ID PRR5_HUMAN Reviewed; 388 AA. AC P85299; B1AHF6; B1AHG5; B3KP73; O75983; O95695; Q5BIW2; Q5EAJ8; Q5EAJ9; AC Q5XKJ6; Q96RW1; Q96RW2; Q9HA49; Q9HC46; Q9NSG0; Q9NVX8; Q9NXL1; Q9UH20; DT 23-OCT-2007, integrated into UniProtKB/Swiss-Prot. DT 23-OCT-2007, sequence version 1. DT 24-JAN-2024, entry version 125. DE RecName: Full=Proline-rich protein 5; DE AltName: Full=Protein observed with Rictor-1; DE Short=Protor-1; GN Name=PRR5; Synonyms=PROTOR1; ORFNames=PP610; 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] (ISOFORMS 2 AND 5). RC TISSUE=Colon mucosa, and Kidney; 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 [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). 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 GENOMIC DNA]. RX PubMed=10591208; DOI=10.1038/990031; RA Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M., Clamp M., RA Smink L.J., Ainscough R., Almeida J.P., Babbage A.K., Bagguley C., RA Bailey J., Barlow K.F., Bates K.N., Beasley O.P., Bird C.P., Blakey S.E., RA Bridgeman A.M., Buck D., Burgess J., Burrill W.D., Burton J., Carder C., RA Carter N.P., Chen Y., Clark G., Clegg S.M., Cobley V.E., Cole C.G., RA Collier R.E., Connor R., Conroy D., Corby N.R., Coville G.J., Cox A.V., RA Davis J., Dawson E., Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M., RA Ellington A.G., Evans K.L., Fey J.M., Fleming K., French L., Garner A.A., RA Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C., RA Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S., Hunt S.E., RA Jones M.C., Kershaw J., Kimberley A.M., King A., Laird G.K., Langford C.F., RA Leversha M.A., Lloyd C., Lloyd D.M., Martyn I.D., Mashreghi-Mohammadi M., RA Matthews L.H., Mccann O.T., Mcclay J., Mclaren S., McMurray A.A., RA Milne S.A., Mortimore B.J., Odell C.N., Pavitt R., Pearce A.V., Pearson D., RA Phillimore B.J.C.T., Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y., RA Rogers L., Ross M.T., Scott C.E., Sehra H.K., Skuce C.D., Smalley S., RA Smith M.L., Soderlund C., Spragon L., Steward C.A., Sulston J.E., RA Swann R.M., Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L., RA Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L., RA Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N., RA Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J., Shintani A., RA Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S., Roe B.A., Chen F., Chu L., RA Crabtree J., Deschamps S., Do A., Do T., Dorman A., Fang F., Fu Y., Hu P., RA Hua A., Kenton S., Lai H., Lao H.I., Lewis J., Lewis S., Lin S.-P., Loh P., RA Malaj E., Nguyen T., Pan H., Phan S., Qi S., Qian Y., Ray L., Ren Q., RA Shaull S., Sloan D., Song L., Wang Q., Wang Y., Wang Z., White J., RA Willingham D., Wu H., Yao Z., Zhan M., Zhang G., Chissoe S., Murray J., RA Miller N., Minx P., Fulton R., Johnson D., Bemis G., Bentley D., RA Bradshaw H., Bourne S., Cordes M., Du Z., Fulton L., Goela D., Graves T., RA Hawkins J., Hinds K., Kemp K., Latreille P., Layman D., Ozersky P., RA Rohlfing T., Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K., RA Nelson J., Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R., RA Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S., Budarf M.L., RA McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E., Edelmann L., Kim U.J., RA Shizuya H., Simon M.I., Dumanski J.P., Peyrard M., Kedra D., Seroussi E., RA Fransson I., Tapia I., Bruder C.E., O'Brien K.P., Wilkinson P., RA Bodenteich A., Hartman K., Hu X., Khan A.S., Lane L., Tilahun Y., RA Wright H.; RT "The DNA sequence of human chromosome 22."; RL Nature 402:489-495(1999). 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 MRNA] (ISOFORM 2). RC TISSUE=Liver; 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 IDENTIFICATION (ISOFORMS 1; 3 AND 4), FUNCTION, AND TISSUE SPECIFICITY. RX PubMed=15718101; DOI=10.1016/j.ygeno.2004.11.002; RA Johnstone C.N., Castellvi-Bel S., Chang L.M., Sung R.K., Bowser M.J., RA Pique J.M., Castells A., Rustgi A.K.; RT "PRR5 encodes a conserved proline-rich protein predominant in kidney: RT analysis of genomic organization, expression, and mutation status in breast RT and colorectal carcinomas."; RL Genomics 85:338-351(2005). RN [7] RP IDENTIFICATION IN THE TORC2 COMPLEX, AND INTERACTION WITH RICTOR. RX PubMed=17461779; DOI=10.1042/bj20070540; RA Pearce L.R., Huang X., Boudeau J., Pawlowski R., Wullschleger S., Deak M., RA Ibrahim A.F.M., Gourlay R., Magnuson M.A., Alessi D.R.; RT "Identification of Protor as a novel Rictor-binding component of mTOR RT complex-2."; RL Biochem. J. 405:513-522(2007). RN [8] RP FUNCTION, IDENTIFICATION IN THE TORC2 COMPLEX, INTERACTION WITH MTOR AND RP RICTOR, AND TISSUE SPECIFICITY. RX PubMed=17599906; DOI=10.1074/jbc.m704343200; RA Woo S.-Y., Kim D.-H., Jun C.-B., Kim Y.-M., Haar E.V., Lee S.-I., RA Hegg J.W., Bandhakavi S., Griffin T.J., Kim D.-H.; RT "PRR5, a novel component of mTOR complex 2, regulates platelet-derived RT growth factor receptor beta expression and signaling."; RL J. Biol. Chem. 282:25604-25612(2007). RN [9] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=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 [10] 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: Subunit of mTORC2, which regulates cell growth and survival CC in response to hormonal signals. mTORC2 is activated by growth factors, CC but, in contrast to mTORC1, seems to be nutrient-insensitive. mTORC2 CC seems to function upstream of Rho GTPases to regulate the actin CC cytoskeleton, probably by activating one or more Rho-type guanine CC nucleotide exchange factors. mTORC2 promotes the serum-induced CC formation of stress-fibers or F-actin. mTORC2 plays a critical role in CC AKT1 'Ser-473' phosphorylation, which may facilitate the CC phosphorylation of the activation loop of AKT1 on 'Thr-308' by PDK1 CC which is a prerequisite for full activation. mTORC2 regulates the CC phosphorylation of SGK1 at 'Ser-422'. mTORC2 also modulates the CC phosphorylation of PRKCA on 'Ser-657'. PRR5 plays an important role in CC regulation of PDGFRB expression and in modulation of platelet-derived CC growth factor signaling. May act as a tumor suppressor in breast CC cancer. {ECO:0000269|PubMed:15718101, ECO:0000269|PubMed:17599906}. CC -!- SUBUNIT: Part of the mammalian target of rapamycin complex 2 (mTORC2) CC which contains MTOR, MLST8, PRR5, RICTOR, MAPKAP1 and DEPTOR. Contrary CC to mTORC1, mTORC2 does not bind to and is not sensitive to FKBP12- CC rapamycin. Binds directly to MTOR and RICTOR within the TORC2 complex. CC {ECO:0000269|PubMed:17461779, ECO:0000269|PubMed:17599906}. CC -!- INTERACTION: CC P85299; Q12959: DLG1; NbExp=2; IntAct=EBI-1387467, EBI-357481; CC P85299-2; Q9UI47-2: CTNNA3; NbExp=3; IntAct=EBI-12944296, EBI-11962928; CC P85299-2; Q6ICB0: DESI1; NbExp=3; IntAct=EBI-12944296, EBI-2806959; CC P85299-2; Q9Y4H4: GPSM3; NbExp=3; IntAct=EBI-12944296, EBI-347538; CC P85299-2; O14964: HGS; NbExp=3; IntAct=EBI-12944296, EBI-740220; CC P85299-2; Q8N6Y0: USHBP1; NbExp=3; IntAct=EBI-12944296, EBI-739895; CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=5; CC Name=1; Synonyms=alpha; CC IsoId=P85299-1, Q9NSG0-5; Sequence=Displayed; CC Name=2; CC IsoId=P85299-2, Q9NSG0-8; Sequence=VSP_001646, VSP_001648; CC Name=3; Synonyms=beta; CC IsoId=P85299-3; Sequence=VSP_028885; CC Name=4; Synonyms=gamma; CC IsoId=P85299-4; Sequence=VSP_028884; CC Name=5; CC IsoId=P85299-5; Sequence=VSP_045883; CC -!- TISSUE SPECIFICITY: Most abundant in kidney and liver. Also highly CC expressed in brain, spleen, testis and placenta. Overexpressed in CC several colorectal tumors. {ECO:0000269|PubMed:15718101, CC ECO:0000269|PubMed:17599906}. CC -!- SIMILARITY: Belongs to the PROTOR 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; AK000192; BAA90999.1; -; mRNA. DR EMBL; AK055848; BAG51585.1; -; mRNA. DR EMBL; AF177331; AAG17975.1; -; mRNA. DR EMBL; Z93244; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; Z98743; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471138; EAW73353.1; -; Genomic_DNA. DR EMBL; CH471138; EAW73355.1; -; Genomic_DNA. DR EMBL; BC016921; AAH16921.1; -; mRNA. DR EMBL; BK005635; DAA05654.1; -; mRNA. DR EMBL; BK005636; DAA05655.1; -; mRNA. DR EMBL; BK005637; DAA05656.1; -; mRNA. DR EMBL; BK005638; DAA05657.1; -; mRNA. DR EMBL; BK005639; DAA05658.1; -; mRNA. DR CCDS; CCDS14058.1; -. DR CCDS; CCDS14059.1; -. [P85299-3] DR CCDS; CCDS56232.1; -. [P85299-5] DR CCDS; CCDS74875.1; -. [P85299-4] DR RefSeq; NP_001017528.1; NM_001017528.2. [P85299-3] DR RefSeq; NP_001017529.1; NM_001017529.2. [P85299-4] DR RefSeq; NP_001017530.1; NM_001017530.1. [P85299-4] DR RefSeq; NP_001185650.1; NM_001198721.1. [P85299-5] DR RefSeq; NP_056181.2; NM_015366.3. [P85299-3] DR RefSeq; NP_851850.1; NM_181333.3. [P85299-1] DR AlphaFoldDB; P85299; -. DR SMR; P85299; -. DR BioGRID; 120755; 40. DR ComplexPortal; CPX-4402; mTORC2 complex. DR IntAct; P85299; 25. DR MINT; P85299; -. DR STRING; 9606.ENSP00000384848; -. DR GlyGen; P85299; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; P85299; -. DR PhosphoSitePlus; P85299; -. DR BioMuta; PRR5; -. DR DMDM; 160016058; -. DR EPD; P85299; -. DR jPOST; P85299; -. DR MassIVE; P85299; -. DR MaxQB; P85299; -. DR PaxDb; 9606-ENSP00000384848; -. DR PeptideAtlas; P85299; -. DR ProteomicsDB; 2938; -. DR ProteomicsDB; 57768; -. DR ProteomicsDB; 57769; -. [P85299-2] DR ProteomicsDB; 57770; -. [P85299-3] DR ProteomicsDB; 57771; -. [P85299-4] DR Antibodypedia; 46008; 210 antibodies from 30 providers. DR DNASU; 55615; -. DR Ensembl; ENST00000006251.11; ENSP00000006251.7; ENSG00000186654.21. [P85299-3] DR Ensembl; ENST00000336985.11; ENSP00000337464.6; ENSG00000186654.21. [P85299-1] DR Ensembl; ENST00000403581.5; ENSP00000384848.1; ENSG00000186654.21. [P85299-5] DR Ensembl; ENST00000611394.4; ENSP00000480357.1; ENSG00000186654.21. [P85299-3] DR Ensembl; ENST00000617066.4; ENSP00000479623.1; ENSG00000186654.21. [P85299-4] DR Ensembl; ENST00000624862.3; ENSP00000485597.1; ENSG00000186654.21. [P85299-4] DR GeneID; 55615; -. DR KEGG; hsa:55615; -. DR MANE-Select; ENST00000336985.11; ENSP00000337464.6; NM_181333.4; NP_851850.1. DR UCSC; uc003bew.2; human. DR AGR; HGNC:31682; -. DR CTD; 55615; -. DR DisGeNET; 55615; -. DR GeneCards; PRR5; -. DR HGNC; HGNC:31682; PRR5. DR HPA; ENSG00000186654; Low tissue specificity. DR MIM; 609406; gene. DR neXtProt; NX_P85299; -. DR OpenTargets; ENSG00000186654; -. DR PharmGKB; PA144596392; -. DR VEuPathDB; HostDB:ENSG00000186654; -. DR eggNOG; KOG4406; Eukaryota. DR GeneTree; ENSGT00530000063981; -. DR HOGENOM; CLU_046146_0_0_1; -. DR InParanoid; P85299; -. DR OMA; HSVCEMS; -. DR OrthoDB; 5385062at2759; -. DR PhylomeDB; P85299; -. DR TreeFam; TF314826; -. DR PathwayCommons; P85299; -. DR Reactome; R-HSA-1257604; PIP3 activates AKT signaling. DR Reactome; R-HSA-389357; CD28 dependent PI3K/Akt signaling. DR Reactome; R-HSA-5218920; VEGFR2 mediated vascular permeability. DR Reactome; R-HSA-5674400; Constitutive Signaling by AKT1 E17K in Cancer. DR Reactome; R-HSA-6804757; Regulation of TP53 Degradation. DR SignaLink; P85299; -. DR SIGNOR; P85299; -. DR BioGRID-ORCS; 55615; 12 hits in 1149 CRISPR screens. DR ChiTaRS; PRR5; human. DR GenomeRNAi; 55615; -. DR Pharos; P85299; Tbio. DR PRO; PR:P85299; -. DR Proteomes; UP000005640; Chromosome 22. DR RNAct; P85299; Protein. DR Bgee; ENSG00000186654; Expressed in spleen and 159 other cell types or tissues. DR ExpressionAtlas; P85299; baseline and differential. DR GO; GO:0005829; C:cytosol; TAS:Reactome. DR GO; GO:0031932; C:TORC2 complex; IDA:UniProtKB. DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW. DR GO; GO:0031669; P:cellular response to nutrient levels; NAS:ComplexPortal. DR GO; GO:0007010; P:cytoskeleton organization; NAS:ComplexPortal. DR GO; GO:0043066; P:negative regulation of apoptotic process; NAS:ComplexPortal. DR GO; GO:0043491; P:phosphatidylinositol 3-kinase/protein kinase B signal transduction; IEA:Ensembl. DR GO; GO:0030307; P:positive regulation of cell growth; NAS:ComplexPortal. DR GO; GO:0051897; P:positive regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction; IEA:Ensembl. DR GO; GO:0001934; P:positive regulation of protein phosphorylation; IEA:Ensembl. DR GO; GO:0038203; P:TORC2 signaling; IBA:GO_Central. DR InterPro; IPR013745; Bit61/PRR5. DR InterPro; IPR016159; Cullin_repeat-like_dom_sf. DR PANTHER; PTHR32428:SF4; PROLINE-RICH PROTEIN 5; 1. DR PANTHER; PTHR32428; TARGET OF RAPAMYCIN COMPLEX 2 SUBUNIT BIT61-RELATED; 1. DR Pfam; PF08539; HbrB; 1. DR SUPFAM; SSF74788; Cullin repeat-like; 1. DR Genevisible; P85299; HS. PE 1: Evidence at protein level; KW Alternative splicing; Cell cycle; Phosphoprotein; Reference proteome; KW Tumor suppressor. FT CHAIN 1..388 FT /note="Proline-rich protein 5" FT /id="PRO_0000308162" FT REGION 10..95 FT /note="Interaction with RICTOR" FT REGION 12..31 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 188..218 FT /note="Interaction with RICTOR" FT REGION 254..388 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 299..313 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 325..354 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 252 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q812A5" FT VAR_SEQ 1..101 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:14702039, FT ECO:0000303|PubMed:15489334" FT /id="VSP_001646" FT VAR_SEQ 1..95 FT /note="Missing (in isoform 4)" FT /evidence="ECO:0000305" FT /id="VSP_028884" FT VAR_SEQ 1..9 FT /note="Missing (in isoform 3)" FT /evidence="ECO:0000305" FT /id="VSP_028885" FT VAR_SEQ 1..5 FT /note="MRTLR -> MVCLELSQREAWGSGSPEKMPAQPEGLY (in isoform FT 5)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_045883" FT VAR_SEQ 102..107 FT /note="KIRFYE -> MAPMPT (in isoform 2)" FT /evidence="ECO:0000303|PubMed:14702039, FT ECO:0000303|PubMed:15489334" FT /id="VSP_001648" FT VARIANT 243 FT /note="V -> M (in dbSNP:rs36082900)" FT /id="VAR_062230" FT CONFLICT 280 FT /note="R -> W (in Ref. 1; BAA90999)" FT /evidence="ECO:0000305" SQ SEQUENCE 388 AA; 42753 MW; FA6B90495623EF3F CRC64; MRTLRRLKFM SSPSLSDLGK REPAAAADER GTQQRRACAN ATWNSIHNGV IAVFQRKGLP DQELFSLNEG VRQLLKTELG SFFTEYLQNQ LLTKGMVILR DKIRFYEGQK LLDSLAETWD FFFSDVLPML QAIFYPVQGK EPSVRQLALL HFRNAITLSV KLEDALARAH ARVPPAIVQM LLVLQGVHES RGVTEDYLRL ETLVQKVVSP YLGTYGLHSS EGPFTHSCIL EKRLLRRSRS GDVLAKNPVV RSKSYNTPLL NPVQEHEAEG AAAGGTSIRR HSVSEMTSCP EPQGFSDPPG QGPTGTFRSS PAPHSGPCPS RLYPTTQPPE QGLDPTRSSL PRSSPENLVD QILESVDSDS EGIFIDFGRG RGSGMSDLEG SGGRQSVV //