Q5T4F4 (ZFY27_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Protrudin

Alternative name(s):
Zinc finger FYVE domain-containing protein 27

Gene names

Name:

ZFYVE27

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Dipnotetrapodomorpha › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	411 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Functions as an upstream inhibitor of RAB11, regulating directional protein transport to the forming neurites. Involved in nerve growth factor-induced neurite formation. May have a more general role in cell projections formation. Ref.5 Ref.7
Subunit structure	Interacts with SPAST. Interacts with RAB11A (GDP-bound form); regulates RAB11A. Interacts with FKBP8; may negatively regulate ZFYVE27 phosphorylation. Interacts with VAPA (via MSP domain); may regulate ZFYVE27 retention in the endoplasmic reticulum and its function in cell projections formation. Interacts with VAPB (via MSP domain). Ref.5 Ref.6 Ref.7 Ref.9
Subcellular location	Recycling endosome membrane; Multi-pass membrane protein. Endoplasmic reticulum membrane; Multi-pass membrane protein. Cell projection › growth cone membrane; Multi-pass membrane protein. Cell membrane; Multi-pass membrane protein. Note: Localizes at both dendrites and axons By similarity. Ref.7 Ref.9
Post-translational modification	Phosphorylated. Phosphorylation is induced by NGF through the MAPK/ERK pathway and modulates interaction with RAB11A. Ref.5
Involvement in disease	Spastic paraplegia 33, autosomal dominant (SPG33) [MIM:610244]: A form of spastic paraplegia, a neurodegenerative disorder characterized by a slow, gradual, progressive weakness and spasticity of the lower limbs. Rate of progression and the severity of symptoms are quite variable. Initial symptoms may include difficulty with balance, weakness and stiffness in the legs, muscle spasms, and dragging the toes when walking. In some forms of the disorder, bladder symptoms (such as incontinence) may appear, or the weakness and stiffness may spread to other parts of the body. Note: The disease is caused by mutations affecting the gene represented in this entry. According to Ref.10, the properties of the variant Val-191 and its frequency in some populations raise doubts on the implication of that gene in the disease. Ref.9 Ref.10
Sequence similarities	Contains 1 FYVE-type zinc finger.
Sequence caution	The sequence CAD38913.2 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

Ontologies

Keywords
Cellular component	Cell membrane Cell projection Endoplasmic reticulum Endosome Membrane
Coding sequence diversity	Alternative splicing Polymorphism
Disease	Disease mutation Hereditary spastic paraplegia Neurodegeneration
Domain	Transmembrane Transmembrane helix Zinc-finger
Ligand	Metal-binding Zinc
PTM	Glycoprotein Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	cell death Inferred from electronic annotation. Source: UniProtKB-KW neuron projection development Inferred from direct assay Ref.5. Source: UniProtKB neurotrophin TRK receptor signaling pathway Inferred from sequence or structural similarity. Source: UniProtKB protein localization to plasma membrane Inferred from sequence or structural similarity. Source: UniProtKB
Cellular_component	axon Inferred from sequence or structural similarity. Source: UniProtKB dendrite Inferred from sequence or structural similarity. Source: UniProtKB endoplasmic reticulum Inferred from direct assay Ref.7. Source: UniProtKB endoplasmic reticulum membrane Inferred from electronic annotation. Source: UniProtKB-SubCell growth cone membrane Inferred from sequence or structural similarity. Source: UniProtKB integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW recycling endosome membrane Inferred from sequence or structural similarity. Source: UniProtKB
Molecular_function	metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
FKBP8	Q14318	4	EBI-3892947,EBI-724839
RAB11A	P62491	4	EBI-3892947,EBI-745098
VAPA	Q9P0L0	5	EBI-3892947,EBI-1059156
VAPB	O95292	2	EBI-3892947,EBI-1188298

Alternative products

This entry describes 8 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q5T4F4-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Isoform 2 (identifier: Q5T4F4-2)

The sequence of this isoform differs from the canonical sequence as follows:
     294-300: Missing.

Isoform 3 (identifier: Q5T4F4-3)

The sequence of this isoform differs from the canonical sequence as follows:
     268-268: E → ESLSSQ

Isoform 4 (identifier: Q5T4F4-4)

The sequence of this isoform differs from the canonical sequence as follows:
     1-68: Missing.
     268-268: E → ESLSSQ
     294-300: Missing.
     349-356: NCTGCSAT → VTGAGSS
     357-411: Missing.

Isoform 5 (identifier: Q5T4F4-5)

The sequence of this isoform differs from the canonical sequence as follows:
     66-152: RWQMPLCSLL...PEAVAEVKSF → S
     294-300: Missing.

Isoform 6 (identifier: Q5T4F4-6)

The sequence of this isoform differs from the canonical sequence as follows:
     67-184: Missing.
     294-300: Missing.

Note: No experimental confirmation available.

Isoform 7 (identifier: Q5T4F4-7)

The sequence of this isoform differs from the canonical sequence as follows:
     1-98: Missing.
     268-268: E → ESLSSQ
     294-300: Missing.

Note: No experimental confirmation available.

Isoform 8 (identifier: Q5T4F4-8)

The sequence of this isoform differs from the canonical sequence as follows:
     58-89: Missing.
     294-300: Missing.

Note: No experimental confirmation available.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 411

411

Protrudin

PRO_0000245601

Regions

Topological domain

1 – 66

66

Cytoplasmic Potential

Transmembrane

67 – 87

21

Helical; Potential

Topological domain

88

1

Extracellular Potential

Transmembrane

89 – 109

21

Helical; Potential

Topological domain

110 – 187

78

Cytoplasmic Potential

Transmembrane

188 – 208

21

Helical; Potential

Topological domain

209 – 411

203

Extracellular Potential

Zinc finger

344 – 410

67

FYVE-type

Region

51 – 64

14

Necessary for interaction with RAB11A and function in neurite outgrowth

Region

286 – 292

7

Necessary for interaction with VAPA and function in cell projections formation

Compositional bias

246 – 249

4

Poly-Pro

Amino acid modifications

Glycosylation

209

1

N-linked (GlcNAc...) Potential

Natural variations

Alternative sequence

1 – 98

98

Missing in isoform 7.

VSP_045265

Alternative sequence

1 – 68

68

Missing in isoform 4.

VSP_019751

Alternative sequence

58 – 89

32

Missing in isoform 8.

VSP_046051

Alternative sequence

66 – 152

87

RWQMP…EVKSF → S in isoform 5.

VSP_019752

Alternative sequence

67 – 184

118

Missing in isoform 6.

VSP_045266

Alternative sequence

268

1

E → ESLSSQ in isoform 3, isoform 4 and isoform 7.

VSP_019753

Alternative sequence

294 – 300

7

Missing in isoform 2, isoform 4, isoform 5, isoform 6, isoform 7 and isoform 8.

VSP_019754

Alternative sequence

349 – 356

8

NCTGCSAT → VTGAGSS in isoform 4.

VSP_019755

Alternative sequence

357 – 411

55

Missing in isoform 4.

VSP_019756

Natural variant

82

1

V → I.
Corresponds to variant rs17108378 [ dbSNP | Ensembl ].

VAR_027002

Natural variant

138

1

G → V. Ref.1 Ref.3 Ref.4
Corresponds to variant rs10882993 [ dbSNP | Ensembl ].

VAR_027003

Natural variant

191

1

G → V in SPG33; aberrant subcellular localization and altered interaction with SPAST. Ref.9 Ref.10
Corresponds to variant rs35077384 [ dbSNP | Ensembl ].

VAR_027269

Experimental info

Mutagenesis

13

1

L → A: Alters interaction with RAB11A; when associated with A-49. Ref.5

Mutagenesis

49

1

I → A: Alters interaction with RAB11A; when associated with A-13. Ref.5

Mutagenesis

289

1

D → A: Loss of interaction with VAPA and loss of function in cell projections formation. Ref.7

Sequence conflict

50

1

Y → N in AAH30621. Ref.3

Sequence conflict

218

1

E → G in BAC11260. Ref.1

Sequence conflict

222

1

V → F in BAH13112. Ref.1

Sequence conflict

340

1

K → R in BAH13112. Ref.1

Sequence conflict

387

1

M → A in BAH13112. Ref.1

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

411

Helix Strand Turn

Details...

Beta strand

351 – 353

3

Beta strand

359 – 361

3

Beta strand

367 – 369

3

Turn

375 – 377

3

Beta strand

380 – 382

3

Turn

385 – 387

3

Beta strand

399 – 401

3

Helix

403 – 410

8

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified December 21, 2004. Version 1. Checksum: 5B86C64A398033D2	FASTA	411	45,843
	10 20 30 40 50 60 MQTSEREGSG PELSPSVMPE APLESPPFPT KSPAFDLFNL VLSYKRLEIY LEPLKDAGDG 70 80 90 100 110 120 VRYLLRWQMP LCSLLTCLGL NVLFLTLNEG AWYSVGALMI SVPALLGYLQ EVCRARLPDS 130 140 150 160 170 180 ELMRRKYHSV RQEDLQRGRL SRPEAVAEVK SFLIQLEAFL SRLCCTCEAA YRVLHWENPV 190 200 210 220 230 240 VSSQFYGALL GTVCMLYLLP LCWVLTLLNS TLFLGNVEFF RVVSEYRASL QQRMNPKQEE 250 260 270 280 290 300 HAFESPPPPD VGGKDGLMDS TPALTPTEDL TPGSVEEAEE AEPDEEFKDA IEETHLVVLE 310 320 330 340 350 360 DDEGAPCPAE DELALQDNGF LSKNEVLRSK VSRLTERLRK RYPTNNFGNC TGCSATFSVL 370 380 390 400 410 KKRRSCSNCG NSFCSRCCSF KVPKSSMGAT APEAQRETVF VCASCNQTLS K
	Isoform 2 [UniParc]. Checksum: 0FA0436DAE7716D7	FASTA	404	45,052
	10 20 30 40 50 60 MQTSEREGSG PELSPSVMPE APLESPPFPT KSPAFDLFNL VLSYKRLEIY LEPLKDAGDG 70 80 90 100 110 120 VRYLLRWQMP LCSLLTCLGL NVLFLTLNEG AWYSVGALMI SVPALLGYLQ EVCRARLPDS 130 140 150 160 170 180 ELMRRKYHSV RQEDLQRGRL SRPEAVAEVK SFLIQLEAFL SRLCCTCEAA YRVLHWENPV 190 200 210 220 230 240 VSSQFYGALL GTVCMLYLLP LCWVLTLLNS TLFLGNVEFF RVVSEYRASL QQRMNPKQEE 250 260 270 280 290 300 HAFESPPPPD VGGKDGLMDS TPALTPTEDL TPGSVEEAEE AEPDEEFKDA IEEDDEGAPC 310 320 330 340 350 360 PAEDELALQD NGFLSKNEVL RSKVSRLTER LRKRYPTNNF GNCTGCSATF SVLKKRRSCS 370 380 390 400 NCGNSFCSRC CSFKVPKSSM GATAPEAQRE TVFVCASCNQ TLSK
	Isoform 3 [UniParc]. Checksum: BF488D2456C6B924	FASTA	416	46,346
	10 20 30 40 50 60 MQTSEREGSG PELSPSVMPE APLESPPFPT KSPAFDLFNL VLSYKRLEIY LEPLKDAGDG 70 80 90 100 110 120 VRYLLRWQMP LCSLLTCLGL NVLFLTLNEG AWYSVGALMI SVPALLGYLQ EVCRARLPDS 130 140 150 160 170 180 ELMRRKYHSV RQEDLQRGRL SRPEAVAEVK SFLIQLEAFL SRLCCTCEAA YRVLHWENPV 190 200 210 220 230 240 VSSQFYGALL GTVCMLYLLP LCWVLTLLNS TLFLGNVEFF RVVSEYRASL QQRMNPKQEE 250 260 270 280 290 300 HAFESPPPPD VGGKDGLMDS TPALTPTESL SSQDLTPGSV EEAEEAEPDE EFKDAIEETH 310 320 330 340 350 360 LVVLEDDEGA PCPAEDELAL QDNGFLSKNE VLRSKVSRLT ERLRKRYPTN NFGNCTGCSA 370 380 390 400 410 TFSVLKKRRS CSNCGNSFCS RCCSFKVPKS SMGATAPEAQ RETVFVCASC NQTLSK
	Isoform 4 [UniParc]. Checksum: 977E99E1E5857BDD	FASTA	285	31,744
	10 20 30 40 50 60 MPLCSLLTCL GLNVLFLTLN EGAWYSVGAL MISVPALLGY LQEVCRARLP DSELMRRKYH 70 80 90 100 110 120 SVRQEDLQRG RLSRPEAVAE VKSFLIQLEA FLSRLCCTCE AAYRVLHWEN PVVSSQFYGA 130 140 150 160 170 180 LLGTVCMLYL LPLCWVLTLL NSTLFLGNVE FFRVVSEYRA SLQQRMNPKQ EEHAFESPPP 190 200 210 220 230 240 PDVGGKDGLM DSTPALTPTE SLSSQDLTPG SVEEAEEAEP DEEFKDAIEE DDEGAPCPAE 250 260 270 280 DELALQDNGF LSKNEVLRSK VSRLTERLRK RYPTNNFGVT GAGSS
	Isoform 5 [UniParc]. Checksum: 1E3E1DF487779DEB	FASTA	318	35,205
	10 20 30 40 50 60 MQTSEREGSG PELSPSVMPE APLESPPFPT KSPAFDLFNL VLSYKRLEIY LEPLKDAGDG 70 80 90 100 110 120 VRYLLSLIQL EAFLSRLCCT CEAAYRVLHW ENPVVSSQFY GALLGTVCML YLLPLCWVLT 130 140 150 160 170 180 LLNSTLFLGN VEFFRVVSEY RASLQQRMNP KQEEHAFESP PPPDVGGKDG LMDSTPALTP 190 200 210 220 230 240 TEDLTPGSVE EAEEAEPDEE FKDAIEEDDE GAPCPAEDEL ALQDNGFLSK NEVLRSKVSR 250 260 270 280 290 300 LTERLRKRYP TNNFGNCTGC SATFSVLKKR RSCSNCGNSF CSRCCSFKVP KSSMGATAPE 310 AQRETVFVCA SCNQTLSK
	Isoform 6 [UniParc]. Checksum: C4F817D0A286151B	FASTA	286	31,612
	10 20 30 40 50 60 MQTSEREGSG PELSPSVMPE APLESPPFPT KSPAFDLFNL VLSYKRLEIY LEPLKDAGDG 70 80 90 100 110 120 VRYLLRFYGA LLGTVCMLYL LPLCWVLTLL NSTLFLGNVE FFRVVSEYRA SLQQRMNPKQ 130 140 150 160 170 180 EEHAFESPPP PDVGGKDGLM DSTPALTPTE DLTPGSVEEA EEAEPDEEFK DAIEEDDEGA 190 200 210 220 230 240 PCPAEDELAL QDNGFLSKNE VLRSKVSRLT ERLRKRYPTN NFGNCTGCSA TFSVLKKRRS 250 260 270 280 CSNCGNSFCS RCCSFKVPKS SMGATAPEAQ RETVFVCASC NQTLSK
	Isoform 7 [UniParc]. Checksum: 3035EAF2EF4EEA53	FASTA	311	34,681
	10 20 30 40 50 60 MISVPALLGY LQEVCRARLP DSELMRRKYH SVRQEDLQRG RLSRPEAVAE VKSFLIQLEA 70 80 90 100 110 120 FLSRLCCTCE AAYRVLHWEN PVVSSQFYGA LLGTVCMLYL LPLCWVLTLL NSTLFLGNVE 130 140 150 160 170 180 FFRVVSEYRA SLQQRMNPKQ EEHAFESPPP PDVGGKDGLM DSTPALTPTE SLSSQDLTPG 190 200 210 220 230 240 SVEEAEEAEP DEEFKDAIEE DDEGAPCPAE DELALQDNGF LSKNEVLRSK VSRLTERLRK 250 260 270 280 290 300 RYPTNNFGNC TGCSATFSVL KKRRSCSNCG NSFCSRCCSF KVPKSSMGAT APEAQRETVF 310 VCASCNQTLS K
	Isoform 8 [UniParc]. Checksum: 0D235A6E1A98B2E2	FASTA	372	41,417
	10 20 30 40 50 60 MQTSEREGSG PELSPSVMPE APLESPPFPT KSPAFDLFNL VLSYKRLEIY LEPLKDAGAW 70 80 90 100 110 120 YSVGALMISV PALLGYLQEV CRARLPDSEL MRRKYHSVRQ EDLQRGRLSR PEAVAEVKSF 130 140 150 160 170 180 LIQLEAFLSR LCCTCEAAYR VLHWENPVVS SQFYGALLGT VCMLYLLPLC WVLTLLNSTL 190 200 210 220 230 240 FLGNVEFFRV VSEYRASLQQ RMNPKQEEHA FESPPPPDVG GKDGLMDSTP ALTPTEDLTP 250 260 270 280 290 300 GSVEEAEEAE PDEEFKDAIE EDDEGAPCPA EDELALQDNG FLSKNEVLRS KVSRLTERLR 310 320 330 340 350 360 KRYPTNNFGN CTGCSATFSV LKKRRSCSNC GNSFCSRCCS FKVPKSSMGA TAPEAQRETV 370 FVCASCNQTL SK

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Complete sequencing and characterization of 21,243 full-length human cDNAs." Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S. Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2; 4; 5; 6; 7 AND 8), VARIANT VAL-138. Tissue: Brain, Testis, Thalamus and Thymus.
[2]	"The DNA sequence and comparative analysis of human chromosome 10." Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L., Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K., Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L., Taylor A., Battles J. , Bird C.P., Ainscough R., Almeida J.P., Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P., Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N., Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A., Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C., Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C., Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K., Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A., Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S., McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S., Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A., Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P., Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y., Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D., Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J. Nature 429:375-381(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[3]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), VARIANT VAL-138. Tissue: Brain.
[4]	"The full-ORF clone resource of the German cDNA consortium." Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I. BMC Genomics 8:399-399(2007) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 23-411 (ISOFORM 3), VARIANT VAL-138. Tissue: Brain.
[5]	"Protrudin induces neurite formation by directional membrane trafficking." Shirane M., Nakayama K.I. Science 314:818-821(2006) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, INTERACTION WITH FKBP8 AND RAB11A, PHOSPHORYLATION, MUTAGENESIS OF LEU-13 AND ILE-49.
[6]	"Regulation of apoptosis and neurite extension by FKBP38 is required for neural tube formation in the mouse." Shirane M., Ogawa M., Motoyama J., Nakayama K.I. Genes Cells 13:635-651(2008) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH FKBP8.
[7]	"Promotion of neurite extension by protrudin requires its interaction with vesicle-associated membrane protein-associated protein." Saita S., Shirane M., Natume T., Iemura S., Nakayama K.I. J. Biol. Chem. 284:13766-13777(2009) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, INTERACTION WITH VAPA AND VAPB, MUTAGENESIS OF ASP-289, SUBCELLULAR LOCATION.
[8]	"Solution structure of the FYVE domain from human FYVE domain containing 27 isoform B protein." RIKEN structural genomics initiative (RSGI) Submitted (NOV-2005) to the PDB data bank Cited for: STRUCTURE BY NMR OF 341-411.
[9]	"ZFYVE27 (SPG33), a novel spastin-binding protein, is mutated in hereditary spastic paraplegia." Mannan A.U., Krawen P., Sauter S.M., Boehm J., Chronowska A., Paulus W., Neesen J., Engel W. Am. J. Hum. Genet. 79:351-357(2006) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT SPG33 VAL-191, CHARACTERIZATION OF VARIANT SPG33 VAL-191, SUBCELLULAR LOCATION, INTERACTION WITH SPAST.
[10]	"The role of ZFYVE27/protrudin in hereditary spastic paraplegia." Martignoni M., Riano E., Rugarli E.I. Am. J. Hum. Genet. 83:127-130(2008) [PubMed] [Europe PMC] [Abstract] Cited for: CHARACTERIZATION OF VARIANT SPG33 VAL-191.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AK057481 mRNA. Translation: BAB71506.1.
AK097945 mRNA. Translation: BAC05200.1.
AK074876 mRNA. Translation: BAC11260.1.
AK296295 mRNA. Translation: BAH12306.1.
AK296588 mRNA. Translation: BAH12390.1.
AK299735 mRNA. Translation: BAH13112.1.
AL358938 Genomic DNA. Translation: CAI14270.1.
AL358938 Genomic DNA. Translation: CAI14271.1.
AL358938 Genomic DNA. Translation: CAI14272.1.
BC030621 mRNA. Translation: AAH30621.2.
AL834235 mRNA. Translation: CAD38913.2. Different initiation.

IPI

IPI00166179.
IPI00301446.
IPI00332094.
IPI00434983.
IPI00922790.
IPI00927269.
IPI00956653.
IPI00956753.

RefSeq

NP_001002261.1. NM_001002261.3.
NP_001002262.1. NM_001002262.3.
NP_001167590.1. NM_001174119.1.
NP_001167591.1. NM_001174120.1.
NP_001167592.1. NM_001174121.1.
NP_001167593.1. NM_001174122.1.
NP_653189.3. NM_144588.6.
XP_005269559.1. XM_005269502.1.
XP_005269560.1. XM_005269503.1.
XP_005269561.1. XM_005269504.1.
XP_005269563.1. XM_005269506.1.

UniGene

Hs.744075.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1X4U	NMR	-	A	341-411	[»]

ProteinModelPortal

Q5T4F4.

SMR

Q5T4F4. Positions 341-411.

ModBase

Search...

Protein-protein interaction databases

IntAct

Q5T4F4. 7 interactions.

PTM databases

PhosphoSite

Q5T4F4.

Polymorphism databases

DMDM

74744927.

Proteomic databases

PaxDb

Q5T4F4.

PRIDE

Q5T4F4.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000337540; ENSP00000337993; ENSG00000155256.
ENST00000356257; ENSP00000348593; ENSG00000155256.
ENST00000357540; ENSP00000350148; ENSG00000155256.
ENST00000359980; ENSP00000353069; ENSG00000155256.
ENST00000370610; ENSP00000359642; ENSG00000155256.
ENST00000370613; ENSP00000359646; ENSG00000155256.
ENST00000393677; ENSP00000377282; ENSG00000155256.

GeneID

118813.

KEGG

hsa:118813.

UCSC

uc010qpd.2. human.

Organism-specific databases

CTD

118813.

GeneCards

GC10P099486.

HGNC

HGNC:26559. ZFYVE27.

HPA

HPA037523.

MIM

610243. gene.
610244. phenotype.

neXtProt

NX_Q5T4F4.

PharmGKB

PA134863310.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG28771.

HOVERGEN

HBG054907.

OMA

FNLVLSY.

OrthoDB

EOG7VTDNG.

Gene expression databases

ArrayExpress

Q5T4F4.

Bgee

Q5T4F4.

Genevestigator

Q5T4F4.

Family and domain databases

Gene3D

3.30.40.10. 1 hit.

InterPro

IPR000306. Znf_FYVE.
IPR017455. Znf_FYVE-rel.
IPR011011. Znf_FYVE_PHD.
IPR013083. Znf_RING/FYVE/PHD.
[Graphical view]

Pfam

PF01363. FYVE. 1 hit.
[Graphical view]

SMART

SM00064. FYVE. 1 hit.
[Graphical view]

SUPFAM

SSF57903. SSF57903. 1 hit.

PROSITE

PS50178. ZF_FYVE. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

ChiTaRS

ZFYVE27. human.

EvolutionaryTrace

Q5T4F4.

GenomeRNAi

118813.

NextBio

35535086.

PRO

Q5T4F4.

SOURCE

Search...

Entry information

Entry name

ZFY27_HUMAN

Accession

Primary (citable) accession number: Q5T4F4
Secondary accession number(s): B7Z3S0 , B7Z404, B7Z626, G8JLC3, G8JLF0, J3KP98, Q5T4F1, Q5T4F2, Q5T4F3, Q8N1K0, Q8N6D6, Q8NCA0, Q8NDE4, Q96M08

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 11, 2006
Last sequence update:	December 21, 2004
Last modified:	November 13, 2013
This is version 98 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.