HECAM_HUMAN
ID HECAM_HUMAN Reviewed; 416 AA.
AC Q14CZ8; Q67IP8; Q6ZWL4; Q8N7I3; Q8ND35;
DT 21-AUG-2007, integrated into UniProtKB/Swiss-Prot.
DT 22-AUG-2006, sequence version 1.
DT 03-AUG-2022, entry version 131.
DE RecName: Full=Hepatocyte cell adhesion molecule;
DE Short=Protein hepaCAM;
DE Flags: Precursor;
GN Name=HEPACAM {ECO:0000312|EMBL:AAI13563.1};
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] {ECO:0000305, ECO:0000312|EMBL:AAQ93018.1}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, SUBCELLULAR LOCATION,
RP INDUCTION, AND GLYCOSYLATION.
RC TISSUE=Liver {ECO:0000312|EMBL:AAQ93018.1};
RX PubMed=15885354; DOI=10.1016/j.jhep.2005.01.025;
RA Moh M.C., Lee L.H., Shen S.;
RT "Cloning and characterization of hepaCAM, a novel Ig-like cell adhesion
RT molecule suppressed in human hepatocellular carcinoma.";
RL J. Hepatol. 42:833-841(2005).
RN [2] {ECO:0000305, ECO:0000312|EMBL:BAC05297.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2), AND VARIANT
RP VAL-218.
RC TISSUE=Brain {ECO:0000312|EMBL:BAC05297.1};
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 [3] {ECO:0000305, ECO:0000312|EMBL:AAI13563.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT VAL-218.
RC TISSUE=Brain {ECO:0000312|EMBL:AAI13563.1};
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 251-416 (ISOFORM 1).
RC TISSUE=Fetal brain;
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 [5] {ECO:0000305}
RP FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, TOPOLOGY, DOMAIN, GLYCOSYLATION,
RP AND PHOSPHORYLATION.
RX PubMed=15917256; DOI=10.1074/jbc.m500852200;
RA Moh M.C., Zhang C., Luo C., Lee L.H., Shen S.;
RT "Structural and functional analyses of a novel Ig-like cell adhesion
RT molecule, hepaCAM, in the human breast carcinoma MCF7 cells.";
RL J. Biol. Chem. 280:27366-27374(2005).
RN [6]
RP SUBUNIT.
RX PubMed=22328087; DOI=10.1093/hmg/dds032;
RA Lanciotti A., Brignone M.S., Molinari P., Visentin S., De Nuccio C.,
RA Macchia G., Aiello C., Bertini E., Aloisi F., Petrucci T.C., Ambrosini E.;
RT "Megalencephalic leukoencephalopathy with subcortical cysts protein 1
RT functionally cooperates with the TRPV4 cation channel to activate the
RT response of astrocytes to osmotic stress: dysregulation by pathological
RT mutations.";
RL Hum. Mol. Genet. 21:2166-2180(2012).
RN [7]
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).
RN [8]
RP VARIANTS MLC2A HIS-23; GLN-92; CYS-98; SER-148; TYR-196 AND ASN-211, AND
RP VARIANTS MLC2B ASP-89; SER-89; TRP-92; ASN-128; LYS-135 DEL AND CYS-288.
RX PubMed=21419380; DOI=10.1016/j.ajhg.2011.02.009;
RA Lopez-Hernandez T., Ridder M.C., Montolio M., Capdevila-Nortes X.,
RA Polder E., Sirisi S., Duarri A., Schulte U., Fakler B., Nunes V.,
RA Scheper G.C., Martinez A., Estevez R., van der Knaap M.S.;
RT "Mutant GlialCAM causes megalencephalic leukoencephalopathy with
RT subcortical cysts, benign familial macrocephaly, and macrocephaly with
RT retardation and autism.";
RL Am. J. Hum. Genet. 88:422-432(2011).
CC -!- FUNCTION: Involved in regulating cell motility and cell-matrix
CC interactions. May inhibit cell growth through suppression of cell
CC proliferation. {ECO:0000269|PubMed:15885354,
CC ECO:0000269|PubMed:15917256}.
CC -!- SUBUNIT: Homodimer. Dimer formation occurs predominantly through cis
CC interactions on the cell surface. Part of a complex containing MLC1,
CC TRPV4, AQP4 and ATP1B1. {ECO:0000269|PubMed:15917256,
CC ECO:0000269|PubMed:22328087}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:15885354,
CC ECO:0000269|PubMed:15917256}. Membrane; Single-pass type I membrane
CC protein; Cytoplasmic side {ECO:0000269|PubMed:15885354,
CC ECO:0000269|PubMed:15917256}. Note=In MCF-7 breast carcinoma and
CC hepatic Hep 3B2.1-7 and Hep-G2 cell lines, localization of HEPACAM is
CC cell density-dependent. In well spread cells, localized to punctate
CC structures in the perinuclear membrane, cytoplasm, and at cell surface
CC of protusions. In confluent cells, localized predominantly to the
CC cytoplasmic membrane, particularly in areas of cell-cell contacts.
CC Colocalizes with CDH1.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1 {ECO:0000269|PubMed:15885354};
CC IsoId=Q14CZ8-1; Sequence=Displayed;
CC Name=2 {ECO:0000269|PubMed:14702039};
CC IsoId=Q14CZ8-2; Sequence=VSP_052497, VSP_052498;
CC -!- INDUCTION: Down-regulated in 20 out of 23 of hepatocellular carcinoma
CC (HCC) samples and is undetectable in 5 HCC cell lines tested.
CC {ECO:0000269|PubMed:15885354}.
CC -!- DOMAIN: The cytoplasmic domain plays an important role in regulation of
CC cell-matrix adhesion and cell motility. {ECO:0000269|PubMed:15917256}.
CC -!- PTM: N-glycosylated. {ECO:0000269|PubMed:15885354,
CC ECO:0000269|PubMed:15917256}.
CC -!- DISEASE: Leukoencephalopathy, megalencephalic, with subcortical cysts,
CC 2A (MLC2A) [MIM:613925]: A neurodegenerative disorder characterized by
CC infantile-onset macrocephaly and later onset of motor deterioration,
CC with ataxia and spasticity, seizures, and cognitive decline of variable
CC severity. The brain appears swollen on magnetic resonance imaging with
CC white-matter abnormalities and subcortical cysts, in all stages of the
CC disease. {ECO:0000269|PubMed:21419380}. Note=The disease is caused by
CC variants affecting the gene represented in this entry.
CC -!- DISEASE: Leukoencephalopathy, megalencephalic, with subcortical cysts,
CC 2B (MLC2B) [MIM:613926]: A neurodegenerative disorder characterized by
CC infantile-onset of macrocephaly and mildly delayed motor development
CC associated with white-matter abnormalities on brain magnetic resonance
CC imaging. The phenotype is milder that MLC2A, with better preserved
CC cerebellar white matter and no subcortical cysts outside the temporal
CC region. On follow-up, patients show normal or almost normal motor
CC function. Some patients have normal intelligence, whereas others have a
CC significant cognitive deficiency. {ECO:0000269|PubMed:21419380}.
CC Note=The disease is caused by variants affecting the gene represented
CC in this entry.
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; AY047587; AAQ93018.1; -; mRNA.
DR EMBL; AK098396; BAC05297.1; -; mRNA.
DR EMBL; AK122595; BAC85486.1; -; mRNA.
DR EMBL; BC104831; AAI04832.1; -; mRNA.
DR EMBL; BC113562; AAI13563.1; -; mRNA.
DR EMBL; AL834419; CAD39081.1; -; mRNA.
DR CCDS; CCDS8456.1; -. [Q14CZ8-1]
DR RefSeq; NP_689935.2; NM_152722.4. [Q14CZ8-1]
DR AlphaFoldDB; Q14CZ8; -.
DR SMR; Q14CZ8; -.
DR BioGRID; 128639; 2.
DR CORUM; Q14CZ8; -.
DR IntAct; Q14CZ8; 1.
DR STRING; 9606.ENSP00000298251; -.
DR TCDB; 8.A.23.1.5; the basigin (basigin) family.
DR GlyGen; Q14CZ8; 5 sites, 1 O-linked glycan (1 site).
DR iPTMnet; Q14CZ8; -.
DR PhosphoSitePlus; Q14CZ8; -.
DR BioMuta; HEPACAM; -.
DR DMDM; 121945515; -.
DR jPOST; Q14CZ8; -.
DR MassIVE; Q14CZ8; -.
DR MaxQB; Q14CZ8; -.
DR PaxDb; Q14CZ8; -.
DR PeptideAtlas; Q14CZ8; -.
DR PRIDE; Q14CZ8; -.
DR ProteomicsDB; 60339; -. [Q14CZ8-1]
DR ProteomicsDB; 60340; -. [Q14CZ8-2]
DR Antibodypedia; 2574; 200 antibodies from 30 providers.
DR DNASU; 220296; -.
DR Ensembl; ENST00000298251.5; ENSP00000298251.4; ENSG00000165478.7. [Q14CZ8-1]
DR GeneID; 220296; -.
DR KEGG; hsa:220296; -.
DR MANE-Select; ENST00000298251.5; ENSP00000298251.4; NM_152722.5; NP_689935.2.
DR UCSC; uc001qbk.4; human. [Q14CZ8-1]
DR CTD; 220296; -.
DR DisGeNET; 220296; -.
DR GeneCards; HEPACAM; -.
DR GeneReviews; HEPACAM; -.
DR HGNC; HGNC:26361; HEPACAM.
DR HPA; ENSG00000165478; Group enriched (brain, choroid plexus).
DR MalaCards; HEPACAM; -.
DR MIM; 611642; gene.
DR MIM; 613925; phenotype.
DR MIM; 613926; phenotype.
DR neXtProt; NX_Q14CZ8; -.
DR OpenTargets; ENSG00000165478; -.
DR Orphanet; 210548; Macrocephaly-intellectual disability-autism syndrome.
DR Orphanet; 2478; Megalencephalic leukoencephalopathy with subcortical cysts.
DR PharmGKB; PA162390830; -.
DR VEuPathDB; HostDB:ENSG00000165478; -.
DR eggNOG; ENOG502QPJB; Eukaryota.
DR GeneTree; ENSGT01010000222242; -.
DR HOGENOM; CLU_058570_1_0_1; -.
DR InParanoid; Q14CZ8; -.
DR OMA; DRKNPMA; -.
DR PhylomeDB; Q14CZ8; -.
DR TreeFam; TF331199; -.
DR PathwayCommons; Q14CZ8; -.
DR SignaLink; Q14CZ8; -.
DR BioGRID-ORCS; 220296; 11 hits in 1073 CRISPR screens.
DR ChiTaRS; HEPACAM; human.
DR GenomeRNAi; 220296; -.
DR Pharos; Q14CZ8; Tbio.
DR PRO; PR:Q14CZ8; -.
DR Proteomes; UP000005640; Chromosome 11.
DR RNAct; Q14CZ8; protein.
DR Bgee; ENSG00000165478; Expressed in lateral globus pallidus and 127 other tissues.
DR Genevisible; Q14CZ8; HS.
DR GO; GO:0030424; C:axon; IDA:MGI.
DR GO; GO:0005911; C:cell-cell junction; IDA:MGI.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0008104; P:protein localization; IEA:Ensembl.
DR GO; GO:0040008; P:regulation of growth; IEA:UniProtKB-KW.
DR Gene3D; 2.60.40.10; -; 2.
DR InterPro; IPR007110; Ig-like_dom.
DR InterPro; IPR036179; Ig-like_dom_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR003599; Ig_sub.
DR InterPro; IPR003598; Ig_sub2.
DR InterPro; IPR013106; Ig_V-set.
DR Pfam; PF07686; V-set; 1.
DR SMART; SM00409; IG; 2.
DR SMART; SM00408; IGc2; 1.
DR SUPFAM; SSF48726; SSF48726; 2.
DR PROSITE; PS50835; IG_LIKE; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell adhesion; Cell cycle; Cytoplasm;
KW Disease variant; Disulfide bond; Glycoprotein; Growth arrest;
KW Growth regulation; Immunoglobulin domain; Membrane; Phosphoprotein;
KW Reference proteome; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..33
FT /evidence="ECO:0000255"
FT CHAIN 34..416
FT /note="Hepatocyte cell adhesion molecule"
FT /evidence="ECO:0000255"
FT /id="PRO_0000298777"
FT TOPO_DOM 34..240
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 241..261
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 262..416
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 34..142
FT /note="Ig-like V-type"
FT /evidence="ECO:0000255"
FT DOMAIN 148..234
FT /note="Ig-like C2-type"
FT /evidence="ECO:0000255"
FT REGION 273..416
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 273..301
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 308..324
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 330..344
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 369..395
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 278
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q640R3"
FT MOD_RES 350
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q640R3"
FT MOD_RES 377
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q640R3"
FT CARBOHYD 35
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 138
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 167
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 189
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 168..217
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT VAR_SEQ 293..367
FT /note="ADTLPRSGEQERKNPMALYILKDKDSPETEENPAPEPRSATEPGPPGYSVSP
FT AVPGRSPGLPIRSARRYPRSPAR -> GELPATQSPIPSTIRSVGCWEKAELGDKENSS
FT AGTLPSDLGASKGKEPEPASLASSHSLPRRHAMPSTLSVSVHE (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_052497"
FT VAR_SEQ 368..416
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_052498"
FT VARIANT 23
FT /note="L -> H (in MLC2A)"
FT /evidence="ECO:0000269|PubMed:21419380"
FT /id="VAR_065849"
FT VARIANT 89
FT /note="G -> D (in MLC2B; dbSNP:rs387907054)"
FT /evidence="ECO:0000269|PubMed:21419380"
FT /id="VAR_065850"
FT VARIANT 89
FT /note="G -> S (in MLC2B; dbSNP:rs387907053)"
FT /evidence="ECO:0000269|PubMed:21419380"
FT /id="VAR_065851"
FT VARIANT 92
FT /note="R -> Q (in MLC2A; dbSNP:rs387907050)"
FT /evidence="ECO:0000269|PubMed:21419380"
FT /id="VAR_065852"
FT VARIANT 92
FT /note="R -> W (in MLC2B; dbSNP:rs387907055)"
FT /evidence="ECO:0000269|PubMed:21419380"
FT /id="VAR_065853"
FT VARIANT 98
FT /note="R -> C (in MLC2A; dbSNP:rs387907052)"
FT /evidence="ECO:0000269|PubMed:21419380"
FT /id="VAR_065854"
FT VARIANT 128
FT /note="D -> N (in MLC2B)"
FT /evidence="ECO:0000269|PubMed:21419380"
FT /id="VAR_065855"
FT VARIANT 135
FT /note="Missing (in MLC2B)"
FT /evidence="ECO:0000269|PubMed:21419380"
FT /id="VAR_065856"
FT VARIANT 148
FT /note="P -> S (in MLC2A; dbSNP:rs1555055028)"
FT /evidence="ECO:0000269|PubMed:21419380"
FT /id="VAR_065857"
FT VARIANT 196
FT /note="S -> Y (in MLC2A; dbSNP:rs387907049)"
FT /evidence="ECO:0000269|PubMed:21419380"
FT /id="VAR_065858"
FT VARIANT 211
FT /note="D -> N (in MLC2A; dbSNP:rs387907051)"
FT /evidence="ECO:0000269|PubMed:21419380"
FT /id="VAR_065859"
FT VARIANT 218
FT /note="M -> V (in dbSNP:rs10790715)"
FT /evidence="ECO:0000269|PubMed:14702039,
FT ECO:0000269|PubMed:15489334"
FT /id="VAR_034731"
FT VARIANT 288
FT /note="R -> C (in MLC2B; dbSNP:rs149782549)"
FT /evidence="ECO:0000269|PubMed:21419380"
FT /id="VAR_065860"
FT CONFLICT 2
FT /note="K -> E (in Ref. 1; AAQ93018)"
FT /evidence="ECO:0000305"
FT CONFLICT 95
FT /note="Y -> S (in Ref. 2; BAC85486)"
FT /evidence="ECO:0000305"
FT CONFLICT 284
FT /note="Q -> R (in Ref. 1; AAQ93018)"
FT /evidence="ECO:0000305"
FT CONFLICT 293
FT /note="Missing (in Ref. 4; CAD39081)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 416 AA; 46026 MW; 3CB5111207135F3C CRC64;
MKRERGALSR ASRALRLAPF VYLLLIQTDP LEGVNITSPV RLIHGTVGKS ALLSVQYSST
SSDRPVVKWQ LKRDKPVTVV QSIGTEVIGT LRPDYRDRIR LFENGSLLLS DLQLADEGTY
EVEISITDDT FTGEKTINLT VDVPISRPQV LVASTTVLEL SEAFTLNCSH ENGTKPSYTW
LKDGKPLLND SRMLLSPDQK VLTITRVLME DDDLYSCMVE NPISQGRSLP VKITVYRRSS
LYIILSTGGI FLLVTLVTVC ACWKPSKRKQ KKLEKQNSLE YMDQNDDRLK PEADTLPRSG
EQERKNPMAL YILKDKDSPE TEENPAPEPR SATEPGPPGY SVSPAVPGRS PGLPIRSARR
YPRSPARSPA TGRTHSSPPR APSSPGRSRS ASRTLRTAGV HIIREQDEAG PVEISA
