MACOI_HUMAN
ID MACOI_HUMAN Reviewed; 664 AA.
AC Q8N5G2; B1AK00; Q2TLX5; Q2TLX6; Q9NVG6;
DT 07-FEB-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 142.
DE RecName: Full=Macoilin {ECO:0000303|PubMed:21589894};
DE AltName: Full=Macoilin-1 {ECO:0000312|HGNC:HGNC:25572};
DE AltName: Full=Transmembrane protein 57;
GN Name=MACO1 {ECO:0000312|HGNC:HGNC:25572};
GN Synonyms=TMEM57 {ECO:0000312|HGNC:HGNC:25572};
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] (ISOFORMS 1; 2 AND 3).
RA Huang C.-H., Peng J., Ye T., Chen Y.;
RT "Identification of macoilin as a novel membrane-associated coiled-coil
RT tetraspanin protein.";
RL Submitted (DEC-2004) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain;
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 [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-332 AND SER-631, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19369195; DOI=10.1074/mcp.m800588-mcp200;
RA Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,
RA Mann M., Daub H.;
RT "Large-scale proteomics analysis of the human kinome.";
RL Mol. Cell. Proteomics 8:1751-1764(2009).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-332 AND SER-634, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-332, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [10]
RP SUBCELLULAR LOCATION, AND FUNCTION.
RX PubMed=21589894; DOI=10.1371/journal.pgen.1001384;
RA Miyara A., Ohta A., Okochi Y., Tsukada Y., Kuhara A., Mori I.;
RT "Novel and conserved protein macoilin is required for diverse neuronal
RT functions in Caenorhabditis elegans.";
RL PLoS Genet. 7:E1001384-E1001384(2011).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-305, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [12]
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).
CC -!- FUNCTION: Plays a role in the regulation of neuronal activity.
CC {ECO:0000269|PubMed:21589894}.
CC -!- INTERACTION:
CC Q8N5G2; P48745: CCN3; NbExp=3; IntAct=EBI-2683507, EBI-3904822;
CC Q8N5G2; Q9UGL9: CRCT1; NbExp=5; IntAct=EBI-2683507, EBI-713677;
CC Q8N5G2; P49639: HOXA1; NbExp=3; IntAct=EBI-2683507, EBI-740785;
CC Q8N5G2; Q701N4: KRTAP5-2; NbExp=3; IntAct=EBI-2683507, EBI-11958178;
CC Q8N5G2; Q6L8G8: KRTAP5-7; NbExp=3; IntAct=EBI-2683507, EBI-11987425;
CC Q8N5G2; Q5T751: LCE1C; NbExp=3; IntAct=EBI-2683507, EBI-12224199;
CC Q8N5G2; Q5T752: LCE1D; NbExp=3; IntAct=EBI-2683507, EBI-11741311;
CC Q8N5G2; Q5T753: LCE1E; NbExp=3; IntAct=EBI-2683507, EBI-11955335;
CC Q8N5G2; Q5T754: LCE1F; NbExp=3; IntAct=EBI-2683507, EBI-11958008;
CC Q8N5G2; Q5TA81: LCE2C; NbExp=3; IntAct=EBI-2683507, EBI-11973993;
CC Q8N5G2; Q5TA76: LCE3A; NbExp=3; IntAct=EBI-2683507, EBI-9394625;
CC Q8N5G2; Q5T5B0: LCE3E; NbExp=3; IntAct=EBI-2683507, EBI-10245456;
CC Q8N5G2; Q96FE5: LINGO1; NbExp=3; IntAct=EBI-2683507, EBI-719955;
CC Q8N5G2; A8MW99: MEI4; NbExp=3; IntAct=EBI-2683507, EBI-19944212;
CC Q8N5G2; Q6FHY5: MEOX2; NbExp=3; IntAct=EBI-2683507, EBI-16439278;
CC Q8N5G2; P0DPK4: NOTCH2NLC; NbExp=3; IntAct=EBI-2683507, EBI-22310682;
CC Q8N5G2; Q92570: NR4A3; NbExp=3; IntAct=EBI-2683507, EBI-13644623;
CC Q8N5G2; A0JP26: POTEB3; NbExp=3; IntAct=EBI-2683507, EBI-18165900;
CC Q8N5G2; P49901: SMCP; NbExp=3; IntAct=EBI-2683507, EBI-750494;
CC Q8N5G2; Q8WZ59: TMEM190; NbExp=3; IntAct=EBI-2683507, EBI-10278423;
CC Q8N5G2; Q8N720: ZNF655; NbExp=3; IntAct=EBI-2683507, EBI-625509;
CC -!- SUBCELLULAR LOCATION: Nucleus membrane {ECO:0000250|UniProtKB:Q7TQE6};
CC Multi-pass membrane protein {ECO:0000255}. Cell projection, axon
CC {ECO:0000250|UniProtKB:Q7TQE6}. Rough endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:21589894}; Multi-pass membrane protein
CC {ECO:0000255}. Note=Detected in the nucleus membrane of non-neuronal
CC cells and in axonal outgrowths of neuronal cells.
CC {ECO:0000250|UniProtKB:Q7TQE6}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q8N5G2-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8N5G2-2; Sequence=VSP_017203;
CC Name=3;
CC IsoId=Q8N5G2-3; Sequence=VSP_017204, VSP_017205;
CC -!- SIMILARITY: Belongs to the macoilin family. {ECO:0000305}.
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DR EMBL; AY845015; AAX11913.1; -; mRNA.
DR EMBL; AY845036; AAX11934.1; -; mRNA.
DR EMBL; AY845035; AAX11933.1; -; mRNA.
DR EMBL; AK001609; BAA91786.1; -; mRNA.
DR EMBL; AL031284; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BX572623; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471059; EAX07876.1; -; Genomic_DNA.
DR EMBL; BC032427; AAH32427.1; -; mRNA.
DR CCDS; CCDS30638.1; -. [Q8N5G2-1]
DR CCDS; CCDS60034.1; -. [Q8N5G2-3]
DR RefSeq; NP_001269493.1; NM_001282564.1. [Q8N5G2-3]
DR RefSeq; NP_060672.2; NM_018202.5. [Q8N5G2-1]
DR AlphaFoldDB; Q8N5G2; -.
DR SMR; Q8N5G2; -.
DR BioGRID; 120515; 177.
DR IntAct; Q8N5G2; 54.
DR MINT; Q8N5G2; -.
DR STRING; 9606.ENSP00000363463; -.
DR TCDB; 8.A.38.1.1; the animal macoilin regulator of ion channels (macoilin) family.
DR GlyGen; Q8N5G2; 4 sites.
DR iPTMnet; Q8N5G2; -.
DR PhosphoSitePlus; Q8N5G2; -.
DR BioMuta; TMEM57; -.
DR DMDM; 74728992; -.
DR EPD; Q8N5G2; -.
DR jPOST; Q8N5G2; -.
DR MassIVE; Q8N5G2; -.
DR MaxQB; Q8N5G2; -.
DR PaxDb; Q8N5G2; -.
DR PeptideAtlas; Q8N5G2; -.
DR PRIDE; Q8N5G2; -.
DR ProteomicsDB; 72049; -. [Q8N5G2-1]
DR ProteomicsDB; 72050; -. [Q8N5G2-2]
DR ProteomicsDB; 72051; -. [Q8N5G2-3]
DR Antibodypedia; 15928; 78 antibodies from 16 providers.
DR DNASU; 55219; -.
DR Ensembl; ENST00000374343.5; ENSP00000363463.4; ENSG00000204178.11. [Q8N5G2-1]
DR Ensembl; ENST00000399766.7; ENSP00000382668.3; ENSG00000204178.11. [Q8N5G2-3]
DR GeneID; 55219; -.
DR KEGG; hsa:55219; -.
DR MANE-Select; ENST00000374343.5; ENSP00000363463.4; NM_018202.6; NP_060672.2.
DR UCSC; uc001bkk.5; human. [Q8N5G2-1]
DR CTD; 55219; -.
DR DisGeNET; 55219; -.
DR GeneCards; MACO1; -.
DR HGNC; HGNC:25572; MACO1.
DR HPA; ENSG00000204178; Low tissue specificity.
DR MIM; 610301; gene.
DR neXtProt; NX_Q8N5G2; -.
DR OpenTargets; ENSG00000204178; -.
DR PharmGKB; PA142670773; -.
DR VEuPathDB; HostDB:ENSG00000204178; -.
DR eggNOG; KOG1821; Eukaryota.
DR GeneTree; ENSGT00390000016613; -.
DR HOGENOM; CLU_051352_0_0_1; -.
DR InParanoid; Q8N5G2; -.
DR OMA; KIHEMEY; -.
DR OrthoDB; 1227984at2759; -.
DR PhylomeDB; Q8N5G2; -.
DR TreeFam; TF324023; -.
DR PathwayCommons; Q8N5G2; -.
DR Reactome; R-HSA-8980692; RHOA GTPase cycle.
DR Reactome; R-HSA-9013106; RHOC GTPase cycle.
DR SignaLink; Q8N5G2; -.
DR BioGRID-ORCS; 55219; 13 hits in 1081 CRISPR screens.
DR ChiTaRS; MACO1; human.
DR GenomeRNAi; 55219; -.
DR Pharos; Q8N5G2; Tbio.
DR PRO; PR:Q8N5G2; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; Q8N5G2; protein.
DR Bgee; ENSG00000204178; Expressed in cortical plate and 187 other tissues.
DR ExpressionAtlas; Q8N5G2; baseline and differential.
DR Genevisible; Q8N5G2; HS.
DR GO; GO:0030424; C:axon; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0044306; C:neuron projection terminus; ISS:BHF-UCL.
DR GO; GO:0031965; C:nuclear membrane; ISS:BHF-UCL.
DR GO; GO:0005634; C:nucleus; ISS:BHF-UCL.
DR GO; GO:0030867; C:rough endoplasmic reticulum membrane; IDA:UniProtKB.
DR GO; GO:0045202; C:synapse; ISS:BHF-UCL.
DR GO; GO:0008017; F:microtubule binding; IBA:GO_Central.
DR GO; GO:0007420; P:brain development; IEA:Ensembl.
DR GO; GO:0006935; P:chemotaxis; IBA:GO_Central.
DR GO; GO:0023041; P:neuronal signal transduction; IMP:UniProtKB.
DR InterPro; IPR019130; Macoilin.
DR PANTHER; PTHR47464:SF3; PTHR47464:SF3; 1.
DR Pfam; PF09726; Macoilin; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell projection; Endoplasmic reticulum; Glycoprotein;
KW Membrane; Nucleus; Phosphoprotein; Reference proteome; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..664
FT /note="Macoilin"
FT /id="PRO_0000070266"
FT TRANSMEM 28..48
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 75..95
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 120..140
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 154..174
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 253..274
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 320..375
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 630..664
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 253..267
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 320..351
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 630..655
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 305
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 332
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231"
FT MOD_RES 631
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 634
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332"
FT CARBOHYD 324
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 340
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 452
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 655
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 27..384
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|Ref.1"
FT /id="VSP_017203"
FT VAR_SEQ 158
FT /note="C -> W (in isoform 3)"
FT /evidence="ECO:0000303|Ref.1"
FT /id="VSP_017204"
FT VAR_SEQ 159..385
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|Ref.1"
FT /id="VSP_017205"
FT CONFLICT 577
FT /note="R -> I (in Ref. 2; BAA91786)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 664 AA; 76178 MW; C0F16B66E13AC281 CRC64;
MKRRNADCSK LRRPLKRNRI TEGIYGSTFL YLKFLVVWAL VLLADFVLEF RFEYLWPFWL
FIRSVYDSFR YQGLAFSVFF VCVAFTSNII CLLFIPIQWL FFAASTYVWV QYVWHTERGV
CLPTVSLWIL FVYIEAAIRF KDLKNFHVDL CRPFAAHCIG YPVVTLGFGF KSYVSYKMRL
RKQKEVQKEN EFYMQLLQQA LPPEQQMLQK QEKEAEEAAK GLPDMDSSIL IHHNGGIPAN
KKLSTTLPEI EYREKGKEKD KDAKKHNLGI NNNNILQPVD SKIQEIEYME NHINSKRLNN
DLVGSTENLL KEDSCTASSK NYKNASGVVN SSPRSHSATN GSIPSSSSKN EKKQKCTSKS
PSTHKDLMEN CIPNNQLSKP DALVRLEQDI KKLKADLQAS RQVEQELRSQ ISSLSSTERG
IRSEMGQLRQ ENELLQNKLH NAVQMKQKDK QNISQLEKKL KAEQEARSFV EKQLMEEKKR
KKLEEATAAR AVAFAAASRG ECTETLRNRI RELEAEGKKL TMDMKVKEDQ IRELELKVQE
LRKYKENEKD TEVLMSALSA MQDKTQHLEN SLSAETRIKL DLFSALGDAK RQLEIAQGQI
LQKDQEIKDL KQKIAEVMAV MPSITYSAAT SPLSPVSPHY SSKFVETSPS GLDPNASVYQ
PLKK
