated. Phosphorylation is induced by NGF through the
CC MAPK/ERK pathway and modulates interaction with RAB11A (By similarity).
CC {ECO:0000250}.
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DR EMBL; CR860113; CAH92258.1; -; mRNA.
DR RefSeq; NP_001126322.1; NM_001132850.1.
DR AlphaFoldDB; Q5R7K2; -.
DR BMRB; Q5R7K2; -.
DR SMR; Q5R7K2; -.
DR STRING; 9601.ENSPPYP00000002949; -.
DR GeneID; 100173301; -.
DR KEGG; pon:100173301; -.
DR CTD; 118813; -.
DR eggNOG; ENOG502QVKC; Eukaryota.
DR InParanoid; Q5R7K2; -.
DR Proteomes; UP000001595; 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; Phosphoprotein; Reference proteome; Transmembrane;
KW Transmembrane helix; Zinc; Zinc-finger.
FT CHAIN 1..411
FT /note="Protrudin"
FT /id="PRO_0000245603"
FT TOPO_DOM 1..66
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q5T4F4"
FT TRANSMEM 67..87
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 88
FT /note="Lumenal"
FT /evidence="ECO:0000250|UniProtKB:Q5T4F4"
FT TRANSMEM 89..109
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 110..187
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q5T4F4"
FT INTRAMEM 188..208
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 209..411
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q5T4F4"
FT ZN_FING 344..410
FT /note="FYVE-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT REGION 1..205
FT /note="Sufficient for localization to endoplasmic reticulum
FT tubular network and for interactions with REEP1, REEP5,
FT ATL1, ATL2, ATL3 and SPAST"
FT /evidence="ECO:0000250|UniProtKB:Q5T4F4"
FT REGION 1..92
FT /note="Sufficient for homooligomerization"
FT /evidence="ECO:0000250|UniProtKB:Q5T4F4"
FT REGION 1..27
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 51..64
FT /note="Necessary for interaction with RAB11A and function
FT in neurite outgrowth"
FT /evidence="ECO:0000250"
FT REGION 234..286
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 271..361
FT /note="Necessary for interaction with KIF5A"
FT /evidence="ECO:0000250|UniProtKB:Q5T4F4"
FT REGION 286..292
FT /note="Necessary for interaction with VAPA"
FT /evidence="ECO:0000250"
FT BINDING 350
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 353
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 366
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="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 374
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 377
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 402
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 405
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
SQ SEQUENCE 411 AA; 45856 MW; C7ED09636FD9F163 CRC64;
MQTSEREGSG PELSPSVMPE APLESPPFPT KSPAFDLFNL VLSYKRLEIY LEPLKDAGDG
VRYLLRWQMP LCSLLTCLGL NVLFLTLNEG AWYSVGALMI SVPALLGYLQ EVCRARLPES
ELMRRKYHSV RQEDLQRVRL SRPEAVAEVK SFLIQLEAFL SRLCCTCEAA YRVLHWENPV
VSSQFYGALL GTICMLYLLP LCWVLTLLNS TLFLGNVEFF RVVSEYRASL QQRMNPKQEE
HAFESPPPPD VGGKGGLMDS TPALTPTEDL TPGSVEEAEE AEPDEEFKDA IEETHLVVLE
DDEGAPCPAE DELALQDNGF LSKNEVLRSK VSRLTERLRK RYPTNNFGNC TGCSATFSVL
KKRRSCSNCG NSFCSRCCSF KVPKSSMGAT APEAQRETVF VCASCNQTLS K
