YIPF3_HUMAN
ID YIPF3_HUMAN Reviewed; 350 AA.
AC Q9GZM5; Q5JTD2; Q6FI85; Q8NI57; Q9NWE3; Q9Y3U9;
DT 27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 154.
DE RecName: Full=Protein YIPF3;
DE AltName: Full=Killer lineage protein 1;
DE AltName: Full=Natural killer cell-specific antigen KLIP1;
DE AltName: Full=YIP1 family member 3;
DE Contains:
DE RecName: Full=Protein YIPF3, 36 kDa form III;
GN Name=YIPF3; Synonyms=C6orf109, KLIP1;
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 [MRNA], FUNCTION, DEVELOPMENTAL STAGE, TISSUE
RP SPECIFICITY, GLYCOSYLATION, AND SUBCELLULAR LOCATION.
RC TISSUE=Lung;
RX PubMed=12490290; DOI=10.1006/bcmd.2002.0563;
RA Prost S., LeDiscorde M., Haddad R., Gluckman J.-C., Canque B.,
RA Kirszenbaum M.;
RT "Characterization of a novel hematopoietic marker expressed from early
RT embryonic hematopoietic stem cells to adult mature lineages.";
RL Blood Cells Mol. Dis. 29:236-248(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Embryo;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=14574404; DOI=10.1038/nature02055;
RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R.,
RA Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D.,
RA Andrews T.D., Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H.,
RA Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J.,
RA Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E.,
RA Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J.,
RA French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J.,
RA Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C.,
RA Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A.,
RA Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R.,
RA Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M.,
RA Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K.,
RA Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R.,
RA Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A.,
RA Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L.,
RA Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I.,
RA Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y.,
RA Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E.,
RA Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A.,
RA Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W.,
RA Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M.,
RA West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J.,
RA Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M.,
RA Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I.,
RA Rogers J., Beck S.;
RT "The DNA sequence and analysis of human chromosome 6.";
RL Nature 425:805-811(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Skin;
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 7-350.
RC TISSUE=Fetal kidney;
RX PubMed=11230166; DOI=10.1101/gr.gr1547r;
RA Wiemann S., Weil B., Wellenreuther R., Gassenhuber J., Glassl S.,
RA Ansorge W., Boecher M., Bloecker H., Bauersachs S., Blum H., Lauber J.,
RA Duesterhoeft A., Beyer A., Koehrer K., Strack N., Mewes H.-W.,
RA Ottenwaelder B., Obermaier B., Tampe J., Heubner D., Wambutt R., Korn B.,
RA Klein M., Poustka A.;
RT "Towards a catalog of human genes and proteins: sequencing and analysis of
RT 500 novel complete protein coding human cDNAs.";
RL Genome Res. 11:422-435(2001).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 36-350.
RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [7]
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 [8]
RP FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH YIPF4, AND GLYCOSYLATION
RP AT THR-333; THR-334; ASN-337 AND THR-346.
RX PubMed=21757827; DOI=10.1247/csf.11002;
RA Tanimoto K., Suzuki K., Jokitalo E., Sakai N., Sakaguchi T., Tamura D.,
RA Fujii G., Aoki K., Takada S., Ishida R., Tanabe M., Itoh H., Yoneda Y.,
RA Sohda M., Misumi Y., Nakamura N.;
RT "Characterization of YIPF3 and YIPF4, cis-Golgi localizing Yip domain
RT family proteins.";
RL Cell Struct. Funct. 36:171-185(2011).
RN [9]
RP GLYCOSYLATION AT THR-346, STRUCTURE OF CARBOHYDRATES, AND IDENTIFICATION BY
RP MASS SPECTROMETRY.
RX PubMed=22171320; DOI=10.1074/mcp.m111.013649;
RA Halim A., Nilsson J., Ruetschi U., Hesse C., Larson G.;
RT "Human urinary glycoproteomics; attachment site specific analysis of N- and
RT O-linked glycosylations by CID and ECD.";
RL Mol. Cell. Proteomics 11:1-17(2012).
RN [10]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [11]
RP GLYCOSYLATION AT THR-339 AND THR-346, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RX PubMed=23234360; DOI=10.1021/pr300963h;
RA Halim A., Ruetschi U., Larson G., Nilsson J.;
RT "LC-MS/MS characterization of O-glycosylation sites and glycan structures
RT of human cerebrospinal fluid glycoproteins.";
RL J. Proteome Res. 12:573-584(2013).
RN [12]
RP SUBCELLULAR LOCATION, TOPOLOGY, AND INTERACTION WITH YIPF4 AND YIPF5.
RX PubMed=27999994; DOI=10.1007/s00418-016-1527-3;
RA Kranjc T., Dempsey E., Cagney G., Nakamura N., Shields D.C., Simpson J.C.;
RT "Functional characterisation of the YIPF protein family in mammalian
RT cells.";
RL Histochem. Cell Biol. 147:439-451(2017).
CC -!- FUNCTION: Involved in the maintenance of the Golgi structure. May play
CC a role in hematopoiesis. {ECO:0000269|PubMed:12490290,
CC ECO:0000269|PubMed:21757827}.
CC -!- SUBUNIT: Interacts with YIPF4 and YIPF5. {ECO:0000269|PubMed:21757827,
CC ECO:0000269|PubMed:27999994}.
CC -!- INTERACTION:
CC Q9GZM5; P49639: HOXA1; NbExp=3; IntAct=EBI-743787, EBI-740785;
CC Q9GZM5; Q0VD86: INCA1; NbExp=3; IntAct=EBI-743787, EBI-6509505;
CC Q9GZM5; Q8IUG1: KRTAP1-3; NbExp=3; IntAct=EBI-743787, EBI-11749135;
CC Q9GZM5; P60410: KRTAP10-8; NbExp=3; IntAct=EBI-743787, EBI-10171774;
CC Q9GZM5; P60411: KRTAP10-9; NbExp=3; IntAct=EBI-743787, EBI-10172052;
CC Q9GZM5; Q8IUC1: KRTAP11-1; NbExp=3; IntAct=EBI-743787, EBI-1052037;
CC Q9GZM5; P59991: KRTAP12-2; NbExp=3; IntAct=EBI-743787, EBI-10176379;
CC Q9GZM5; Q9BYR7: KRTAP3-2; NbExp=7; IntAct=EBI-743787, EBI-751260;
CC Q9GZM5; P26371: KRTAP5-9; NbExp=3; IntAct=EBI-743787, EBI-3958099;
CC Q9GZM5; Q9BYQ2: KRTAP9-4; NbExp=3; IntAct=EBI-743787, EBI-10185730;
CC Q9GZM5; Q9BYQ0: KRTAP9-8; NbExp=3; IntAct=EBI-743787, EBI-11958364;
CC Q9GZM5; Q7Z3S9: NOTCH2NLA; NbExp=4; IntAct=EBI-743787, EBI-945833;
CC Q9GZM5; Q8IWZ5: TRIM42; NbExp=3; IntAct=EBI-743787, EBI-5235829;
CC Q9GZM5; Q9BSR8: YIPF4; NbExp=10; IntAct=EBI-743787, EBI-751253;
CC -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
CC Cytoplasm. Golgi apparatus, cis-Golgi network membrane
CC {ECO:0000269|PubMed:27999994}; Multi-pass membrane protein.
CC Note=Localization to the cytoplasm or to the cell membrane is
CC developmentally and ontogenetically regulated.
CC -!- TISSUE SPECIFICITY: Expressed by nucleated hematopoietic cells (at
CC protein level). {ECO:0000269|PubMed:12490290}.
CC -!- DEVELOPMENTAL STAGE: Expressed in fetal liver (at protein level).
CC Expressed in embryonic hematopoiesis sites.
CC {ECO:0000269|PubMed:12490290}.
CC -!- PTM: N-glycosylated in the ER (40 kDa form I), then O-glycosylated in
CC the Golgi apparatus (46 kDa form II), the C-terminal lumenal region is
CC later removed in the Golgi apparatus to produce a 36 kDa form III. O-
CC glycosylated with core 1-like and core 2-like glycans. O-glycan
CC heterogeneity at Thr-346: HexNAc (minor), HexHexNAc (major),
CC Hex1HexNAc2 (minor), Hex2HexNAc2 (minor) and dHex1Hex2HexNAc2 (minor).
CC {ECO:0000269|PubMed:12490290, ECO:0000269|PubMed:21757827,
CC ECO:0000269|PubMed:22171320, ECO:0000269|PubMed:23234360}.
CC -!- SIMILARITY: Belongs to the YIP1 family. {ECO:0000305}.
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DR EMBL; AF162672; AAM21161.1; -; mRNA.
DR EMBL; AK000946; BAA91439.1; -; mRNA.
DR EMBL; AK021655; BAB13866.1; -; mRNA.
DR EMBL; AK022757; BAB14231.1; -; mRNA.
DR EMBL; AL355802; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC019297; AAH19297.1; -; mRNA.
DR EMBL; AL050274; CAB43375.2; -; mRNA.
DR EMBL; CR533541; CAG38572.1; -; mRNA.
DR CCDS; CCDS4899.1; -.
DR PIR; T08721; T08721.
DR RefSeq; NP_056203.2; NM_015388.3.
DR AlphaFoldDB; Q9GZM5; -.
DR BioGRID; 117370; 204.
DR IntAct; Q9GZM5; 113.
DR MINT; Q9GZM5; -.
DR STRING; 9606.ENSP00000361499; -.
DR TCDB; 9.B.135.2.1; the membrane trafficking yip (yip) family.
DR CarbonylDB; Q9GZM5; -.
DR GlyConnect; 641; 7 N-Linked glycans (1 site), 40 O-Linked glycans (3 sites).
DR GlyGen; Q9GZM5; 7 sites, 7 N-linked glycans (1 site), 16 O-linked glycans (4 sites).
DR iPTMnet; Q9GZM5; -.
DR MetOSite; Q9GZM5; -.
DR PhosphoSitePlus; Q9GZM5; -.
DR SwissPalm; Q9GZM5; -.
DR BioMuta; YIPF3; -.
DR DMDM; 74752534; -.
DR EPD; Q9GZM5; -.
DR jPOST; Q9GZM5; -.
DR MassIVE; Q9GZM5; -.
DR MaxQB; Q9GZM5; -.
DR PaxDb; Q9GZM5; -.
DR PeptideAtlas; Q9GZM5; -.
DR PRIDE; Q9GZM5; -.
DR ProteomicsDB; 80087; -.
DR Antibodypedia; 3101; 118 antibodies from 23 providers.
DR DNASU; 25844; -.
DR Ensembl; ENST00000372422.7; ENSP00000361499.2; ENSG00000137207.12.
DR GeneID; 25844; -.
DR KEGG; hsa:25844; -.
DR MANE-Select; ENST00000372422.7; ENSP00000361499.2; NM_015388.4; NP_056203.2.
DR UCSC; uc003ovl.2; human.
DR CTD; 25844; -.
DR DisGeNET; 25844; -.
DR GeneCards; YIPF3; -.
DR HGNC; HGNC:21023; YIPF3.
DR HPA; ENSG00000137207; Low tissue specificity.
DR MIM; 609775; gene.
DR neXtProt; NX_Q9GZM5; -.
DR OpenTargets; ENSG00000137207; -.
DR PharmGKB; PA134946615; -.
DR VEuPathDB; HostDB:ENSG00000137207; -.
DR eggNOG; KOG3114; Eukaryota.
DR GeneTree; ENSGT00940000153766; -.
DR InParanoid; Q9GZM5; -.
DR OMA; HCIVLFV; -.
DR OrthoDB; 1332379at2759; -.
DR PhylomeDB; Q9GZM5; -.
DR TreeFam; TF314073; -.
DR PathwayCommons; Q9GZM5; -.
DR SignaLink; Q9GZM5; -.
DR BioGRID-ORCS; 25844; 56 hits in 1081 CRISPR screens.
DR ChiTaRS; YIPF3; human.
DR GeneWiki; YIPF3; -.
DR GenomeRNAi; 25844; -.
DR Pharos; Q9GZM5; Tbio.
DR PRO; PR:Q9GZM5; -.
DR Proteomes; UP000005640; Chromosome 6.
DR RNAct; Q9GZM5; protein.
DR Bgee; ENSG00000137207; Expressed in body of pancreas and 185 other tissues.
DR ExpressionAtlas; Q9GZM5; baseline and differential.
DR Genevisible; Q9GZM5; HS.
DR GO; GO:0005794; C:Golgi apparatus; IDA:HPA.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0030133; C:transport vesicle; IDA:LIFEdb.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR InterPro; IPR026637; YIPF3.
DR PANTHER; PTHR15627:SF14; PTHR15627:SF14; 1.
PE 1: Evidence at protein level;
KW Acetylation; Cell membrane; Cytoplasm; Differentiation; Glycoprotein;
KW Golgi apparatus; Membrane; Reference proteome; Transmembrane;
KW Transmembrane helix.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:22814378"
FT CHAIN 2..350
FT /note="Protein YIPF3"
FT /id="PRO_0000244446"
FT CHAIN 2..?
FT /note="Protein YIPF3, 36 kDa form III"
FT /id="PRO_0000418216"
FT TOPO_DOM 2..148
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:27999994"
FT TRANSMEM 149..169
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 170..187
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 188..208
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 209..214
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 215..237
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 238..240
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 241..263
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 264..274
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 275..295
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 296..350
FT /note="Lumenal"
FT /evidence="ECO:0000305|PubMed:27999994"
FT REGION 1..51
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0007744|PubMed:22814378"
FT CARBOHYD 333
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000269|PubMed:21757827"
FT CARBOHYD 334
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000269|PubMed:21757827"
FT CARBOHYD 337
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:21757827"
FT CARBOHYD 339
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000269|PubMed:23234360"
FT CARBOHYD 346
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000269|PubMed:21757827,
FT ECO:0000269|PubMed:22171320, ECO:0000269|PubMed:23234360"
FT VARIANT 5
FT /note="A -> V (in dbSNP:rs2231763)"
FT /id="VAR_026906"
FT CONFLICT 103
FT /note="R -> G (in Ref. 6; CAG38572)"
FT /evidence="ECO:0000305"
FT CONFLICT 142
FT /note="M -> V (in Ref. 2; BAA91439)"
FT /evidence="ECO:0000305"
FT CONFLICT 161
FT /note="F -> L (in Ref. 1; AAM21161)"
FT /evidence="ECO:0000305"
FT CONFLICT 305
FT /note="D -> V (in Ref. 5; CAB43375 and 6; CAG38572)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 350 AA; 38248 MW; ED7A566716A6B364 CRC64;
MATTAAPAGG ARNGAGPEWG GFEENIQGGG SAVIDMENMD DTSGSSFEDM GELHQRLREE
EVDADAADAA AAEEEDGEFL GMKGFKGQLS RQVADQMWQA GKRQASRAFS LYANIDILRP
YFDVEPAQVR SRLLESMIPI KMVNFPQKIA GELYGPLMLV FTLVAILLHG MKTSDTIIRE
GTLMGTAIGT CFGYWLGVSS FIYFLAYLCN AQITMLQMLA LLGYGLFGHC IVLFITYNIH
LHALFYLFWL LVGGLSTLRM VAVLVSRTVG PTQRLLLCGT LAALHMLFLL YLHFAYHKVV
EGILDTLEGP NIPPIQRVPR DIPAMLPAAR LPTTVLNATA KAVAVTLQSH
