ID   E41L5_HUMAN             Reviewed;         733 AA.
AC   Q9HCM4; Q7Z5S1; Q8IZ12; Q9H975;
DT   11-JUL-2001, integrated into UniProtKB/Swiss-Prot.
DT   29-APR-2008, sequence version 3.
DT   27-MAR-2024, entry version 181.
DE   RecName: Full=Band 4.1-like protein 5;
DE   AltName: Full=Erythrocyte membrane protein band 4.1-like 5 {ECO:0000312|HGNC:HGNC:19819};
GN   Name=EPB41L5; Synonyms=KIAA1548;
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 4), AND VARIANT
RP   THR-462.
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 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   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC   TISSUE=Retinoblastoma, and Testis;
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   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 188-732 (ISOFORM 3), AND VARIANT
RP   THR-462.
RC   TISSUE=Brain;
RX   PubMed=10997877; DOI=10.1093/dnares/7.4.271;
RA   Nagase T., Kikuno R., Nakayama M., Hirosawa M., Ohara O.;
RT   "Prediction of the coding sequences of unidentified human genes. XVIII. The
RT   complete sequences of 100 new cDNA clones from brain which code for large
RT   proteins in vitro.";
RL   DNA Res. 7:273-281(2000).
RN   [5]
RP   FUNCTION, IDENTIFICATION IN A COMPLEX WITH CRB1 AND PALS1, AND INTERACTION
RP   WITH PALS1; CRB1; CRB2 AND CRB3.
RX   PubMed=17920587; DOI=10.1016/j.yexcr.2007.08.025;
RA   Gosens I., Sessa A., den Hollander A.I., Letteboer S.J.F., Belloni V.,
RA   Arends M.L., Le Bivic A., Cremers F.P.M., Broccoli V., Roepman R.;
RT   "FERM protein EPB41L5 is a novel member of the mammalian CRB-MPP5 polarity
RT   complex.";
RL   Exp. Cell Res. 313:3959-3970(2007).
RN   [6]
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   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-436, 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   [8]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA   Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA   Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT   "System-wide temporal characterization of the proteome and phosphoproteome
RT   of human embryonic stem cell differentiation.";
RL   Sci. Signal. 4:RS3-RS3(2011).
RN   [9]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-517, AND IDENTIFICATION BY
RP   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   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-39, AND IDENTIFICATION BY
RP   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 formation and organization of tight
CC       junctions during the establishment of polarity in epithelial cells.
CC       {ECO:0000269|PubMed:17920587}.
CC   -!- SUBUNIT: Component of a complex composed of PALS1, CRB1 and EPB41L5
CC       (PubMed:17920587). Within the complex, interacts (via FERM domain) with
CC       PALS1 (via HOOK domain) and with CRB1 (via intracellular domain)
CC       (PubMed:17920587). Interacts with CRB2 (via intracellular domain)
CC       (PubMed:17920587). Interacts with CRB3 (via intracellular domain)
CC       (PubMed:17920587). {ECO:0000269|PubMed:17920587}.
CC   -!- INTERACTION:
CC       Q9HCM4; P82279: CRB1; NbExp=4; IntAct=EBI-1047162, EBI-1048648;
CC       Q9HCM4; Q9BUF7: CRB3; NbExp=3; IntAct=EBI-1047162, EBI-9844372;
CC       Q9HCM4; Q8N3R9: PALS1; NbExp=4; IntAct=EBI-1047162, EBI-2513978;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q8BGS1}. Cell
CC       junction, adherens junction {ECO:0000250|UniProtKB:Q8BGS1}. Cell
CC       membrane {ECO:0000250|UniProtKB:Q8BGS1}; Peripheral membrane protein
CC       {ECO:0000305}. Photoreceptor inner segment
CC       {ECO:0000250|UniProtKB:Q5FVG2}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=4;
CC       Name=1;
CC         IsoId=Q9HCM4-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q9HCM4-2; Sequence=VSP_033034, VSP_033035;
CC       Name=3;
CC         IsoId=Q9HCM4-3; Sequence=VSP_033036;
CC       Name=4;
CC         IsoId=Q9HCM4-4; Sequence=VSP_033037, VSP_033038;
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DR   EMBL; AK023019; BAB14360.1; -; mRNA.
DR   EMBL; AK290895; BAF83584.1; -; mRNA.
DR   EMBL; CH471103; EAW95234.1; -; Genomic_DNA.
DR   EMBL; BC032822; AAH32822.1; -; mRNA.
DR   EMBL; BC054508; AAH54508.1; -; mRNA.
DR   EMBL; AB046768; BAB13374.1; -; mRNA.
DR   CCDS; CCDS2130.1; -. [Q9HCM4-1]
DR   CCDS; CCDS54392.1; -. [Q9HCM4-2]
DR   CCDS; CCDS54393.1; -. [Q9HCM4-4]
DR   CCDS; CCDS82506.1; -. [Q9HCM4-3]
DR   RefSeq; NP_001171866.1; NM_001184937.1. [Q9HCM4-4]
DR   RefSeq; NP_001171867.1; NM_001184938.3. [Q9HCM4-2]
DR   RefSeq; NP_001171868.1; NM_001184939.2. [Q9HCM4-2]
DR   RefSeq; NP_001317239.1; NM_001330310.1. [Q9HCM4-3]
DR   RefSeq; NP_065960.2; NM_020909.3. [Q9HCM4-1]
DR   AlphaFoldDB; Q9HCM4; -.
DR   SMR; Q9HCM4; -.
DR   BioGRID; 121701; 369.
DR   IntAct; Q9HCM4; 82.
DR   MINT; Q9HCM4; -.
DR   STRING; 9606.ENSP00000263713; -.
DR   iPTMnet; Q9HCM4; -.
DR   PhosphoSitePlus; Q9HCM4; -.
DR   SwissPalm; Q9HCM4; -.
DR   BioMuta; EPB41L5; -.
DR   DMDM; 187608883; -.
DR   EPD; Q9HCM4; -.
DR   jPOST; Q9HCM4; -.
DR   MassIVE; Q9HCM4; -.
DR   MaxQB; Q9HCM4; -.
DR   PaxDb; 9606-ENSP00000263713; -.
DR   PeptideAtlas; Q9HCM4; -.
DR   ProteomicsDB; 81763; -. [Q9HCM4-1]
DR   ProteomicsDB; 81764; -. [Q9HCM4-2]
DR   ProteomicsDB; 81765; -. [Q9HCM4-3]
DR   ProteomicsDB; 81766; -. [Q9HCM4-4]
DR   Pumba; Q9HCM4; -.
DR   Antibodypedia; 33383; 159 antibodies from 27 providers.
DR   DNASU; 57669; -.
DR   Ensembl; ENST00000263713.10; ENSP00000263713.5; ENSG00000115109.14. [Q9HCM4-1]
DR   Ensembl; ENST00000331393.8; ENSP00000329687.4; ENSG00000115109.14. [Q9HCM4-2]
DR   Ensembl; ENST00000443124.5; ENSP00000393722.1; ENSG00000115109.14. [Q9HCM4-2]
DR   Ensembl; ENST00000443902.6; ENSP00000393856.2; ENSG00000115109.14. [Q9HCM4-4]
DR   Ensembl; ENST00000452780.1; ENSP00000390439.1; ENSG00000115109.14. [Q9HCM4-3]
DR   GeneID; 57669; -.
DR   KEGG; hsa:57669; -.
DR   MANE-Select; ENST00000263713.10; ENSP00000263713.5; NM_020909.4; NP_065960.2.
DR   UCSC; uc002tmg.4; human. [Q9HCM4-1]
DR   AGR; HGNC:19819; -.
DR   CTD; 57669; -.
DR   DisGeNET; 57669; -.
DR   GeneCards; EPB41L5; -.
DR   HGNC; HGNC:19819; EPB41L5.
DR   HPA; ENSG00000115109; Low tissue specificity.
DR   MIM; 611730; gene.
DR   neXtProt; NX_Q9HCM4; -.
DR   OpenTargets; ENSG00000115109; -.
DR   PharmGKB; PA134862834; -.
DR   VEuPathDB; HostDB:ENSG00000115109; -.
DR   eggNOG; KOG3530; Eukaryota.
DR   GeneTree; ENSGT00940000156332; -.
DR   HOGENOM; CLU_003623_5_1_1; -.
DR   InParanoid; Q9HCM4; -.
DR   OMA; WPPDAAG; -.
DR   OrthoDB; 3682543at2759; -.
DR   PhylomeDB; Q9HCM4; -.
DR   TreeFam; TF319780; -.
DR   PathwayCommons; Q9HCM4; -.
DR   Reactome; R-HSA-6794361; Neurexins and neuroligins.
DR   SignaLink; Q9HCM4; -.
DR   BioGRID-ORCS; 57669; 18 hits in 1160 CRISPR screens.
DR   ChiTaRS; EPB41L5; human.
DR   GeneWiki; EPB41L5; -.
DR   GenomeRNAi; 57669; -.
DR   Pharos; Q9HCM4; Tbio.
DR   PRO; PR:Q9HCM4; -.
DR   Proteomes; UP000005640; Chromosome 2.
DR   RNAct; Q9HCM4; Protein.
DR   Bgee; ENSG00000115109; Expressed in oocyte and 166 other cell types or tissues.
DR   GO; GO:0005912; C:adherens junction; IEA:UniProtKB-SubCell.
DR   GO; GO:0005856; C:cytoskeleton; IBA:GO_Central.
DR   GO; GO:0005829; C:cytosol; IDA:HPA.
DR   GO; GO:0005925; C:focal adhesion; IEA:Ensembl.
DR   GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR   GO; GO:0001917; C:photoreceptor inner segment; IEA:UniProtKB-SubCell.
DR   GO; GO:0005886; C:plasma membrane; IDA:HPA.
DR   GO; GO:0032587; C:ruffle membrane; IEA:Ensembl.
DR   GO; GO:0008092; F:cytoskeletal protein binding; IEA:InterPro.
DR   GO; GO:0019904; F:protein domain specific binding; IEA:Ensembl.
DR   GO; GO:0031032; P:actomyosin structure organization; IBA:GO_Central.
DR   GO; GO:0003383; P:apical constriction; IEA:Ensembl.
DR   GO; GO:0048319; P:axial mesoderm morphogenesis; IEA:Ensembl.
DR   GO; GO:0071560; P:cellular response to transforming growth factor beta stimulus; IEA:Ensembl.
DR   GO; GO:0007398; P:ectoderm development; IEA:Ensembl.
DR   GO; GO:0048617; P:embryonic foregut morphogenesis; IEA:Ensembl.
DR   GO; GO:0007492; P:endoderm development; IEA:Ensembl.
DR   GO; GO:0001837; P:epithelial to mesenchymal transition; IEA:Ensembl.
DR   GO; GO:0001701; P:in utero embryonic development; IEA:Ensembl.
DR   GO; GO:0070986; P:left/right axis specification; IEA:Ensembl.
DR   GO; GO:0007509; P:mesoderm migration involved in gastrulation; IEA:Ensembl.
DR   GO; GO:0022408; P:negative regulation of cell-cell adhesion; IEA:Ensembl.
DR   GO; GO:0001839; P:neural plate morphogenesis; IEA:Ensembl.
DR   GO; GO:0048339; P:paraxial mesoderm development; IEA:Ensembl.
DR   GO; GO:0010634; P:positive regulation of epithelial cell migration; IEA:Ensembl.
DR   GO; GO:0051894; P:positive regulation of focal adhesion assembly; IEA:Ensembl.
DR   GO; GO:0010608; P:post-transcriptional regulation of gene expression; IEA:Ensembl.
DR   GO; GO:0070201; P:regulation of establishment of protein localization; IEA:Ensembl.
DR   GO; GO:0032525; P:somite rostral/caudal axis specification; IEA:Ensembl.
DR   GO; GO:0006931; P:substrate-dependent cell migration, cell attachment to substrate; IEA:Ensembl.
DR   GO; GO:0009826; P:unidimensional cell growth; IEA:Ensembl.
DR   CDD; cd14473; FERM_B-lobe; 1.
DR   CDD; cd13186; FERM_C_NBL4_NBL5; 1.
DR   CDD; cd17205; FERM_F1_EPB41L5; 1.
DR   Gene3D; 1.20.80.10; -; 1.
DR   Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1.
DR   InterPro; IPR019749; Band_41_domain.
DR   InterPro; IPR000798; Ez/rad/moesin-like.
DR   InterPro; IPR014847; FA.
DR   InterPro; IPR014352; FERM/acyl-CoA-bd_prot_sf.
DR   InterPro; IPR035963; FERM_2.
DR   InterPro; IPR019748; FERM_central.
DR   InterPro; IPR019747; FERM_CS.
DR   InterPro; IPR000299; FERM_domain.
DR   InterPro; IPR018979; FERM_N.
DR   InterPro; IPR018980; FERM_PH-like_C.
DR   InterPro; IPR011993; PH-like_dom_sf.
DR   InterPro; IPR029071; Ubiquitin-like_domsf.
DR   PANTHER; PTHR23280; 4.1 G PROTEIN; 1.
DR   PANTHER; PTHR23280:SF15; BAND 4.1-LIKE PROTEIN 5; 1.
DR   Pfam; PF08736; FA; 1.
DR   Pfam; PF09380; FERM_C; 1.
DR   Pfam; PF00373; FERM_M; 1.
DR   Pfam; PF09379; FERM_N; 1.
DR   PRINTS; PR00935; BAND41.
DR   PRINTS; PR00661; ERMFAMILY.
DR   SMART; SM00295; B41; 1.
DR   SMART; SM01195; FA; 1.
DR   SMART; SM01196; FERM_C; 1.
DR   SUPFAM; SSF50729; PH domain-like; 1.
DR   SUPFAM; SSF47031; Second domain of FERM; 1.
DR   SUPFAM; SSF54236; Ubiquitin-like; 1.
DR   PROSITE; PS00660; FERM_1; 1.
DR   PROSITE; PS00661; FERM_2; 1.
DR   PROSITE; PS50057; FERM_3; 1.
DR   Genevisible; Q9HCM4; HS.
PE   1: Evidence at protein level;
KW   Alternative splicing; Cell junction; Cell membrane; Cytoplasm; Membrane;
KW   Phosphoprotein; Reference proteome.
FT   CHAIN           1..733
FT                   /note="Band 4.1-like protein 5"
FT                   /id="PRO_0000219406"
FT   DOMAIN          43..327
FT                   /note="FERM"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00084"
FT   REGION          29..119
FT                   /note="Required for interaction with CRB1"
FT                   /evidence="ECO:0000269|PubMed:17920587"
FT   MOD_RES         39
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:24275569"
FT   MOD_RES         436
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:19690332"
FT   MOD_RES         517
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   VAR_SEQ         446..505
FT                   /note="CIPLNIDLLNSPDLLEATIGDVIGASDTMETSQALNDVNVATRLPGLGEPEV
FT                   EYETLKDT -> WLSAASDCCQRGGNQWNTRALPPPQTAHRNYTDFVHEHNVKNAGIRH
FT                   DVHFPGHTAMTEI (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:14702039,
FT                   ECO:0000303|PubMed:15489334"
FT                   /id="VSP_033034"
FT   VAR_SEQ         506..733
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:14702039,
FT                   ECO:0000303|PubMed:15489334"
FT                   /id="VSP_033035"
FT   VAR_SEQ         668..669
FT                   /note="PQ -> P (in isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:10997877"
FT                   /id="VSP_033036"
FT   VAR_SEQ         669..687
FT                   /note="QSGAMSNGLAGCEMLLTGK -> LWSHFGRRSCPEAEVFTDH (in
FT                   isoform 4)"
FT                   /evidence="ECO:0000303|PubMed:14702039"
FT                   /id="VSP_033037"
FT   VAR_SEQ         688..733
FT                   /note="Missing (in isoform 4)"
FT                   /evidence="ECO:0000303|PubMed:14702039"
FT                   /id="VSP_033038"
FT   VARIANT         334
FT                   /note="H -> Y (in dbSNP:rs28930677)"
FT                   /id="VAR_048357"
FT   VARIANT         462
FT                   /note="A -> T (in dbSNP:rs1034489)"
FT                   /evidence="ECO:0000269|PubMed:10997877,
FT                   ECO:0000269|PubMed:14702039"
FT                   /id="VAR_042699"
SQ   SEQUENCE   733 AA;  81856 MW;  A3712B5927C9C199 CRC64;
     MLSFFRRTLG RRSMRKHAEK ERLREAQRAA THIPAAGDSK SIITCRVSLL DGTDVSVDLP
     KKAKGQELFD QIMYHLDLIE SDYFGLRFMD SAQVAHWLDG TKSIKKQVKI GSPYCLHLRV
     KFYSSEPNNL REELTRYLFV LQLKQDILSG KLDCPFDTAV QLAAYNLQAE LGDYDLAEHS
     PELVSEFRFV PIQTEEMELA IFEKWKEYRG QTPAQAETNY LNKAKWLEMY GVDMHVVKAR
     DGNDYSLGLT PTGVLVFEGD TKIGLFFWPK ITRLDFKKNK LTLVVVEDDD QGKEQEHTFV
     FRLDHPKACK HLWKCAVEHH AFFRLRGPVQ KSSHRSGFIR LGSRFRYSGK TEYQTTKTNK
     ARRSTSFERR PSKRYSRRTL QMKACATKPE ELSVHNNVST QSNGSQQAWG MRSALPVSPS
     ISSAPVPVEI ENLPQSPGTD QHDRKCIPLN IDLLNSPDLL EATIGDVIGA SDTMETSQAL
     NDVNVATRLP GLGEPEVEYE TLKDTSEKLK QLEMENSPLL SPRSNIDVNI NSQEEVVKLT
     EKCLNNVIES PGLNVMRVPP DFKSNILKAQ VEAVHKVTKE DSLLSHKNAN VQDAATNSAV
     LNENNVPLPK ESLETLMLIT PADSGSVLKE ATDELDALLA SLTENLIDHT VAPQVSSTSM
     ITPRWIVPQS GAMSNGLAGC EMLLTGKEGH GNKDGISLIS PPAPFLVDAV TSSGPILAEE
     AVLKQKCLLT TEL
//