ID ZFY27_BOVIN Reviewed; 404 AA.
AC Q5BIM5; A4IFC7;
DT 11-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 12-APR-2005, sequence version 1.
DT 27-MAR-2024, entry version 108.
DE RecName: Full=Protrudin;
DE AltName: Full=Zinc finger FYVE domain-containing protein 27;
GN Name=ZFYVE27;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=16305752; DOI=10.1186/1471-2164-6-166;
RA Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L.,
RA Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L.;
RT "Characterization of 954 bovine full-CDS cDNA sequences.";
RL BMC Genomics 6:166-166(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Ascending colon;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (MAR-2007) 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; BT021199; AAX31381.1; -; mRNA.
DR EMBL; BC134516; AAI34517.1; -; mRNA.
DR RefSeq; NP_001017939.1; NM_001017939.1.
DR AlphaFoldDB; Q5BIM5; -.
DR SMR; Q5BIM5; -.
DR STRING; 9913.ENSBTAP00000071500; -.
DR PaxDb; 9913-ENSBTAP00000024705; -.
DR Ensembl; ENSBTAT00000024705.5; ENSBTAP00000024705.4; ENSBTAG00000018564.6.
DR GeneID; 514383; -.
DR KEGG; bta:514383; -.
DR CTD; 118813; -.
DR VEuPathDB; HostDB:ENSBTAG00000018564; -.
DR VGNC; VGNC:37177; ZFYVE27.
DR eggNOG; ENOG502QVKC; Eukaryota.
DR GeneTree; ENSGT00390000013298; -.
DR HOGENOM; CLU_060341_0_0_1; -.
DR InParanoid; Q5BIM5; -.
DR TreeFam; TF331044; -.
DR Proteomes; UP000009136; Chromosome 26.
DR Bgee; ENSBTAG00000018564; Expressed in retina and 105 other cell types or tissues.
DR ExpressionAtlas; Q5BIM5; baseline.
DR GO; GO:0030424; C:axon; ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0030425; C:dendrite; ISS:UniProtKB.
DR GO; GO:0005783; C:endoplasmic reticulum; ISS:UniProtKB.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; 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:0016020; C:membrane; ISS:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR GO; GO:0055038; C:recycling endosome membrane; ISS:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
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 CDD; cd15723; FYVE_protrudin; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 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; PROTRUDIN; 1.
DR PANTHER; PTHR14543:SF1; PROTRUDIN; 1.
DR Pfam; PF01363; FYVE; 1.
DR SMART; SM00064; FYVE; 1.
DR SUPFAM; SSF57903; FYVE/PHD zinc finger; 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..404
FT /note="Protrudin"
FT /id="PRO_0000245600"
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..404
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q5T4F4"
FT ZN_FING 337..403
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..20
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..354
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 343
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 346
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 359
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 362
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 367
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 370
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 395
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 398
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
SQ SEQUENCE 404 AA; 44777 MW; E03B5E78B1033F88 CRC64;
MQTSEREGCG PEVSPSTVPE ATLESLPVPT KLPAFDLFNL VLSYKRLEVY LEPLKDAGDG
VRYLLRWQTP LCSLLTCLGL NVLFLTLNEG AWYSVGALMI SVPALLGYLQ EGCQARLSES
ELMRRKYHSV RQEDLQRVRL SRPEAVAEVK SFLIQLEALL SRLCGTCEAA YRVLHWENPA
VSSQFYGALL GTVCMLYLLP LCWVLALLNS TLFLGNVEFF RVVSEYRASL QRRMNPKQEE
SAFESPPPSD AGGKGALVDC TPAPTPTEDL TPGSVEEAEE AEPDEEFKDA IEEDDEGAPC
PAEDELVLQD NGFLSKNEVL RSKVSRLTER LRKRYPTNNY GSCTGCSATF SVLKKRRNCS
NCGNIFCSRC CSFKVPRSSM GATAPEAQRE TVFVCASCNQ TLSK
//
