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 27-MAR-2024, entry version 132. DE RecName: Full=Protein YIF1B {ECO:0000305}; DE AltName: Full=YIP1-interacting factor homolog B; GN Name=YIF1B {ECO:0000312|HGNC:HGNC:30511}; GN 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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. DR RefSeq; XP_016882938.1; XM_017027449.1. DR AlphaFoldDB; Q5BJH7; -. DR BioGRID; 124728; 97. DR IntAct; Q5BJH7; 22. DR MINT; Q5BJH7; -. DR STRING; 9606.ENSP00000343435; -. DR GlyCosmos; Q5BJH7; 1 site, 1 glycan. DR GlyGen; Q5BJH7; 4 sites, 1 O-linked glycan (4 sites). DR iPTMnet; Q5BJH7; -. DR PhosphoSitePlus; Q5BJH7; -. DR SwissPalm; Q5BJH7; -. DR BioMuta; YIF1B; -. DR DMDM; 121944384; -. DR EPD; Q5BJH7; -. DR jPOST; Q5BJH7; -. DR MassIVE; Q5BJH7; -. DR MaxQB; Q5BJH7; -. DR PaxDb; 9606-ENSP00000343435; -. DR PeptideAtlas; 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 Pumba; Q5BJH7; -. DR Antibodypedia; 30011; 135 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 AGR; HGNC:30511; -. 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 Orphanet; 88616; Autosomal recessive non-syndromic intellectual disability. DR PharmGKB; PA142670561; -. DR VEuPathDB; HostDB:ENSG00000167645; -. DR eggNOG; KOG3094; Eukaryota. DR GeneTree; ENSGT00390000009423; -. DR InParanoid; Q5BJH7; -. DR OMA; SGYKFVH; -. DR OrthoDB; 149453at2759; -. DR PhylomeDB; Q5BJH7; -. DR TreeFam; TF314528; -. DR PathwayCommons; Q5BJH7; -. DR SignaLink; Q5BJH7; -. DR SIGNOR; Q5BJH7; -. DR BioGRID-ORCS; 90522; 10 hits in 1157 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 169 other cell types or tissues. DR ExpressionAtlas; Q5BJH7; baseline and differential. 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:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell. 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 GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW. DR InterPro; IPR005578; Yif1_fam. DR PANTHER; PTHR14083:SF1; PROTEIN YIF1B; 1. DR PANTHER; PTHR14083; YIP1 INTERACTING FACTOR HOMOLOG YIF1 PROTEIN; 1. DR Pfam; PF03878; YIF1; 1. DR Genevisible; Q5BJH7; HS. 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 dbSNP:rs1969205627)" 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 //