VWA8_HUMAN
ID VWA8_HUMAN Reviewed; 1905 AA.
AC A3KMH1; O60310; Q5JTP6; Q5VW08; Q7Z6I9; Q86YC9; Q8N3E4;
DT 22-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT 22-JUL-2008, sequence version 2.
DT 03-AUG-2022, entry version 124.
DE RecName: Full=von Willebrand factor A domain-containing protein 8 {ECO:0000305};
DE AltName: Full=PEX7-binding protein 2 {ECO:0000303|PubMed:30204880};
DE Short=P7BP2 {ECO:0000303|PubMed:30204880};
DE Flags: Precursor;
GN Name=VWA8 {ECO:0000312|HGNC:HGNC:29071}; Synonyms=KIAA0564;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15057823; DOI=10.1038/nature02379;
RA Dunham A., Matthews L.H., Burton J., Ashurst J.L., Howe K.L.,
RA Ashcroft K.J., Beare D.M., Burford D.C., Hunt S.E., Griffiths-Jones S.,
RA Jones M.C., Keenan S.J., Oliver K., Scott C.E., Ainscough R., Almeida J.P.,
RA Ambrose K.D., Andrews D.T., Ashwell R.I.S., Babbage A.K., Bagguley C.L.,
RA Bailey J., Bannerjee R., Barlow K.F., Bates K., Beasley H., Bird C.P.,
RA Bray-Allen S., Brown A.J., Brown J.Y., Burrill W., Carder C., Carter N.P.,
RA Chapman J.C., Clamp M.E., Clark S.Y., Clarke G., Clee C.M., Clegg S.C.,
RA Cobley V., Collins J.E., Corby N., Coville G.J., Deloukas P., Dhami P.,
RA Dunham I., Dunn M., Earthrowl M.E., Ellington A.G., Faulkner L.,
RA Frankish A.G., Frankland J., French L., Garner P., Garnett J.,
RA Gilbert J.G.R., Gilson C.J., Ghori J., Grafham D.V., Gribble S.M.,
RA Griffiths C., Hall R.E., Hammond S., Harley J.L., Hart E.A., Heath P.D.,
RA Howden P.J., Huckle E.J., Hunt P.J., Hunt A.R., Johnson C., Johnson D.,
RA Kay M., Kimberley A.M., King A., Laird G.K., Langford C.J., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Lloyd C., Loveland J.E., Lovell J.,
RA Martin S., Mashreghi-Mohammadi M., McLaren S.J., McMurray A., Milne S.,
RA Moore M.J.F., Nickerson T., Palmer S.A., Pearce A.V., Peck A.I., Pelan S.,
RA Phillimore B., Porter K.M., Rice C.M., Searle S., Sehra H.K., Shownkeen R.,
RA Skuce C.D., Smith M., Steward C.A., Sycamore N., Tester J., Thomas D.W.,
RA Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P.,
RA Whitehead S.L., Willey D.L., Wilming L., Wray P.W., Wright M.W., Young L.,
RA Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Beck S., Bentley D.R.,
RA Rogers J., Ross M.T.;
RT "The DNA sequence and analysis of human chromosome 13.";
RL Nature 428:522-528(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] (ISOFORM 3).
RC TISSUE=Blood;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 295-1905 (ISOFORM 2), AND VARIANT
RP THR-383.
RC TISSUE=Amygdala;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 465-1905.
RC TISSUE=Brain;
RX PubMed=9628581; DOI=10.1093/dnares/5.1.31;
RA Nagase T., Ishikawa K., Miyajima N., Tanaka A., Kotani H., Nomura N.,
RA Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. IX. The
RT complete sequences of 100 new cDNA clones from brain which can code for
RT large proteins in vitro.";
RL DNA Res. 5:31-39(1998).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [7]
RP SUBUNIT, SUBCELLULAR LOCATION, INTERACTION WITH PEX7 AND PEX5, AND
RP ALTERNATIVE SPLICING.
RX PubMed=30204880; DOI=10.1093/jb/mvy073;
RA Niwa H., Miyauchi-Nanri Y., Okumoto K., Mukai S., Noi K., Ogura T.,
RA Fujiki Y.;
RT "A newly isolated Pex7-binding, atypical PTS2 protein P7BP2 is a novel
RT dynein-type AAA+ protein.";
RL J. Biochem. 164:437-447(2018).
CC -!- FUNCTION: Exhibits ATPase activity in vitro.
CC {ECO:0000250|UniProtKB:Q8CC88}.
CC -!- SUBUNIT: Monomer (PubMed:30204880). Isoform 1 and isoform 2 interact
CC with PEX7 (PubMed:30204880). Isoform 2 interacts with isoform 1 of PEX5
CC in a PEX7-dependent manner (PubMed:30204880).
CC {ECO:0000269|PubMed:30204880}.
CC -!- SUBCELLULAR LOCATION: [Isoform 1]: Mitochondrion
CC {ECO:0000269|PubMed:30204880}.
CC -!- SUBCELLULAR LOCATION: [Isoform 2]: Mitochondrion
CC {ECO:0000269|PubMed:30204880}. Peroxisome
CC {ECO:0000269|PubMed:30204880}. Note=Localizes to peroxisomes in a PEX7-
CC dependent manner. {ECO:0000269|PubMed:30204880}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1; Synonyms=P7BP2L {ECO:0000303|PubMed:30204880};
CC IsoId=A3KMH1-1; Sequence=Displayed;
CC Name=2; Synonyms=P7BP2S {ECO:0000303|PubMed:30204880};
CC IsoId=A3KMH1-2; Sequence=VSP_034533;
CC Name=3;
CC IsoId=A3KMH1-3; Sequence=VSP_061575;
CC -!- MISCELLANEOUS: [Isoform 2]: AA 66-79 are essential for peroxisome
CC localization. {ECO:0000269|PubMed:30204880}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAI31803.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AL160252; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL161417; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL163544; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL354833; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL442203; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC042924; AAH42924.2; -; mRNA.
DR EMBL; BC053674; AAH53674.2; -; mRNA.
DR EMBL; BC131802; AAI31803.1; ALT_INIT; mRNA.
DR EMBL; AB011136; BAA25490.1; -; mRNA.
DR EMBL; AL834181; CAD38878.1; -; mRNA.
DR CCDS; CCDS31963.1; -. [A3KMH1-2]
DR CCDS; CCDS41881.1; -. [A3KMH1-1]
DR PIR; T00335; T00335.
DR RefSeq; NP_001009814.1; NM_001009814.1. [A3KMH1-2]
DR RefSeq; NP_055873.1; NM_015058.1. [A3KMH1-1]
DR RefSeq; XP_016875963.1; XM_017020474.1.
DR AlphaFoldDB; A3KMH1; -.
DR BioGRID; 116710; 334.
DR IntAct; A3KMH1; 49.
DR MINT; A3KMH1; -.
DR STRING; 9606.ENSP00000368612; -.
DR GlyGen; A3KMH1; 6 sites, 1 O-linked glycan (1 site).
DR iPTMnet; A3KMH1; -.
DR PhosphoSitePlus; A3KMH1; -.
DR SwissPalm; A3KMH1; -.
DR BioMuta; VWA8; -.
DR EPD; A3KMH1; -.
DR jPOST; A3KMH1; -.
DR MassIVE; A3KMH1; -.
DR MaxQB; A3KMH1; -.
DR PaxDb; A3KMH1; -.
DR PeptideAtlas; A3KMH1; -.
DR PRIDE; A3KMH1; -.
DR ProteomicsDB; 577; -. [A3KMH1-1]
DR ProteomicsDB; 578; -. [A3KMH1-2]
DR ProteomicsDB; 579; -. [A3KMH1-3]
DR Antibodypedia; 23432; 13 antibodies from 7 providers.
DR DNASU; 23078; -.
DR Ensembl; ENST00000281496.6; ENSP00000281496.6; ENSG00000102763.18. [A3KMH1-2]
DR Ensembl; ENST00000379310.8; ENSP00000368612.3; ENSG00000102763.18. [A3KMH1-1]
DR GeneID; 23078; -.
DR KEGG; hsa:23078; -.
DR MANE-Select; ENST00000379310.8; ENSP00000368612.3; NM_015058.2; NP_055873.1.
DR UCSC; uc001uyj.4; human. [A3KMH1-1]
DR CTD; 23078; -.
DR DisGeNET; 23078; -.
DR GeneCards; VWA8; -.
DR HGNC; HGNC:29071; VWA8.
DR HPA; ENSG00000102763; Low tissue specificity.
DR MIM; 617509; gene.
DR neXtProt; NX_A3KMH1; -.
DR OpenTargets; ENSG00000102763; -.
DR PharmGKB; PA162392941; -.
DR VEuPathDB; HostDB:ENSG00000102763; -.
DR eggNOG; KOG1808; Eukaryota.
DR GeneTree; ENSGT00390000006601; -.
DR HOGENOM; CLU_001400_0_0_1; -.
DR InParanoid; A3KMH1; -.
DR OMA; GTHIVHP; -.
DR OrthoDB; 79800at2759; -.
DR PhylomeDB; A3KMH1; -.
DR TreeFam; TF300317; -.
DR PathwayCommons; A3KMH1; -.
DR SignaLink; A3KMH1; -.
DR BioGRID-ORCS; 23078; 12 hits in 1077 CRISPR screens.
DR ChiTaRS; VWA8; human.
DR GenomeRNAi; 23078; -.
DR Pharos; A3KMH1; Tdark.
DR PRO; PR:A3KMH1; -.
DR Proteomes; UP000005640; Chromosome 13.
DR RNAct; A3KMH1; protein.
DR Bgee; ENSG00000102763; Expressed in vastus lateralis and 198 other tissues.
DR Genevisible; A3KMH1; HS.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005739; C:mitochondrion; IDA:UniProtKB.
DR GO; GO:0005777; C:peroxisome; IDA:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; ISS:UniProtKB.
DR Gene3D; 3.40.50.300; -; 3.
DR Gene3D; 3.40.50.410; -; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR011704; ATPase_dyneun-rel_AAA.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR039891; VWA8.
DR InterPro; IPR002035; VWF_A.
DR InterPro; IPR036465; vWFA_dom_sf.
DR PANTHER; PTHR21610; PTHR21610; 1.
DR Pfam; PF07728; AAA_5; 3.
DR SMART; SM00382; AAA; 2.
DR SMART; SM00327; VWA; 1.
DR SUPFAM; SSF52540; SSF52540; 3.
DR SUPFAM; SSF53300; SSF53300; 1.
DR PROSITE; PS50234; VWFA; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; ATP-binding; Glycoprotein; Mitochondrion;
KW Nucleotide-binding; Peroxisome; Reference proteome; Transit peptide.
FT TRANSIT 1..28
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 29..1905
FT /note="von Willebrand factor A domain-containing protein 8"
FT /evidence="ECO:0000255"
FT /id="PRO_0000342685"
FT DOMAIN 1714..1896
FT /note="VWFA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00219"
FT REGION 1..261
FT /note="Interaction with PEX7"
FT /evidence="ECO:0000269|PubMed:30204880"
FT REGION 1542..1563
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1546..1560
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 447..454
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT CARBOHYD 284
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 855
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1096
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1142
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1833
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 1..96
FT /note="Missing (in isoform 3)"
FT /id="VSP_061575"
FT VAR_SEQ 1040..1905
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:17974005"
FT /id="VSP_034533"
FT VARIANT 165
FT /note="R -> H (in dbSNP:rs9562362)"
FT /id="VAR_044337"
FT VARIANT 383
FT /note="M -> T (in dbSNP:rs3742262)"
FT /evidence="ECO:0000269|PubMed:17974005"
FT /id="VAR_044338"
FT VARIANT 408
FT /note="G -> R (in dbSNP:rs17062601)"
FT /id="VAR_044339"
FT VARIANT 660
FT /note="R -> G (in dbSNP:rs9562353)"
FT /id="VAR_044340"
FT VARIANT 898
FT /note="R -> K (in dbSNP:rs41288291)"
FT /id="VAR_061239"
FT VARIANT 1300
FT /note="E -> K (in dbSNP:rs2274810)"
FT /id="VAR_049512"
SQ SEQUENCE 1905 AA; 214824 MW; 66706A1CF4E506B0 CRC64;
MQSRLLLLGA PGGHGGPASR RMRLLLRQVV QRRPGGDRQR PEVRLLHAGS GADTGDTVNI
GDVSYKLKIP KNPELVPQNY ISDSLAQSVV QHLRWIMQKD LLGQDVFLIG PPGPLRRSIA
MQYLELTKRE VEYIALSRDT TETDLKQRRE IRAGTAFYID QCAVRAATEG RTLILEGLEK
AERNVLPVLN NLLENREMQL EDGRFLMSAE RYDKLLRDHT KKELDSWKIV RVSENFRVIA
LGLPVPRYSG NPLDPPLRSR FQARDIYYLP FKDQLKLLYS IGANVSAEKV SQLLSFATTL
CSQESSTLGL PDFPLDSLAA AVQILDSFPM MPIKHAIQWL YPYSILLGHE GKMAVEGVLK
RFELQDSGSS LLPKEIVKVE KMMENHVSQA SVTIRIADKE VTIKVPAGTR LLSQPCASDR
FIQTLSHKQL QAEMMQSHMV KDICLIGGKG CGKTVIAKNF ADTLGYNIEP IMLYQDMTAR
DLLQQRYTLP NGDTAWRSSP LVNAALEGKL VLLDGIHRVN AGTLAVLQRL IHDRELSLYD
GSRLLREDRY MRLKEELQLS DEQLQKRSIF PIHPSFRIIA LAEPPVIGST AHQWLGPEFL
TMFFFHYMKP LVKSEEIQVI KEKVPNVPQE ALDKLLSFTH KLRETQDPTA QSLAASLSTR
QLLRISRRLS QYPNENLHSA VTKACLSRFL PSLARSALEK NLADATIEIN TDDNLEPELK
DYKCEVTSGT LRIGAVSAPI YNAHEKMKVP DVLFYDNIQH VIVMEDMLKD FLLGEHLLLV
GNQGVGKNKI VDRFLHLLNR PREYIQLHRD TTVQTLTLQP SVKDGLIVYE DSPLVKAVKL
GHILVVDEAD KAPTNVTCIL KTLVENGEMI LADGRRIVAN SANVNGRENV VVIHPDFRMI
VLANRPGFPF LGNDFFGTLG DIFSCHAVDN PKPHSELEML RQYGPNVPEP ILQKLVAAFG
ELRSLADQGI INYPYSTREV VNIVKHLQKF PTEGLSSVVR NVFDFDSYNN DMREILINTL
HKYGIPIGAK PTSVQLAKEL TLPEQTFMGY WTIGQARSGM QKLLCPVETH HIDIKGPALI
NIQEYPIERH EERSLNFTEE CASWRIPLDE INIICDIATS HENEQNTLYV VTCNPASLYF
MNMTGKSGFF VDFFDIFPRT ANGVWHPFVT VAPLGSPLKG QVVLHEQQSN VILLLDTTGR
ALHRLILPSE KFTSKKPFWW NKEEAETYKM CKEFSHKNWL VFYKEKGNSL TVLDVLEGRT
HTISLPINLK TVFLVAEDKW LLVESKTNQK YLLTKPAHIE SEGSGVCQLY VLKEEPPSTG
FGVTQETEFS IPHKISSDQL SSEHLSSAVE QKIASPNRIL SDEKNYATIV VGFPDLMSPS
EVYSWKRPSS LHKRSGTDTS FYRGKKKRGT PKQSNCVTLL DTNQVVRILP PGEVPLKDIY
PKDVTPPQTS GYIEVTDLQS KKLRYIPIPR SESLSPYTTW LSTISDTDAL LAEWDKSGVV
TVDMGGHIRL WETGLERLQR SLMEWRNMIG QDDRNMQITI NRDSGEDVSS PKHGKEDPDN
MPHVGGNTWA GGTGGRDTAG LGGKGGPYRL DAGHTVYQVS QAEKDAVPEE VKRAAREMGQ
RAFQQRLKEI QMSEYDAATY ERFSGAVRRQ VHSLRIILDN LQAKGKERQW LRHQATGELD
DAKIIDGLTG EKAIYKRRGE LEPQLGSPQQ KPKRLRLVVD VSGSMYRFNR MDGRLERTME
AVCMVMEAFE NYEEKFQYDI VGHSGDGYNI GLVPMNKIPK DNKQRLEILK TMHAHSQFCM
SGDHTLEGTE HAIKEIVKEE ADEYFVIVLS DANLSRYGIH PAKFAQILTR DPQVNAFAIF
IGSLGDQATR LQRTLPAGRS FVAMDTKDIP QILQQIFTST MLSSV
