CEMIP_HUMAN
ID CEMIP_HUMAN Reviewed; 1361 AA.
AC Q8WUJ3; Q6L9J5; Q9H1K5; Q9NPN9; Q9ULM1;
DT 13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT 13-APR-2004, sequence version 2.
DT 03-AUG-2022, entry version 152.
DE RecName: Full=Cell migration-inducing and hyaluronan-binding protein;
DE EC=3.2.1.35 {ECO:0000269|PubMed:23509262, ECO:0000269|PubMed:24269685};
DE Flags: Precursor;
GN Name=CEMIP; Synonyms=KIAA1199;
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 [MRNA], VARIANTS CYS-187; HIS-187 AND TYR-783, AND
RP VARIANTS ARG-783; ILE-1109 AND ALA-1169.
RX PubMed=14577002; DOI=10.1007/s10038-003-0079-2;
RA Abe S., Usami S., Nakamura Y.;
RT "Mutations in the gene encoding KIAA1199 protein, an inner-ear protein
RT expressed in Deiters' cells and the fibrocytes, as the cause of
RT nonsyndromic hearing loss.";
RL J. Hum. Genet. 48:564-570(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=16157444; DOI=10.1016/j.canlet.2005.07.028;
RA Michishita E., Garces G., Barrett J.C., Horikawa I.;
RT "Upregulation of the KIAA1199 gene is associated with cellular mortality.";
RL Cancer Lett. 239:71-77(2006).
RN [3]
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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Skin;
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 349-1361 (ISOFORM 1), AND TISSUE
RP SPECIFICITY.
RC TISSUE=Brain;
RX PubMed=10574462; DOI=10.1093/dnares/6.5.337;
RA Nagase T., Ishikawa K., Kikuno R., Hirosawa M., Nomura N., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XV. The
RT complete sequences of 100 new cDNA clones from brain which code for large
RT proteins in vitro.";
RL DNA Res. 6:337-345(1999).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 558-1361.
RG The European IMAGE consortium;
RL Submitted (JUN-2000) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 862-1361.
RX PubMed=11247670; DOI=10.1006/geno.2000.6466;
RA Wines M.E., Lee L., Katari M.S., Zhang L., DeRossi C., Shi Y., Perkins S.,
RA Feldman M., McCombie W.R., Holdener B.C.;
RT "Identification of mesoderm development (mesd) candidate genes by
RT comparative mapping and genome sequence analysis.";
RL Genomics 72:88-98(2001).
RN [8]
RP TISSUE SPECIFICITY.
RX PubMed=12471561; DOI=10.1086/345398;
RA Abe S., Katagiri T., Saito-Hisaminato A., Usami S., Inoue Y., Tsunoda T.,
RA Nakamura Y.;
RT "Identification of CRYM as a candidate responsible for nonsyndromic
RT deafness, through cDNA microarray analysis of human cochlear and vestibular
RT tissues.";
RL Am. J. Hum. Genet. 72:73-82(2003).
RN [9]
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=19434458; DOI=10.1245/s10434-009-0469-6;
RA Matsuzaki S., Tanaka F., Mimori K., Tahara K., Inoue H., Mori M.;
RT "Clinicopathologic significance of KIAA1199 overexpression in human gastric
RT cancer.";
RL Ann. Surg. Oncol. 16:2042-2051(2009).
RN [10]
RP PROBABLE FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=21772334; DOI=10.1038/bjc.2011.268;
RA Birkenkamp-Demtroder K., Maghnouj A., Mansilla F., Thorsen K.,
RA Andersen C.L., Oster B., Hahn S., Orntoft T.F.;
RT "Repression of KIAA1199 attenuates Wnt-signalling and decreases the
RT proliferation of colon cancer cells.";
RL Br. J. Cancer 105:552-561(2011).
RN [11]
RP TISSUE SPECIFICITY, AND INDUCTION.
RX PubMed=22970280; DOI=10.1371/journal.pone.0044661;
RA Kuscu C., Evensen N., Kim D., Hu Y.J., Zucker S., Cao J.;
RT "Transcriptional and epigenetic regulation of KIAA1199 gene expression in
RT human breast cancer.";
RL PLoS ONE 7:E44661-E44661(2012).
RN [12]
RP FUNCTION IN CANCER, INTERACTION WITH HSPA5, SUBCELLULAR LOCATION, AND
RP TISSUE SPECIFICITY.
RX PubMed=23990668; DOI=10.1093/jnci/djt224;
RA Evensen N.A., Kuscu C., Nguyen H.L., Zarrabi K., Dufour A., Kadam P.,
RA Hu Y.J., Pulkoski-Gross A., Bahou W.F., Zucker S., Cao J.;
RT "Unraveling the role of KIAA1199, a novel endoplasmic reticulum protein, in
RT cancer cell migration.";
RL J. Natl. Cancer Inst. 105:1402-1416(2013).
RN [13]
RP INTERACTION WITH EPHA2 AND ITPR3, GLYCOSYLATION, SUBCELLULAR LOCATION, AND
RP TISSUE SPECIFICITY.
RX PubMed=23936024; DOI=10.1371/journal.pone.0069473;
RA Tiwari A., Schneider M., Fiorino A., Haider R., Okoniewski M.J.,
RA Roschitzki B., Uzozie A., Menigatti M., Jiricny J., Marra G.;
RT "Early insights into the function of KIAA1199, a markedly overexpressed
RT protein in human colorectal tumors.";
RL PLoS ONE 8:E69473-E69473(2013).
RN [14]
RP FUNCTION IN HYALURONIC ACID DEGRADATION, CATALYTIC ACTIVITY, ACTIVITY
RP REGULATION, HYALURONIC ACID-BINDING, INTERACTION WITH CLATHRIN, SUBCELLULAR
RP LOCATION, INDUCTION, AND CHARACTERIZATION OF VARIANTS CYS-187; HIS-187;
RP ARG-783 AND ILE-1109.
RX PubMed=23509262; DOI=10.1073/pnas.1215432110;
RA Yoshida H., Nagaoka A., Kusaka-Kikushima A., Tobiishi M., Kawabata K.,
RA Sayo T., Sakai S., Sugiyama Y., Enomoto H., Okada Y., Inoue S.;
RT "KIAA1199, a deafness gene of unknown function, is a new hyaluronan binding
RT protein involved in hyaluronan depolymerization.";
RL Proc. Natl. Acad. Sci. U.S.A. 110:5612-5617(2013).
RN [15]
RP FUNCTION IN HYALURONIC ACID DEGRADATION, CATALYTIC ACTIVITY, GLYCOSYLATION,
RP SUBCELLULAR LOCATION, PROTEOLYTIC PROCESSING, AND SIGNAL SEQUENCE CLEAVAGE
RP SITE.
RX PubMed=24269685; DOI=10.1016/j.febslet.2013.11.017;
RA Yoshida H., Nagaoka A., Nakamura S., Tobiishi M., Sugiyama Y., Inoue S.;
RT "N-Terminal signal sequence is required for cellular trafficking and
RT hyaluronan-depolymerization of KIAA1199.";
RL FEBS Lett. 588:111-116(2014).
CC -!- FUNCTION: Mediates depolymerization of hyaluronic acid (HA) via the
CC cell membrane-associated clathrin-coated pit endocytic pathway. Binds
CC to hyaluronic acid. Hydrolyzes high molecular weight hyaluronic acid to
CC produce an intermediate-sized product, a process that may occur through
CC rapid vesicle endocytosis and recycling without intracytoplasmic
CC accumulation or digestion in lysosomes. Involved in hyaluronan
CC catabolism in the dermis of the skin and arthritic synovium. Positively
CC regulates epithelial-mesenchymal transition (EMT), and hence tumor cell
CC growth, invasion and cancer dissemination. In collaboration with
CC HSPA5/BIP, promotes cancer cell migration in a calcium and PKC-
CC dependent manner. May be involved in hearing.
CC {ECO:0000269|PubMed:23509262, ECO:0000269|PubMed:23990668,
CC ECO:0000269|PubMed:24269685}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Random hydrolysis of (1->4)-linkages between N-acetyl-beta-D-
CC glucosamine and D-glucuronate residues in hyaluronate.; EC=3.2.1.35;
CC Evidence={ECO:0000269|PubMed:23509262, ECO:0000269|PubMed:24269685};
CC -!- ACTIVITY REGULATION: Activity is up-regulated by histamine.
CC {ECO:0000269|PubMed:23509262}.
CC -!- SUBUNIT: Interacts with EPHA2 and ITPR3. Interacts with HSPA5/BIP; the
CC interaction induces calcium leakage from the endoplasmic reticulum and
CC cell migration. Interacts with clathrin heavy chain/CLTC.
CC {ECO:0000269|PubMed:23509262, ECO:0000269|PubMed:23936024,
CC ECO:0000269|PubMed:23990668}.
CC -!- SUBCELLULAR LOCATION: Nucleus. Cytoplasm. Endoplasmic reticulum. Cell
CC membrane. Membrane, clathrin-coated pit. Secreted. Note=Retained in the
CC endoplasmic reticulum (ER) in a HSPA5/BIP-dependent manner. Colocalized
CC with clathrin heavy chain/CLTC in clathrin-coated vesicles. Strongly
CC detected in the cytoplasm of breast carcinoma cells, whereas poorly
CC detected in adjacent normal epithelial cells, stromal cells, or benign
CC breast tissues. Localized in the nucleus and cytoplasm of colon
CC adenocarcinomas.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8WUJ3-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8WUJ3-2; Sequence=VSP_009814, VSP_009815;
CC -!- TISSUE SPECIFICITY: Expressed in dermal and in synovial fibroblasts.
CC Strongly expressed in gastric cancers compared with the paired normal
CC tissues. Strongly expressed in both ductal carcinoma and invasive
CC breast cancer cells compared with benign epithelial cells (at protein
CC level). Strongly expressed in brain, placenta, prostate, breast, lung
CC and testis. Expressed in fibroblasts, epithelial cells and cancer
CC cells. In ear, it is specifically expressed in inner ear. Expressed in
CC cochlea and vestibule tissues. Strongly expressed in gastric cancers
CC compared with the paired normal tissues. Strongly expressed in colon
CC adenocarcinomas compared with normal colonic mucosas. Strongly
CC expressed in breast cancer as compared to normal breast tissue.
CC {ECO:0000269|PubMed:10574462, ECO:0000269|PubMed:12471561,
CC ECO:0000269|PubMed:16157444, ECO:0000269|PubMed:19434458,
CC ECO:0000269|PubMed:21772334, ECO:0000269|PubMed:22970280,
CC ECO:0000269|PubMed:23936024, ECO:0000269|PubMed:23990668}.
CC -!- INDUCTION: Up-regulated by histamine. Up-regulated by the adapter
CC protein complex 1 (AP-1) and NF-kappaB/RELA. Down-regulated by
CC transforming growth factor TGFB1. {ECO:0000269|PubMed:22970280,
CC ECO:0000269|PubMed:23509262}.
CC -!- DOMAIN: The signal sequence is essential in mediating its proper
CC translocation, hyaluronic acid (HA) degradation activity and secretion.
CC -!- PTM: N-glycosylated; glycosylation is not necessary for HA-binding.
CC {ECO:0000269|PubMed:23936024, ECO:0000269|PubMed:24269685}.
CC -!- SIMILARITY: Belongs to the CEMIP family. {ECO:0000305}.
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DR EMBL; AB103330; BAD02451.1; -; mRNA.
DR EMBL; CH471136; EAW99111.1; -; Genomic_DNA.
DR EMBL; BC020256; AAH20256.1; -; mRNA.
DR EMBL; AB033025; BAA86513.1; -; mRNA.
DR EMBL; AL359061; CAB94391.1; -; mRNA.
DR EMBL; AY007811; AAG41059.1; -; mRNA.
DR CCDS; CCDS10315.1; -. [Q8WUJ3-1]
DR RefSeq; NP_001280227.1; NM_001293298.1. [Q8WUJ3-1]
DR RefSeq; NP_001280233.1; NM_001293304.1. [Q8WUJ3-1]
DR RefSeq; NP_061159.1; NM_018689.2. [Q8WUJ3-1]
DR AlphaFoldDB; Q8WUJ3; -.
DR SMR; Q8WUJ3; -.
DR BioGRID; 121452; 36.
DR IntAct; Q8WUJ3; 3.
DR STRING; 9606.ENSP00000378177; -.
DR CarbonylDB; Q8WUJ3; -.
DR GlyGen; Q8WUJ3; 7 sites.
DR iPTMnet; Q8WUJ3; -.
DR PhosphoSitePlus; Q8WUJ3; -.
DR BioMuta; CEMIP; -.
DR DMDM; 46396475; -.
DR jPOST; Q8WUJ3; -.
DR MassIVE; Q8WUJ3; -.
DR PaxDb; Q8WUJ3; -.
DR PeptideAtlas; Q8WUJ3; -.
DR PRIDE; Q8WUJ3; -.
DR ProteomicsDB; 74690; -. [Q8WUJ3-1]
DR ProteomicsDB; 74691; -. [Q8WUJ3-2]
DR Antibodypedia; 27890; 230 antibodies from 25 providers.
DR DNASU; 57214; -.
DR Ensembl; ENST00000220244.7; ENSP00000220244.3; ENSG00000103888.17. [Q8WUJ3-1]
DR Ensembl; ENST00000356249.9; ENSP00000348583.5; ENSG00000103888.17. [Q8WUJ3-1]
DR Ensembl; ENST00000394685.8; ENSP00000378177.3; ENSG00000103888.17. [Q8WUJ3-1]
DR GeneID; 57214; -.
DR KEGG; hsa:57214; -.
DR MANE-Select; ENST00000394685.8; ENSP00000378177.3; NM_001293298.2; NP_001280227.1.
DR UCSC; uc002bfw.2; human. [Q8WUJ3-1]
DR CTD; 57214; -.
DR DisGeNET; 57214; -.
DR GeneCards; CEMIP; -.
DR HGNC; HGNC:29213; CEMIP.
DR HPA; ENSG00000103888; Tissue enhanced (choroid plexus, endometrium).
DR MIM; 608366; gene.
DR neXtProt; NX_Q8WUJ3; -.
DR OpenTargets; ENSG00000103888; -.
DR PharmGKB; PA134967531; -.
DR VEuPathDB; HostDB:ENSG00000103888; -.
DR eggNOG; ENOG502QT0K; Eukaryota.
DR GeneTree; ENSGT00940000153636; -.
DR HOGENOM; CLU_005606_1_0_1; -.
DR InParanoid; Q8WUJ3; -.
DR OMA; DGHHGKV; -.
DR PhylomeDB; Q8WUJ3; -.
DR TreeFam; TF316575; -.
DR PathwayCommons; Q8WUJ3; -.
DR Reactome; R-HSA-2142850; Hyaluronan biosynthesis and export.
DR SignaLink; Q8WUJ3; -.
DR BioGRID-ORCS; 57214; 14 hits in 1065 CRISPR screens.
DR ChiTaRS; CEMIP; human.
DR GeneWiki; KIAA1199; -.
DR GenomeRNAi; 57214; -.
DR Pharos; Q8WUJ3; Tbio.
DR PRO; PR:Q8WUJ3; -.
DR Proteomes; UP000005640; Chromosome 15.
DR RNAct; Q8WUJ3; protein.
DR Bgee; ENSG00000103888; Expressed in choroid plexus epithelium and 130 other tissues.
DR ExpressionAtlas; Q8WUJ3; baseline and differential.
DR Genevisible; Q8WUJ3; HS.
DR GO; GO:0045334; C:clathrin-coated endocytic vesicle; IDA:UniProtKB.
DR GO; GO:0005905; C:clathrin-coated pit; IEA:UniProtKB-SubCell.
DR GO; GO:0030665; C:clathrin-coated vesicle membrane; IEA:Ensembl.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:UniProtKB.
DR GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0032050; F:clathrin heavy chain binding; IDA:UniProtKB.
DR GO; GO:0046923; F:ER retention sequence binding; IDA:UniProtKB.
DR GO; GO:0005540; F:hyaluronic acid binding; IDA:UniProtKB.
DR GO; GO:0004415; F:hyalurononglucosaminidase activity; IMP:UniProtKB.
DR GO; GO:0030213; P:hyaluronan biosynthetic process; TAS:Reactome.
DR GO; GO:0030214; P:hyaluronan catabolic process; IMP:UniProtKB.
DR GO; GO:0030335; P:positive regulation of cell migration; IDA:UniProtKB.
DR GO; GO:0010800; P:positive regulation of peptidyl-threonine phosphorylation; IDA:UniProtKB.
DR GO; GO:1900020; P:positive regulation of protein kinase C activity; IDA:UniProtKB.
DR GO; GO:0090314; P:positive regulation of protein targeting to membrane; IDA:UniProtKB.
DR GO; GO:0051281; P:positive regulation of release of sequestered calcium ion into cytosol; IDA:UniProtKB.
DR GO; GO:0007605; P:sensory perception of sound; IMP:UniProtKB.
DR CDD; cd13938; PANDER_like_TMEM2; 1.
DR InterPro; IPR019316; G8_domain.
DR InterPro; IPR039477; ILEI/PANDER_dom.
DR InterPro; IPR011050; Pectin_lyase_fold/virulence.
DR InterPro; IPR039473; TMEM2_PANDER-like.
DR InterPro; IPR025155; WxxW_domain.
DR Pfam; PF10162; G8; 1.
DR Pfam; PF15711; ILEI; 2.
DR Pfam; PF13330; Mucin2_WxxW; 1.
DR SMART; SM01225; G8; 1.
DR SUPFAM; SSF51126; SSF51126; 1.
DR PROSITE; PS51484; G8; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell membrane; Coated pit; Cytoplasm;
KW Endoplasmic reticulum; Glycoprotein; Glycosidase; Hyaluronic acid;
KW Hydrolase; Membrane; Nucleus; Reference proteome; Repeat; Secreted; Signal.
FT SIGNAL 1..30
FT /evidence="ECO:0000269|PubMed:24269685"
FT CHAIN 31..1361
FT /note="Cell migration-inducing and hyaluronan-binding
FT protein"
FT /id="PRO_0000021538"
FT DOMAIN 44..166
FT /note="G8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00817"
FT REPEAT 572..594
FT /note="PbH1 1"
FT REPEAT 595..617
FT /note="PbH1 2"
FT REPEAT 719..741
FT /note="PbH1 3"
FT REPEAT 798..819
FT /note="PbH1 4"
FT REGION 295..591
FT /note="Necessary for its endoplasmic reticulum (ER)
FT retention and interaction with HSPA5"
FT /evidence="ECO:0000269|PubMed:23990668"
FT CARBOHYD 119
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 165
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 312
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 370
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 420
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 889
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 921
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 978..992
FT /note="NWLVRHPDCINVPDW -> KWHSLASKAASGPSG (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_009814"
FT VAR_SEQ 993..1361
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_009815"
FT VARIANT 187
FT /note="R -> C (in a family with non-syndromic hearing loss;
FT reduces hyaluronic acid degradation activity;
FT dbSNP:rs368854657)"
FT /evidence="ECO:0000269|PubMed:14577002,
FT ECO:0000269|PubMed:23509262"
FT /id="VAR_018165"
FT VARIANT 187
FT /note="R -> H (in two unrelated families with non-syndromic
FT hearing loss; reduces hyaluronic acid (HA) degradation
FT activity; dbSNP:rs144446375)"
FT /evidence="ECO:0000269|PubMed:14577002,
FT ECO:0000269|PubMed:23509262"
FT /id="VAR_018166"
FT VARIANT 783
FT /note="H -> R (does not inhibit hyaluronic acid degradation
FT activity; dbSNP:rs12441101)"
FT /evidence="ECO:0000269|PubMed:14577002,
FT ECO:0000269|PubMed:23509262"
FT /id="VAR_018167"
FT VARIANT 783
FT /note="H -> Y (in a sporadic case of non-syndromic hearing
FT loss; dbSNP:rs996035812)"
FT /evidence="ECO:0000269|PubMed:14577002"
FT /id="VAR_018168"
FT VARIANT 1109
FT /note="V -> I (does not inhibit hyaluronic acid degradation
FT activity; dbSNP:rs751807711)"
FT /evidence="ECO:0000269|PubMed:14577002,
FT ECO:0000269|PubMed:23509262"
FT /id="VAR_018169"
FT VARIANT 1169
FT /note="P -> A (in dbSNP:rs16972583)"
FT /evidence="ECO:0000269|PubMed:14577002"
FT /id="VAR_018170"
FT CONFLICT 558..564
FT /note="HFHLAGD -> TRPPTRP (in Ref. 6; CAB94391)"
FT /evidence="ECO:0000305"
FT CONFLICT 862
FT /note="H -> T (in Ref. 7; AAG41059)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1361 AA; 152998 MW; 40CDFFB84F99516C CRC64;
MGAAGRQDFL FKAMLTISWL TLTCFPGATS TVAAGCPDQS PELQPWNPGH DQDHHVHIGQ
GKTLLLTSSA TVYSIHISEG GKLVIKDHDE PIVLRTRHIL IDNGGELHAG SALCPFQGNF
TIILYGRADE GIQPDPYYGL KYIGVGKGGA LELHGQKKLS WTFLNKTLHP GGMAEGGYFF
ERSWGHRGVI VHVIDPKSGT VIHSDRFDTY RSKKESERLV QYLNAVPDGR ILSVAVNDEG
SRNLDDMARK AMTKLGSKHF LHLGFRHPWS FLTVKGNPSS SVEDHIEYHG HRGSAAARVF
KLFQTEHGEY FNVSLSSEWV QDVEWTEWFD HDKVSQTKGG EKISDLWKAH PGKICNRPID
IQATTMDGVN LSTEVVYKKG QDYRFACYDR GRACRSYRVR FLCGKPVRPK LTVTIDTNVN
STILNLEDNV QSWKPGDTLV IASTDYSMYQ AEEFQVLPCR SCAPNQVKVA GKPMYLHIGE
EIDGVDMRAE VGLLSRNIIV MGEMEDKCYP YRNHICNFFD FDTFGGHIKF ALGFKAAHLE
GTELKHMGQQ LVGQYPIHFH LAGDVDERGG YDPPTYIRDL SIHHTFSRCV TVHGSNGLLI
KDVVGYNSLG HCFFTEDGPE ERNTFDHCLG LLVKSGTLLP SDRDSKMCKM ITEDSYPGYI
PKPRQDCNAV STFWMANPNN NLINCAAAGS EETGFWFIFH HVPTGPSVGM YSPGYSEHIP
LGKFYNNRAH SNYRAGMIID NGVKTTEASA KDKRPFLSII SARYSPHQDA DPLKPREPAI
IRHFIAYKNQ DHGAWLRGGD VWLDSCRFAD NGIGLTLASG GTFPYDDGSK QEIKNSLFVG
ESGNVGTEMM DNRIWGPGGL DHSGRTLPIG QNFPIRGIQL YDGPINIQNC TFRKFVALEG
RHTSALAFRL NNAWQSCPHN NVTGIAFEDV PITSRVFFGE PGPWFNQLDM DGDKTSVFHD
VDGSVSEYPG SYLTKNDNWL VRHPDCINVP DWRGAICSGC YAQMYIQAYK TSNLRMKIIK
NDFPSHPLYL EGALTRSTHY QQYQPVVTLQ KGYTIHWDQT APAELAIWLI NFNKGDWIRV
GLCYPRGTTF SILSDVHNRL LKQTSKTGVF VRTLQMDKVE QSYPGRSHYY WDEDSGLLFL
KLKAQNEREK FAFCSMKGCE RIKIKALIPK NAGVSDCTAT AYPKFTERAV VDVPMPKKLF
GSQLKTKDHF LEVKMESSKQ HFFHLWNDFA YIEVDGKKYP SSEDGIQVVV IDGNQGRVVS
HTSFRNSILQ GIPWQLFNYV ATIPDNSIVL MASKGRYVSR GPWTRVLEKL GADRGLKLKE
QMAFVGFKGS FRPIWVTLDT EDHKAKIFQV VPIPVVKKKK L
