YIF1B_HUMAN
ID YIF1B_HUMAN Reviewed; 314 AA.
AC Q5BJH7; H7BXS8; Q5JPC2; Q8WY70; Q96C02; Q96IC4;
DT 23-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT 27-SEP-2005, sequence version 1.
DT 03-AUG-2022, entry version 123.
DE RecName: Full=Protein YIF1B {ECO:0000305};
DE AltName: Full=YIP1-interacting factor homolog B;
GN Name=YIF1B {ECO:0000312|HGNC:HGNC:30511}; ORFNames=PP4519, UNQ3073/PRO9905;
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 MRNA] (ISOFORM 2).
RX PubMed=12975309; DOI=10.1101/gr.1293003;
RA Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J.,
RA Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P.,
RA Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E., Heldens S., Huang A.,
RA Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J., Lewis L., Liao D.,
RA Mark M.R., Robbie E., Sanchez C., Schoenfeld J., Seshagiri S., Simmons L.,
RA Singh J., Smith V., Stinson J., Vagts A., Vandlen R.L., Watanabe C.,
RA Wieand D., Woods K., Xie M.-H., Yansura D.G., Yi S., Yu G., Yuan J.,
RA Zhang M., Zhang Z., Goddard A.D., Wood W.I., Godowski P.J., Gray A.M.;
RT "The secreted protein discovery initiative (SPDI), a large-scale effort to
RT identify novel human secreted and transmembrane proteins: a bioinformatics
RT assessment.";
RL Genome Res. 13:2265-2270(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RX PubMed=15498874; DOI=10.1073/pnas.0404089101;
RA Wan D., Gong Y., Qin W., Zhang P., Li J., Wei L., Zhou X., Li H., Qiu X.,
RA Zhong F., He L., Yu J., Yao G., Jiang H., Qian L., Yu Y., Shu H., Chen X.,
RA Xu H., Guo M., Pan Z., Chen Y., Ge C., Yang S., Gu J.;
RT "Large-scale cDNA transfection screening for genes related to cancer
RT development and progression.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:15724-15729(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
RC TISSUE=Lymph node;
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 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 (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15057824; DOI=10.1038/nature02399;
RA Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E.,
RA Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A.,
RA Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S.,
RA Carrano A.V., Caoile C., Chan Y.M., Christensen M., Cleland C.A.,
RA Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J.,
RA Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M.,
RA Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W.,
RA Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V.,
RA Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D.,
RA McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I.,
RA Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L.,
RA Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A.,
RA She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M.,
RA Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J.,
RA Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E.,
RA Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M.,
RA Rubin E.M., Lucas S.M.;
RT "The DNA sequence and biology of human chromosome 19.";
RL Nature 428:529-535(2004).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 5), AND NUCLEOTIDE
RP SEQUENCE [LARGE SCALE MRNA] OF 2-314 (ISOFORM 3).
RC TISSUE=Colon, Lung, and Placenta;
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 [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-65, AND IDENTIFICATION BY
RP 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 [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-65, AND IDENTIFICATION BY
RP 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 IDENTIFICATION BY 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 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 [11]
RP SUBCELLULAR LOCATION.
RX PubMed=26077767; DOI=10.1111/tra.12306;
RA Alterio J., Masson J., Diaz J., Chachlaki K., Salman H., Areias J.,
RA Al Awabdh S., Emerit M.B., Darmon M.;
RT "Yif1B Is Involved in the Anterograde Traffic Pathway and the Golgi
RT Architecture.";
RL Traffic 16:978-993(2015).
RN [12]
RP INTERACTION WITH ABCB9.
RX PubMed=30877195; DOI=10.1074/jbc.ra118.007071;
RA Graab P., Bock C., Weiss K., Hirth A., Koller N., Braner M., Jung J.,
RA Loehr F., Tampe R., Behrends C., Abele R.;
RT "Lysosomal targeting of the ABC transporter TAPL is determined by membrane-
RT localized charged residues.";
RL J. Biol. Chem. 294:7308-7323(2019).
RN [13]
RP INVOLVEMENT IN KABAMAS, AND VARIANT KABAMAS 200-GLU--ARG-314 DEL.
RX PubMed=32006098; DOI=10.1007/s00401-020-02128-8;
RA AlMuhaizea M., AlMass R., AlHargan A., AlBader A., Medico Salsench E.,
RA Howaidi J., Ihinger J., Karachunski P., Begtrup A., Segura Castell M.,
RA Bauer P., Bertoli-Avella A., Kaya I.H., AlSufayan J., AlQuait L.,
RA Chedrawi A., Arold S.T., Colak D., Barakat T.S., Kaya N.;
RT "Truncating mutations in YIF1B cause a progressive encephalopathy with
RT various degrees of mixed movement disorder, microcephaly, and epilepsy.";
RL Acta Neuropathol. 139:791-794(2020).
RN [14]
RP VARIANTS KABAMAS GLN-123 AND 200-GLU--ARG-314 DEL, CHARACTERIZATION OF
RP VARIANTS KABAMAS GLN-123 AND 200-GLU--ARG-314 DEL, AND FUNCTION.
RX PubMed=33103737; DOI=10.1093/brain/awaa235;
RA Diaz J., Gerard X., Emerit M.B., Areias J., Geny D., Degardin J.,
RA Simonutti M., Guerquin M.J., Collin T., Viollet C., Billard J.M., Metin C.,
RA Hubert L., Larti F., Kahrizi K., Jobling R., Agolini E., Shaheen R.,
RA Zigler A., Rouiller-Fabre V., Rozet J.M., Picaud S., Novelli A.,
RA Alameer S., Najmabadi H., Cohn R., Munnich A., Barth M., Lugli L.,
RA Alkuraya F.S., Blaser S., Gashlan M., Besmond C., Darmon M., Masson J.;
RT "YIF1B mutations cause a post-natal neurodevelopmental syndrome associated
RT with Golgi and primary cilium alterations.";
RL Brain 143:2911-2928(2020).
CC -!- FUNCTION: Functions in endoplasmic reticulum to Golgi vesicle-mediated
CC transport and regulates the proper organization of the endoplasmic
CC reticulum and the Golgi (By similarity). Plays a key role in targeting
CC to neuronal dendrites receptors such as HTR1A (By similarity). Plays
CC also a role in primary cilium and sperm flagellum assembly probably
CC through protein transport to these compartments (PubMed:33103737).
CC {ECO:0000250|UniProtKB:Q6PEC3, ECO:0000250|UniProtKB:Q9CX30,
CC ECO:0000269|PubMed:33103737}.
CC -!- SUBUNIT: Interacts with HTR1A (via C-terminus). Interacts with ABCB9
CC (via TMD0); this interaction allows (but is not essential) the ER-to-
CC Golgi trafficking and strongly depends on a salt bridge within TMD0
CC (PubMed:30877195). {ECO:0000250|UniProtKB:Q6PEC3,
CC ECO:0000269|PubMed:30877195}.
CC -!- INTERACTION:
CC Q5BJH7; O15354: GPR37; NbExp=2; IntAct=EBI-11288011, EBI-15639515;
CC Q5BJH7-5; Q9BS40: LXN; NbExp=3; IntAct=EBI-12158885, EBI-1044504;
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:26077767}; Multi-pass membrane protein
CC {ECO:0000255}. Golgi apparatus membrane {ECO:0000269|PubMed:26077767};
CC Multi-pass membrane protein {ECO:0000255}. Endoplasmic reticulum-Golgi
CC intermediate compartment membrane {ECO:0000269|PubMed:26077767}; Multi-
CC pass membrane protein {ECO:0000255}. Note=Shuttles between the
CC endoplasmic reticulum, the intermediate compartment and the Golgi
CC apparatus. {ECO:0000269|PubMed:26077767}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=6;
CC Name=1;
CC IsoId=Q5BJH7-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q5BJH7-2; Sequence=VSP_028650;
CC Name=3;
CC IsoId=Q5BJH7-3; Sequence=VSP_028651;
CC Name=4;
CC IsoId=Q5BJH7-4; Sequence=VSP_028651, VSP_028653, VSP_028654;
CC Name=5;
CC IsoId=Q5BJH7-5; Sequence=VSP_028651, VSP_028652, VSP_028655;
CC Name=6;
CC IsoId=Q5BJH7-6; Sequence=VSP_046823;
CC -!- DISEASE: Kaya-Barakat-Masson syndrome (KABAMAS) [MIM:619125]: An
CC autosomal recessive neurodevelopmental disorder characterized by
CC impaired intellectual development, absent speech, hypotonia, profound
CC developmental and motor delay with dystonia, poor coordination and
CC spasticity, and visual deficits with brain MRI evidence of ventricle
CC enlargement, myelination alterations and cerebellar atrophy.
CC {ECO:0000269|PubMed:32006098, ECO:0000269|PubMed:33103737}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
CC -!- SIMILARITY: Belongs to the YIF1 family. {ECO:0000305}.
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DR EMBL; AY358965; AAQ89324.1; -; mRNA.
DR EMBL; AF258578; AAG23781.1; -; mRNA.
DR EMBL; AL833382; CAI46138.1; -; mRNA.
DR EMBL; AC011479; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471126; EAW56772.1; -; Genomic_DNA.
DR EMBL; BC007644; AAH07644.1; -; mRNA.
DR EMBL; BC014974; AAH14974.1; -; mRNA.
DR EMBL; BC091477; AAH91477.2; -; mRNA.
DR CCDS; CCDS12512.1; -. [Q5BJH7-2]
DR CCDS; CCDS33010.1; -. [Q5BJH7-1]
DR CCDS; CCDS46066.1; -. [Q5BJH7-6]
DR CCDS; CCDS46067.1; -. [Q5BJH7-4]
DR RefSeq; NP_001034761.1; NM_001039672.2. [Q5BJH7-1]
DR RefSeq; NP_001034762.1; NM_001039673.2. [Q5BJH7-3]
DR RefSeq; NP_001138934.1; NM_001145462.1. [Q5BJH7-2]
DR RefSeq; NP_001138935.1; NM_001145463.1. [Q5BJH7-4]
DR RefSeq; XP_005259442.1; XM_005259385.3. [Q5BJH7-2]
DR RefSeq; XP_016882938.1; XM_017027449.1. [Q5BJH7-5]
DR AlphaFoldDB; Q5BJH7; -.
DR BioGRID; 124728; 87.
DR IntAct; Q5BJH7; 21.
DR MINT; Q5BJH7; -.
DR STRING; 9606.ENSP00000343435; -.
DR GlyGen; Q5BJH7; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q5BJH7; -.
DR PhosphoSitePlus; Q5BJH7; -.
DR BioMuta; YIF1B; -.
DR DMDM; 121944384; -.
DR EPD; Q5BJH7; -.
DR jPOST; Q5BJH7; -.
DR MassIVE; Q5BJH7; -.
DR MaxQB; Q5BJH7; -.
DR PaxDb; Q5BJH7; -.
DR PeptideAtlas; Q5BJH7; -.
DR PRIDE; Q5BJH7; -.
DR ProteomicsDB; 43383; -.
DR ProteomicsDB; 62693; -. [Q5BJH7-1]
DR ProteomicsDB; 62694; -. [Q5BJH7-2]
DR ProteomicsDB; 62695; -. [Q5BJH7-3]
DR ProteomicsDB; 62696; -. [Q5BJH7-4]
DR ProteomicsDB; 62697; -. [Q5BJH7-5]
DR Antibodypedia; 30011; 125 antibodies from 19 providers.
DR DNASU; 90522; -.
DR Ensembl; ENST00000329420.12; ENSP00000329559.7; ENSG00000167645.17. [Q5BJH7-6]
DR Ensembl; ENST00000337679.12; ENSP00000337411.7; ENSG00000167645.17. [Q5BJH7-4]
DR Ensembl; ENST00000339413.11; ENSP00000343435.5; ENSG00000167645.17. [Q5BJH7-1]
DR Ensembl; ENST00000392124.7; ENSP00000375971.2; ENSG00000167645.17. [Q5BJH7-2]
DR Ensembl; ENST00000591755.5; ENSP00000465446.1; ENSG00000167645.17. [Q5BJH7-5]
DR Ensembl; ENST00000591784.5; ENSP00000465230.1; ENSG00000167645.17. [Q5BJH7-2]
DR Ensembl; ENST00000592694.5; ENSP00000466428.1; ENSG00000167645.17. [Q5BJH7-2]
DR GeneID; 90522; -.
DR KEGG; hsa:90522; -.
DR MANE-Select; ENST00000339413.11; ENSP00000343435.5; NM_001039672.3; NP_001034761.1.
DR UCSC; uc002ohw.3; human. [Q5BJH7-1]
DR CTD; 90522; -.
DR DisGeNET; 90522; -.
DR GeneCards; YIF1B; -.
DR HGNC; HGNC:30511; YIF1B.
DR HPA; ENSG00000167645; Low tissue specificity.
DR MalaCards; YIF1B; -.
DR MIM; 619109; gene.
DR MIM; 619125; phenotype.
DR neXtProt; NX_Q5BJH7; -.
DR OpenTargets; ENSG00000167645; -.
DR PharmGKB; PA142670561; -.
DR VEuPathDB; HostDB:ENSG00000167645; -.
DR eggNOG; KOG3094; Eukaryota.
DR GeneTree; ENSGT00390000009423; -.
DR InParanoid; Q5BJH7; -.
DR OMA; FMWLLTR; -.
DR PhylomeDB; Q5BJH7; -.
DR TreeFam; TF314528; -.
DR PathwayCommons; Q5BJH7; -.
DR SignaLink; Q5BJH7; -.
DR SIGNOR; Q5BJH7; -.
DR BioGRID-ORCS; 90522; 9 hits in 1079 CRISPR screens.
DR ChiTaRS; YIF1B; human.
DR GenomeRNAi; 90522; -.
DR Pharos; Q5BJH7; Tbio.
DR PRO; PR:Q5BJH7; -.
DR Proteomes; UP000005640; Chromosome 19.
DR RNAct; Q5BJH7; protein.
DR Bgee; ENSG00000167645; Expressed in monocyte and 167 other tissues.
DR ExpressionAtlas; Q5BJH7; baseline and differential.
DR Genevisible; Q5BJH7; HS.
DR GO; GO:0030134; C:COPII-coated ER to Golgi transport vesicle; IBA:GO_Central.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:UniProtKB.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IBA:GO_Central.
DR GO; GO:0005793; C:endoplasmic reticulum-Golgi intermediate compartment; IDA:UniProtKB.
DR GO; GO:0033116; C:endoplasmic reticulum-Golgi intermediate compartment membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005794; C:Golgi apparatus; IDA:UniProtKB.
DR GO; GO:0030173; C:integral component of Golgi membrane; IBA:GO_Central.
DR GO; GO:0006888; P:endoplasmic reticulum to Golgi vesicle-mediated transport; IMP:UniProtKB.
DR GO; GO:0006612; P:protein targeting to membrane; ISS:UniProtKB.
DR InterPro; IPR005578; Yif1_fam.
DR PANTHER; PTHR14083; PTHR14083; 1.
DR Pfam; PF03878; YIF1; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Disease variant; Endoplasmic reticulum;
KW Golgi apparatus; Intellectual disability; Membrane; Phosphoprotein;
KW Protein transport; Reference proteome; Transmembrane; Transmembrane helix;
KW Transport.
FT CHAIN 1..314
FT /note="Protein YIF1B"
FT /id="PRO_0000307258"
FT TOPO_DOM 1..156
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 157..177
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 178..192
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 193..213
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 214..219
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 220..240
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 241
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 242..262
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 263..292
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 293..313
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 314
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT REGION 1..55
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:Q9CX30"
FT MOD_RES 13
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9CX30"
FT MOD_RES 65
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332"
FT VAR_SEQ 1..31
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:12975309,
FT ECO:0000303|PubMed:15498874"
FT /id="VSP_028650"
FT VAR_SEQ 1..20
FT /note="MHPAGLAAAAAGTPRLRKWP -> MPGSA (in isoform 6)"
FT /evidence="ECO:0000305"
FT /id="VSP_046823"
FT VAR_SEQ 17..19
FT /note="Missing (in isoform 3, isoform 4 and isoform 5)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:17974005"
FT /id="VSP_028651"
FT VAR_SEQ 264..297
FT /note="IRTLRLKILADAAAEGVPVRGARNQLRMYLTMAV -> FPLLPGAVAHACNP
FT STLGGRGGRITRSGDQDHPG (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_028652"
FT VAR_SEQ 264..294
FT /note="IRTLRLKILADAAAEGVPVRGARNQLRMYLT -> FPLLPGAVAHACNPSTL
FT GGRGGRITRSGRCG (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:17974005"
FT /id="VSP_028653"
FT VAR_SEQ 295..314
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:17974005"
FT /id="VSP_028654"
FT VAR_SEQ 298..314
FT /note="Missing (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_028655"
FT VARIANT 56
FT /note="P -> S (in dbSNP:rs11556992)"
FT /id="VAR_035385"
FT VARIANT 123
FT /note="K -> Q (in KABAMAS; decreased protein abundance)"
FT /evidence="ECO:0000269|PubMed:33103737"
FT /id="VAR_085531"
FT VARIANT 200..314
FT /note="Missing (in KABAMAS; loss of expression)"
FT /evidence="ECO:0000269|PubMed:32006098,
FT ECO:0000269|PubMed:33103737"
FT /id="VAR_085532"
SQ SEQUENCE 314 AA; 34435 MW; 93A2521A3332D3AD CRC64;
MHPAGLAAAA AGTPRLRKWP SKRRIPVSQP GMADPHQLFD DTSSAQSRGY GAQRAPGGLS
YPAASPTPHA AFLADPVSNM AMAYGSSLAA QGKELVDKNI DRFIPITKLK YYFAVDTMYV
GRKLGLLFFP YLHQDWEVQY QQDTPVAPRF DVNAPDLYIP AMAFITYVLV AGLALGTQDR
FSPDLLGLQA SSALAWLTLE VLAILLSLYL VTVNTDLTTI DLVAFLGYKY VGMIGGVLMG
LLFGKIGYYL VLGWCCVAIF VFMIRTLRLK ILADAAAEGV PVRGARNQLR MYLTMAVAAA
QPMLMYWLTF HLVR
