HM13_MOUSE
ID HM13_MOUSE Reviewed; 378 AA.
AC Q9D8V0; A3KGS1; O19444; Q15K37; Q3TXP0; Q542R3; Q811Z6; Q8HWA9; Q8HWB5;
AC Q9CQA4; Q9CSK9;
DT 08-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 172.
DE RecName: Full=Minor histocompatibility antigen H13;
DE EC=3.4.23.-;
DE AltName: Full=Presenilin-like protein 3;
DE AltName: Full=Signal peptide peptidase;
GN Name=Hm13; Synonyms=H13, Psl3;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, AND DEVELOPMENTAL STAGE.
RC TISSUE=Placenta;
RX PubMed=12972007; DOI=10.1016/s1567-133x(03)00094-2;
RA Urny J., Hermans-Borgmeyer I., Gercken G., Chica Schaller H.;
RT "Expression of the presenilin-like signal peptide peptidase (SPP) in mouse
RT adult brain and during development.";
RL Gene Expr. Patterns 3:685-691(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 4), SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RX PubMed=16730383; DOI=10.1016/j.bbaexp.2006.02.007;
RA Urny J., Hermans-Borgmeyer I., Schaller H.C.;
RT "Cell-surface expression of a new splice variant of the mouse signal
RT peptide peptidase.";
RL Biochim. Biophys. Acta 1759:159-165(2006).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC STRAIN=BALB/cJ;
RA Irmler M., Tomiuk S., Korner M.R., Hofmann K., Conradt M.;
RT "Characterization of a new protein family with homology to presenilins.";
RL Submitted (SEP-2001) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND NUCLEOTIDE SEQUENCE [GENOMIC
RP DNA] OF 63-344.
RC STRAIN=129P3/J;
RA Brown A.C., Roopenian D.C.;
RT "Genomic analysis of the H13 minor histocompatibility antigen gene.";
RL Submitted (FEB-2002) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=C57BL/6J;
RC TISSUE=Adipose tissue, Cerebellum, Embryo, Lung, Ovary, Pancreas, Thymus,
RC and Uterus;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP NUCLEOTIDE SEQUENCE OF 119-193 (ISOFORM 3), AND FUNCTION.
RC STRAIN=BALB/cJ, C57BL/10, C57BL/6J, and LP/J; TISSUE=Thymic lymphoma;
RX PubMed=9354467; DOI=10.1016/s1074-7613(00)80368-4;
RA Mendoza L.M., Paz P., Zuberi A., Christianson G.J., Roopenian D.C.,
RA Shastri N.;
RT "Minors held by majors: the H13 minor histocompatibility locus defined as a
RT peptide/MHC class I complex.";
RL Immunity 7:461-472(1997).
RN [9]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 203-378 (ISOFORMS 1/3).
RC STRAIN=FVB/N; TISSUE=Mammary gland;
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 [10]
RP INTERACTION WITH RNF139.
RX PubMed=19720873; DOI=10.1083/jcb.200906110;
RA Stagg H.R., Thomas M., van den Boomen D., Wiertz E.J., Drabkin H.A.,
RA Gemmill R.M., Lehner P.J.;
RT "The TRC8 E3 ligase ubiquitinates MHC class I molecules before dislocation
RT from the ER.";
RL J. Cell Biol. 186:685-692(2009).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brown adipose tissue, Liver, Lung, Pancreas, Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [12]
RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 169-177 IN COMPLEX WITH H2-D.
RX PubMed=11751972; DOI=10.4049/jimmunol.168.1.283;
RA Ostrov D.A., Roden M.M., Shi W., Palmieri E., Christianson G.J.,
RA Mendoza L., Villaflor G., Tilley D., Shastri N., Grey H., Almo S.C.,
RA Roopenian D.C., Nathenson S.G.;
RT "How H13 histocompatibility peptides differing by a single methyl group and
RT lacking conventional MHC binding anchor motifs determine self-nonself
RT discrimination.";
RL J. Immunol. 168:283-289(2002).
CC -!- FUNCTION: Catalyzes intramembrane proteolysis of some signal peptides
CC after they have been cleaved from a preprotein, resulting in the
CC release of the fragment from the ER membrane into the cytoplasm.
CC Required to generate lymphocyte cell surface (HLA-E) epitopes derived
CC from MHC class I signal peptides. Involved in the intramembrane
CC cleavage of the integral membrane protein PSEN1. Cleaves the integral
CC membrane protein XBP1 isoform 1 in a DERL1/RNF139-dependent manner (By
CC similarity). May play a role in graft rejection (PubMed:9354467).
CC {ECO:0000250|UniProtKB:Q8TCT9, ECO:0000269|PubMed:9354467}.
CC -!- SUBUNIT: Monomer. Homodimer (By similarity). Interacts with RNF139
CC (PubMed:19720873). Interacts with DERL1 and XBP1 isoform 1 (By
CC similarity). {ECO:0000250|UniProtKB:Q8TCT9,
CC ECO:0000269|PubMed:19720873}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:12972007, ECO:0000269|PubMed:16730383}; Multi-pass
CC membrane protein {ECO:0000305}. Membrane
CC {ECO:0000250|UniProtKB:Q8TCT9}; Multi-pass membrane protein
CC {ECO:0000250|UniProtKB:Q8TCT9}; Lumenal side
CC {ECO:0000250|UniProtKB:Q8TCT9}.
CC -!- SUBCELLULAR LOCATION: [Isoform 4]: Cell membrane
CC {ECO:0000269|PubMed:16730383}; Multi-pass membrane protein
CC {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1; Synonyms=SPP-alpha;
CC IsoId=Q9D8V0-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9D8V0-2; Sequence=VSP_005199, VSP_005200;
CC Name=3;
CC IsoId=Q9D8V0-3; Sequence=VSP_005201, VSP_005202;
CC Name=4; Synonyms=SPP-beta;
CC IsoId=Q9D8V0-4; Sequence=VSP_039805;
CC -!- TISSUE SPECIFICITY: Widely expressed with highest levels in liver and
CC kidney. In the brain, expressed predominantly in hippocampus, amygdala,
CC piriform cortex, choroid plexus and arcuate nucleus of the hypothalamic
CC area. Isoform 1 is more strongly expressed than isoform 4 in most
CC tissues except brain and skeletal muscle where isoform 4 is the
CC dominant isoform and in testis where isoform 1 and isoform 4 are
CC expressed at similar levels. In the brain, isoform 4 is not detected in
CC the choroid plexus. {ECO:0000269|PubMed:12972007,
CC ECO:0000269|PubMed:16730383}.
CC -!- DEVELOPMENTAL STAGE: In the embryo, expression starts at day 6.5.
CC {ECO:0000269|PubMed:12972007}.
CC -!- DOMAIN: The first transmembrane domain may act as a type I signal
CC anchor. The PAL motif is required for normal active site conformation.
CC {ECO:0000250|UniProtKB:P49768, ECO:0000250|UniProtKB:Q8TCT9}.
CC -!- SIMILARITY: Belongs to the peptidase A22B family. {ECO:0000305}.
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DR EMBL; AF515662; AAN77098.1; -; mRNA.
DR EMBL; DQ168449; ABA56162.1; -; mRNA.
DR EMBL; AJ345032; CAC87793.1; -; mRNA.
DR EMBL; AF483214; AAM22075.1; -; mRNA.
DR EMBL; AF483216; AAM22077.1; -; Genomic_DNA.
DR EMBL; AK004690; BAB23476.1; -; mRNA.
DR EMBL; AK007664; BAB25172.1; -; mRNA.
DR EMBL; AK012600; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AK019877; BAB31897.1; -; mRNA.
DR EMBL; AK028109; BAC25752.1; -; mRNA.
DR EMBL; AK049101; BAC33543.1; -; mRNA.
DR EMBL; AK050664; BAC34369.1; -; mRNA.
DR EMBL; AK080966; BAC38098.1; -; mRNA.
DR EMBL; AK159176; BAE34875.1; -; mRNA.
DR EMBL; AK169922; BAE41461.1; -; mRNA.
DR EMBL; AL845162; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH466551; EDL05980.1; -; Genomic_DNA.
DR EMBL; CH466551; EDL05981.1; -; Genomic_DNA.
DR EMBL; AF017785; AAB81863.1; -; mRNA.
DR EMBL; BC034217; -; NOT_ANNOTATED_CDS; mRNA.
DR CCDS; CCDS16896.1; -. [Q9D8V0-1]
DR CCDS; CCDS50752.1; -. [Q9D8V0-4]
DR RefSeq; NP_001153023.1; NM_001159551.1. [Q9D8V0-4]
DR RefSeq; NP_001153025.1; NM_001159553.1. [Q9D8V0-2]
DR RefSeq; NP_034506.1; NM_010376.4. [Q9D8V0-1]
DR PDB; 1INQ; X-ray; 2.20 A; C=169-177.
DR PDB; 1JUF; X-ray; 2.00 A; C=169-177.
DR PDBsum; 1INQ; -.
DR PDBsum; 1JUF; -.
DR AlphaFoldDB; Q9D8V0; -.
DR SMR; Q9D8V0; -.
DR BioGRID; 200142; 2.
DR STRING; 10090.ENSMUSP00000086460; -.
DR MEROPS; A22.003; -.
DR GlyGen; Q9D8V0; 2 sites.
DR iPTMnet; Q9D8V0; -.
DR PhosphoSitePlus; Q9D8V0; -.
DR SwissPalm; Q9D8V0; -.
DR EPD; Q9D8V0; -.
DR jPOST; Q9D8V0; -.
DR MaxQB; Q9D8V0; -.
DR PeptideAtlas; Q9D8V0; -.
DR PRIDE; Q9D8V0; -.
DR ProteomicsDB; 269569; -. [Q9D8V0-1]
DR ProteomicsDB; 269570; -. [Q9D8V0-2]
DR ProteomicsDB; 269571; -. [Q9D8V0-3]
DR ProteomicsDB; 269572; -. [Q9D8V0-4]
DR Antibodypedia; 25181; 141 antibodies from 21 providers.
DR DNASU; 14950; -.
DR Ensembl; ENSMUST00000089059; ENSMUSP00000086460; ENSMUSG00000019188. [Q9D8V0-4]
DR Ensembl; ENSMUST00000125366; ENSMUSP00000120068; ENSMUSG00000019188. [Q9D8V0-1]
DR GeneID; 14950; -.
DR KEGG; mmu:14950; -.
DR UCSC; uc008nfz.2; mouse. [Q9D8V0-2]
DR UCSC; uc008ngb.2; mouse. [Q9D8V0-1]
DR UCSC; uc008ngc.2; mouse. [Q9D8V0-4]
DR CTD; 14950; -.
DR MGI; MGI:95886; H13.
DR VEuPathDB; HostDB:ENSMUSG00000019188; -.
DR eggNOG; KOG2443; Eukaryota.
DR GeneTree; ENSGT00940000156478; -.
DR HOGENOM; CLU_023799_0_0_1; -.
DR InParanoid; Q9D8V0; -.
DR OMA; LFSYEDH; -.
DR OrthoDB; 1087991at2759; -.
DR PhylomeDB; Q9D8V0; -.
DR TreeFam; TF105854; -.
DR BRENDA; 3.4.23.B24; 3474.
DR Reactome; R-MMU-9707587; Regulation of HMOX1 expression and activity.
DR BioGRID-ORCS; 14950; 9 hits in 76 CRISPR screens.
DR ChiTaRS; H13; mouse.
DR EvolutionaryTrace; Q9D8V0; -.
DR PRO; PR:Q9D8V0; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; Q9D8V0; protein.
DR Bgee; ENSMUSG00000019188; Expressed in seminal vesicle and 275 other tissues.
DR ExpressionAtlas; Q9D8V0; baseline and differential.
DR Genevisible; Q9D8V0; MM.
DR GO; GO:0009986; C:cell surface; IDA:UniProtKB.
DR GO; GO:0036513; C:Derlin-1 retrotranslocation complex; ISO:MGI.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:UniProtKB.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IDA:MGI.
DR GO; GO:0071458; C:integral component of cytoplasmic side of endoplasmic reticulum membrane; ISS:UniProtKB.
DR GO; GO:0071556; C:integral component of lumenal side of endoplasmic reticulum membrane; ISS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005791; C:rough endoplasmic reticulum; ISS:UniProtKB.
DR GO; GO:0042500; F:aspartic endopeptidase activity, intramembrane cleaving; ISS:UniProtKB.
DR GO; GO:0008233; F:peptidase activity; ISS:UniProtKB.
DR GO; GO:0042803; F:protein homodimerization activity; ISS:UniProtKB.
DR GO; GO:0031625; F:ubiquitin protein ligase binding; ISO:MGI.
DR GO; GO:0001701; P:in utero embryonic development; IMP:MGI.
DR GO; GO:0033619; P:membrane protein proteolysis; ISS:UniProtKB.
DR GO; GO:1904211; P:membrane protein proteolysis involved in retrograde protein transport, ER to cytosol; ISO:MGI.
DR GO; GO:0006465; P:signal peptide processing; IBA:GO_Central.
DR InterPro; IPR007369; Peptidase_A22B_SPP.
DR InterPro; IPR006639; Preselin/SPP.
DR PANTHER; PTHR12174; PTHR12174; 1.
DR Pfam; PF04258; Peptidase_A22B; 1.
DR SMART; SM00730; PSN; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cell membrane; Endoplasmic reticulum;
KW Glycoprotein; Hydrolase; Membrane; Phosphoprotein; Protease;
KW Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..378
FT /note="Minor histocompatibility antigen H13"
FT /id="PRO_0000073908"
FT TOPO_DOM 1..31
FT /note="Lumenal"
FT /evidence="ECO:0000250|UniProtKB:Q8TCT9"
FT TRANSMEM 32..52
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 53..77
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 78..98
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 99..100
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 101..121
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 122..157
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 158..178
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 179..181
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 182..202
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 203..209
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 210..230
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 231..256
FT /note="Lumenal"
FT /evidence="ECO:0000250|UniProtKB:Q8TCT9"
FT TRANSMEM 257..277
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 278..290
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 291..311
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 312..314
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 315..335
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 336..378
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q8TCT9"
FT REGION 1..27
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 346..378
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 317..319
FT /note="PAL"
FT COMPBIAS 13..27
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 352..378
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 219
FT /evidence="ECO:0000250|UniProtKB:P49810"
FT ACT_SITE 265
FT /evidence="ECO:0000250|UniProtKB:P49810"
FT MOD_RES 368
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8TCT9"
FT CARBOHYD 10
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 20
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 119..151
FT /note="HTISPFMNKFFPANFPNRQYQLLFTQGSGENKE -> DDADSHALLQALTGW
FT GWGGSLTLGSELIWPLCP (in isoform 3)"
FT /evidence="ECO:0000305"
FT /id="VSP_005201"
FT VAR_SEQ 122..173
FT /note="SPFMNKFFPANFPNRQYQLLFTQGSGENKEEIINYEFDTKDLVCLGLSSVVG
FT -> RSEGISRQPLKLLSQEPVQGLGWEHGLLCHSEPGLNPGCKIQGNLPSRQHYT (in
FT isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_005199"
FT VAR_SEQ 174..378
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_005200"
FT VAR_SEQ 181..193
FT /note="HWIANNLFGLAFS -> VSQSLRRRGGWAD (in isoform 3)"
FT /evidence="ECO:0000305"
FT /id="VSP_005202"
FT VAR_SEQ 348..378
FT /note="ESNPKDPAAETESKEESTEASASKRLEKKEK -> SSAVILPHTPRLTHFPT
FT VSGSPASLADSMQQKLAGPRRRRPQNPSAM (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:16730383"
FT /id="VSP_039805"
FT CONFLICT 42
FT /note="M -> T (in Ref. 2; ABA56162)"
FT /evidence="ECO:0000305"
FT CONFLICT 53
FT /note="R -> P (in Ref. 3; CAC87793 and 4; AAM22075)"
FT /evidence="ECO:0000305"
FT CONFLICT 73
FT /note="R -> Q (in Ref. 4; AAM22077)"
FT /evidence="ECO:0000305"
FT CONFLICT 172
FT /note="V -> I (in Ref. 1; AAN77098, 4; AAM22077 and 5;
FT BAE34875)"
FT /evidence="ECO:0000305"
FT CONFLICT 294
FT /note="S -> E (in Ref. 5; BAC25752)"
FT /evidence="ECO:0000305"
FT CONFLICT 357
FT /note="E -> V (in Ref. 1; AAN77098, 3; CAC87793, 4;
FT AAM22075 and 5; BAE34875)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 378 AA; 41748 MW; FB3B047323239A0D CRC64;
MDSAVSDPHN GSAEAGTPAN GTTRPPSTPE GIALAYGSLL LMALLPIFFG ALRSVRCARG
KSSSDMPETI TSRDAARFPI IASCTLLGLY LFFKIFSQEY INLLLSMYFF VLGILALSHT
ISPFMNKFFP ANFPNRQYQL LFTQGSGENK EEIINYEFDT KDLVCLGLSS VVGVWYLLRK
HWIANNLFGL AFSLNGVELL HLNNVSTGCI LLGGLFIYDI FWVFGTNVMV TVAKSFEAPI
KLVFPQDLLE KGLEADNFAM LGLGDIVIPG IFIALLLRFD ISLKKNTHTY FYTSFAAYIF
GLGLTIFIMH IFKHAQPALL YLVPACIGFP VLVALAKGEV AEMFSYEESN PKDPAAETES
KEESTEASAS KRLEKKEK
