ZFY27_RAT
ID ZFY27_RAT Reviewed; 404 AA.
AC Q6P7B7;
DT 28-JUN-2011, integrated into UniProtKB/Swiss-Prot.
DT 28-JUN-2011, sequence version 2.
DT 03-AUG-2022, entry version 114.
DE RecName: Full=Protrudin;
DE AltName: Full=Zinc finger FYVE domain-containing protein 27;
GN Name=Zfyve27;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Prostate;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [2]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH RAB11.
RX PubMed=17082457; DOI=10.1126/science.1134027;
RA Shirane M., Nakayama K.I.;
RT "Protrudin induces neurite formation by directional membrane trafficking.";
RL Science 314:818-821(2006).
CC -!- FUNCTION: Key regulator of RAB11-dependent vesicular trafficking during
CC neurite extension through polarized membrane transport
CC (PubMed:17082457). Promotes axonal elongation and contributes to the
CC establishment of neuronal cell polarity. Involved in nerve growth
CC factor-induced neurite formation in VAPA-dependent manner. Contributes
CC to both the formation and stabilization of the tubular ER network.
CC Involved in ER morphogenesis by regulating the sheet-to-tubule balance
CC and possibly the density of tubule interconnections. Acts as an adapter
CC protein that facilitates the interaction of KIF5A with VAPA, VAPB,
CC SURF4, RAB11A, RAB11B and RTN3 and the ZFYVE27-KIF5A complex
CC contributes to the transport of these proteins in neurons. Can induce
CC formation of neurite-like membrane protrusions in non-neuronal cells in
CC a KIF5A/B-dependent manner (By similarity).
CC {ECO:0000250|UniProtKB:Q3TXX3, ECO:0000250|UniProtKB:Q5T4F4,
CC ECO:0000269|PubMed:17082457}.
CC -!- SUBUNIT: Can form homooligomers (monomers, dimers and tetramers).
CC Interacts with FKBP8; may negatively regulate ZFYVE27 phosphorylation.
CC Interacts with VAPA (via MSP domain); may regulate ZFYVE27 retention in
CC the endoplasmic reticulum and its function in cell projections
CC formation. Interacts with VAPB (via MSP domain) (By similarity).
CC Interacts with RAB11A (GDP-bound form); regulates RAB11A
CC (PubMed:17082457). Interacts with RAB11B (GDP-bound form), REEP1,
CC REEP5, ATL1, ATL2, ATL3, SPAST, SURF4, KIF5A, KIF5B, KIF5C and RTN3 (By
CC similarity). {ECO:0000250|UniProtKB:Q3TXX3,
CC ECO:0000250|UniProtKB:Q5T4F4, ECO:0000269|PubMed:17082457}.
CC -!- SUBCELLULAR LOCATION: Recycling endosome membrane
CC {ECO:0000269|PubMed:17082457}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:17082457}. Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:Q5T4F4}; Multi-pass membrane protein
CC {ECO:0000255}. Cell projection, growth cone membrane
CC {ECO:0000269|PubMed:17082457}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:17082457}. Note=Localizes at both dendrites and
CC axons. Localizes to endoplasmic reticulum tubular network.
CC {ECO:0000250|UniProtKB:Q3TXX3, 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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH61741.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; BC061741; AAH61741.1; ALT_INIT; mRNA.
DR RefSeq; NP_954535.2; NM_199104.2.
DR AlphaFoldDB; Q6P7B7; -.
DR BMRB; Q6P7B7; -.
DR SMR; Q6P7B7; -.
DR IntAct; Q6P7B7; 1.
DR STRING; 10116.ENSRNOP00000051399; -.
DR PaxDb; Q6P7B7; -.
DR PRIDE; Q6P7B7; -.
DR Ensembl; ENSRNOT00000083287; ENSRNOP00000074613; ENSRNOG00000014903.
DR GeneID; 309376; -.
DR KEGG; rno:309376; -.
DR UCSC; RGD:735177; rat.
DR CTD; 118813; -.
DR RGD; 735177; Zfyve27.
DR eggNOG; ENOG502QVKC; Eukaryota.
DR GeneTree; ENSGT00390000013298; -.
DR HOGENOM; CLU_060341_0_0_1; -.
DR InParanoid; Q6P7B7; -.
DR PRO; PR:Q6P7B7; -.
DR Proteomes; UP000002494; Chromosome 1.
DR Bgee; ENSRNOG00000014903; Expressed in frontal cortex and 19 other tissues.
DR ExpressionAtlas; Q6P7B7; baseline and differential.
DR GO; GO:0030424; C:axon; ISS:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; ISO:RGD.
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; IDA: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; IDA:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; ISO:RGD.
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; IMP:UniProtKB.
DR GO; GO:0048011; P:neurotrophin TRK receptor signaling pathway; IMP:UniProtKB.
DR GO; GO:0045773; P:positive regulation of axon extension; ISS:UniProtKB.
DR GO; GO:0072659; P:protein localization to plasma membrane; IDA: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 1: Evidence at protein 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_0000410350"
FT TOPO_DOM 1..63
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q5T4F4"
FT TRANSMEM 64..85
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 86..90
FT /note="Lumenal"
FT /evidence="ECO:0000250|UniProtKB:Q5T4F4"
FT TRANSMEM 91..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..25
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 259..299
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 COMPBIAS 273..299
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
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; 44948 MW; 6D63A2ECB90264FC CRC64;
MQSSDRDLSG PEASPSVMPE VLSECSPAPT KSTAFDLFNL VLSYKRLEIY LEPLKDAGDG
VRYLLRWQMP LCSLLTCLGL NILFLTLNEG AWYSVGALII SVPALLGYLQ EVCRAQLPES
ELMRRKYHSV RQEDLQRVRL SRPEAVAEVK SFLIRLEAFL ARLCYTCESA YRVLHWENPV
VSSQFYGALL GMVCMLYLLP LCWVLALLNS TLFLGNGEFF RVVSEYRACL QRRMSPKQEE
CVCEGSALQD AGGRAVVLDS TPAPTPTEDL TPGSVEEAEE AEPDEEFKDA IEEDDEGTPC
PAEDELTMQD NGFLSKNEVL RSKVSKLTER LRKRYPTNNF GNCAGCAATF SVLKKRRSCS
NCGNSFCSRC CSFKVPKSSM GATAPEAQRE TVFVCASCNQ TLSK
