Full text data of CDH24
CDH24
(CDH11L)
[Confidence: low (only semi-automatic identification from reviews)]
Cadherin-24; Flags: Precursor
Cadherin-24; Flags: Precursor
UniProt
Q86UP0
ID CAD24_HUMAN Reviewed; 819 AA.
AC Q86UP0; D3DS44; Q86UP1; Q9NT84;
DT 31-OCT-2003, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-JUN-2003, sequence version 1.
DT 22-JAN-2014, entry version 104.
DE RecName: Full=Cadherin-24;
DE Flags: Precursor;
GN Name=CDH24; Synonyms=CDH11L; ORFNames=UNQ2834/PRO34009;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), FUNCTION, AND
RP INTERACTION WITH CATENINS.
RX PubMed=12734196; DOI=10.1074/jbc.M304119200;
RA Katafiasz B.J., Nieman M.T., Wheelock M.J., Johnson K.R.;
RT "Characterization of cadherin-24, a novel alternatively spliced type
RT II cadherin.";
RL J. Biol. Chem. 278:27513-27519(2003).
RN [2]
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.,
RA Huang A., Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J.,
RA Lewis L., Liao D., Mark M.R., Robbie E., Sanchez C., Schoenfeld J.,
RA Seshagiri S., Simmons L., Singh J., Smith V., Stinson J., Vagts A.,
RA Vandlen R.L., Watanabe C., Wieand D., Woods K., Xie M.-H.,
RA Yansura D.G., Yi S., Yu G., Yuan J., Zhang M., Zhang Z., Goddard A.D.,
RA Wood W.I., Godowski P.J., Gray A.M.;
RT "The secreted protein discovery initiative (SPDI), a large-scale
RT effort to identify novel human secreted and transmembrane proteins: a
RT bioinformatics assessment.";
RL Genome Res. 13:2265-2270(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC TISSUE=Testis;
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.,
RA Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
RA Ottenwaelder B., Poustka A., 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.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Cadherins are calcium-dependent cell adhesion proteins.
CC They preferentially interact with themselves in a homophilic
CC manner in connecting cells; cadherins may thus contribute to the
CC sorting of heterogeneous cell types. Cadherin-24 mediate strong
CC cell-cell adhesion.
CC -!- SUBUNIT: Associates with alpha-, beta- and delta-catenins.
CC -!- SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane
CC protein (Potential).
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1; Synonyms=Long form;
CC IsoId=Q86UP0-1; Sequence=Displayed;
CC Name=2; Synonyms=Short form;
CC IsoId=Q86UP0-2; Sequence=VSP_008717;
CC Name=3;
CC IsoId=Q86UP0-3; Sequence=VSP_008718, VSP_008719;
CC Note=No experimental confirmation available;
CC -!- DOMAIN: Three calcium ions are usually bound at the interface of
CC each cadherin domain and rigidify the connections, imparting a
CC strong curvature to the full-length ectodomain (By similarity).
CC -!- SIMILARITY: Contains 5 cadherin domains.
CC -----------------------------------------------------------------------
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CC Distributed under the Creative Commons Attribution-NoDerivs License
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DR EMBL; AY260900; AAP20590.1; -; mRNA.
DR EMBL; AY260901; AAP20591.1; -; mRNA.
DR EMBL; AY358199; AAQ88566.1; -; mRNA.
DR EMBL; AL137477; CAB70758.1; -; mRNA.
DR EMBL; CH471078; EAW66190.1; -; Genomic_DNA.
DR EMBL; CH471078; EAW66192.1; -; Genomic_DNA.
DR PIR; T46418; T46418.
DR RefSeq; NP_071923.2; NM_022478.3.
DR RefSeq; NP_659422.2; NM_144985.3.
DR UniGene; Hs.155912; -.
DR ProteinModelPortal; Q86UP0; -.
DR SMR; Q86UP0; 45-615, 719-813.
DR IntAct; Q86UP0; 1.
DR STRING; 9606.ENSP00000267383; -.
DR PhosphoSite; Q86UP0; -.
DR DMDM; 38257450; -.
DR UCD-2DPAGE; Q86UP0; -.
DR PaxDb; Q86UP0; -.
DR PRIDE; Q86UP0; -.
DR DNASU; 64403; -.
DR Ensembl; ENST00000267383; ENSP00000267383; ENSG00000139880.
DR Ensembl; ENST00000397359; ENSP00000380517; ENSG00000139880.
DR Ensembl; ENST00000487137; ENSP00000434821; ENSG00000139880.
DR Ensembl; ENST00000554034; ENSP00000452493; ENSG00000139880.
DR GeneID; 64403; -.
DR KEGG; hsa:64403; -.
DR UCSC; uc001wil.3; human.
DR CTD; 64403; -.
DR GeneCards; GC14M023516; -.
DR HGNC; HGNC:14265; CDH24.
DR neXtProt; NX_Q86UP0; -.
DR PharmGKB; PA26297; -.
DR eggNOG; NOG235567; -.
DR HOGENOM; HOG000231252; -.
DR HOVERGEN; HBG005217; -.
DR InParanoid; Q86UP0; -.
DR KO; K06814; -.
DR OMA; RVWHNLT; -.
DR OrthoDB; EOG7M3HZN; -.
DR PhylomeDB; Q86UP0; -.
DR Reactome; REACT_111155; Cell-Cell communication.
DR GenomeRNAi; 64403; -.
DR NextBio; 66352; -.
DR PRO; PR:Q86UP0; -.
DR ArrayExpress; Q86UP0; -.
DR Bgee; Q86UP0; -.
DR CleanEx; HS_CDH24; -.
DR Genevestigator; Q86UP0; -.
DR GO; GO:0005911; C:cell-cell junction; IDA:MGI.
DR GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR GO; GO:0005509; F:calcium ion binding; IDA:MGI.
DR GO; GO:0034332; P:adherens junction organization; TAS:Reactome.
DR GO; GO:0034329; P:cell junction assembly; TAS:Reactome.
DR GO; GO:0016337; P:cell-cell adhesion; IDA:MGI.
DR GO; GO:0007156; P:homophilic cell adhesion; IEA:InterPro.
DR Gene3D; 2.60.40.60; -; 6.
DR Gene3D; 4.10.900.10; -; 1.
DR InterPro; IPR002126; Cadherin.
DR InterPro; IPR015919; Cadherin-like.
DR InterPro; IPR020894; Cadherin_CS.
DR InterPro; IPR000233; Cadherin_cytoplasmic-dom.
DR InterPro; IPR027397; Catenin_binding_dom.
DR Pfam; PF00028; Cadherin; 4.
DR Pfam; PF01049; Cadherin_C; 1.
DR PRINTS; PR00205; CADHERIN.
DR SMART; SM00112; CA; 4.
DR SUPFAM; SSF49313; SSF49313; 5.
DR PROSITE; PS00232; CADHERIN_1; 2.
DR PROSITE; PS50268; CADHERIN_2; 5.
PE 1: Evidence at protein level;
KW Alternative splicing; Calcium; Cell adhesion; Cell membrane;
KW Cleavage on pair of basic residues; Complete proteome; Glycoprotein;
KW Membrane; Metal-binding; Reference proteome; Repeat; Signal;
KW Transmembrane; Transmembrane helix.
FT SIGNAL 1 19 Potential.
FT PROPEP 21 44 Potential.
FT /FTId=PRO_0000003827.
FT CHAIN 45 819 Cadherin-24.
FT /FTId=PRO_0000003828.
FT TOPO_DOM 45 641 Extracellular (Potential).
FT TRANSMEM 642 662 Helical; (Potential).
FT TOPO_DOM 663 819 Cytoplasmic (Potential).
FT DOMAIN 46 150 Cadherin 1.
FT DOMAIN 151 259 Cadherin 2.
FT DOMAIN 260 374 Cadherin 3.
FT DOMAIN 375 517 Cadherin 4.
FT DOMAIN 517 630 Cadherin 5.
FT CARBOHYD 446 446 N-linked (GlcNAc...) (Potential).
FT CARBOHYD 548 548 N-linked (GlcNAc...) (Potential).
FT CARBOHYD 563 563 N-linked (GlcNAc...) (Potential).
FT VAR_SEQ 1 427 Missing (in isoform 3).
FT /FTId=VSP_008718.
FT VAR_SEQ 428 492 EGTIHTAAPLDREARAWHNLTVLATELGWSWGPERGWVPLL
FT VAEWSAPAAPPQRSPVGSAVGIPQ -> MNIVCTWYCSIHS
FT ATLFSTCTLHAYFMCFLCMLYASCGIHAHAPHMLRVNCVVC
FT VWRVCFGVLPS (in isoform 3).
FT /FTId=VSP_008719.
FT VAR_SEQ 455 492 Missing (in isoform 2).
FT /FTId=VSP_008717.
SQ SEQUENCE 819 AA; 87752 MW; 9083034F18BA7E4A CRC64;
MWGLVRLLLA WLGGWGCMGR LAAPARAWAG SREHPGPALL RTRRSWVWNQ FFVIEEYAGP
EPVLIGKLHS DVDRGEGRTK YLLTGEGAGT VFVIDEATGN IHVTKSLDRE EKAQYVLLAQ
AVDRASNRPL EPPSEFIIKV QDINDNPPIF PLGPYHATVP EMSNVGTSVI QVTAHDADDP
SYGNSAKLVY TVLDGLPFFS VDPQTGVVRT AIPNMDRETQ EEFLVVIQAK DMGGHMGGLS
GSTTVTVTLS DVNDNPPKFP QSLYQFSVVE TAGPGTLVGR LRAQDPDLGD NALMAYSILD
GEGSEAFSIS TDLQGRDGLL TVRKPLDFES QRSYSFRVEA TNTLIDPAYL RRGPFKDVAS
VRVAVQDAPE PPAFTQAAYH LTVPENKAPG TLVGQISAAD LDSPASPIRY SILPHSDPER
CFSIQPEEGT IHTAAPLDRE ARAWHNLTVL ATELGWSWGP ERGWVPLLVA EWSAPAAPPQ
RSPVGSAVGI PQDSSAQASR VQVAIQTLDE NDNAPQLAEP YDTFVCDSAA PGQLIQVIRA
LDRDEVGNSS HVSFQGPLGP DANFTVQDNR DGSASLLLPS RPAPPRHAPY LVPIELWDWG
QPALSSTATV TVSVCRCQPD GSVASCWPEA HLSAAGLSTG ALLAIITCVG ALLALVVLFV
ALRRQKQEAL MVLEEEDVRE NIITYDDEGG GEEDTEAFDI TALQNPDGAA PPAPGPPARR
DVLPRARVSR QPRPPGPADV AQLLALRLRE ADEDPGVPPY DSVQVYGYEG RGSSCGSLSS
LGSGSEAGGA PGPAEPLDDW GPLFRTLAEL YGAKEPPAP
//
ID CAD24_HUMAN Reviewed; 819 AA.
AC Q86UP0; D3DS44; Q86UP1; Q9NT84;
DT 31-OCT-2003, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-JUN-2003, sequence version 1.
DT 22-JAN-2014, entry version 104.
DE RecName: Full=Cadherin-24;
DE Flags: Precursor;
GN Name=CDH24; Synonyms=CDH11L; ORFNames=UNQ2834/PRO34009;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), FUNCTION, AND
RP INTERACTION WITH CATENINS.
RX PubMed=12734196; DOI=10.1074/jbc.M304119200;
RA Katafiasz B.J., Nieman M.T., Wheelock M.J., Johnson K.R.;
RT "Characterization of cadherin-24, a novel alternatively spliced type
RT II cadherin.";
RL J. Biol. Chem. 278:27513-27519(2003).
RN [2]
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.,
RA Huang A., Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J.,
RA Lewis L., Liao D., Mark M.R., Robbie E., Sanchez C., Schoenfeld J.,
RA Seshagiri S., Simmons L., Singh J., Smith V., Stinson J., Vagts A.,
RA Vandlen R.L., Watanabe C., Wieand D., Woods K., Xie M.-H.,
RA Yansura D.G., Yi S., Yu G., Yuan J., Zhang M., Zhang Z., Goddard A.D.,
RA Wood W.I., Godowski P.J., Gray A.M.;
RT "The secreted protein discovery initiative (SPDI), a large-scale
RT effort to identify novel human secreted and transmembrane proteins: a
RT bioinformatics assessment.";
RL Genome Res. 13:2265-2270(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC TISSUE=Testis;
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.,
RA Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
RA Ottenwaelder B., Poustka A., 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.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Cadherins are calcium-dependent cell adhesion proteins.
CC They preferentially interact with themselves in a homophilic
CC manner in connecting cells; cadherins may thus contribute to the
CC sorting of heterogeneous cell types. Cadherin-24 mediate strong
CC cell-cell adhesion.
CC -!- SUBUNIT: Associates with alpha-, beta- and delta-catenins.
CC -!- SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane
CC protein (Potential).
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1; Synonyms=Long form;
CC IsoId=Q86UP0-1; Sequence=Displayed;
CC Name=2; Synonyms=Short form;
CC IsoId=Q86UP0-2; Sequence=VSP_008717;
CC Name=3;
CC IsoId=Q86UP0-3; Sequence=VSP_008718, VSP_008719;
CC Note=No experimental confirmation available;
CC -!- DOMAIN: Three calcium ions are usually bound at the interface of
CC each cadherin domain and rigidify the connections, imparting a
CC strong curvature to the full-length ectodomain (By similarity).
CC -!- SIMILARITY: Contains 5 cadherin domains.
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; AY260900; AAP20590.1; -; mRNA.
DR EMBL; AY260901; AAP20591.1; -; mRNA.
DR EMBL; AY358199; AAQ88566.1; -; mRNA.
DR EMBL; AL137477; CAB70758.1; -; mRNA.
DR EMBL; CH471078; EAW66190.1; -; Genomic_DNA.
DR EMBL; CH471078; EAW66192.1; -; Genomic_DNA.
DR PIR; T46418; T46418.
DR RefSeq; NP_071923.2; NM_022478.3.
DR RefSeq; NP_659422.2; NM_144985.3.
DR UniGene; Hs.155912; -.
DR ProteinModelPortal; Q86UP0; -.
DR SMR; Q86UP0; 45-615, 719-813.
DR IntAct; Q86UP0; 1.
DR STRING; 9606.ENSP00000267383; -.
DR PhosphoSite; Q86UP0; -.
DR DMDM; 38257450; -.
DR UCD-2DPAGE; Q86UP0; -.
DR PaxDb; Q86UP0; -.
DR PRIDE; Q86UP0; -.
DR DNASU; 64403; -.
DR Ensembl; ENST00000267383; ENSP00000267383; ENSG00000139880.
DR Ensembl; ENST00000397359; ENSP00000380517; ENSG00000139880.
DR Ensembl; ENST00000487137; ENSP00000434821; ENSG00000139880.
DR Ensembl; ENST00000554034; ENSP00000452493; ENSG00000139880.
DR GeneID; 64403; -.
DR KEGG; hsa:64403; -.
DR UCSC; uc001wil.3; human.
DR CTD; 64403; -.
DR GeneCards; GC14M023516; -.
DR HGNC; HGNC:14265; CDH24.
DR neXtProt; NX_Q86UP0; -.
DR PharmGKB; PA26297; -.
DR eggNOG; NOG235567; -.
DR HOGENOM; HOG000231252; -.
DR HOVERGEN; HBG005217; -.
DR InParanoid; Q86UP0; -.
DR KO; K06814; -.
DR OMA; RVWHNLT; -.
DR OrthoDB; EOG7M3HZN; -.
DR PhylomeDB; Q86UP0; -.
DR Reactome; REACT_111155; Cell-Cell communication.
DR GenomeRNAi; 64403; -.
DR NextBio; 66352; -.
DR PRO; PR:Q86UP0; -.
DR ArrayExpress; Q86UP0; -.
DR Bgee; Q86UP0; -.
DR CleanEx; HS_CDH24; -.
DR Genevestigator; Q86UP0; -.
DR GO; GO:0005911; C:cell-cell junction; IDA:MGI.
DR GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR GO; GO:0005509; F:calcium ion binding; IDA:MGI.
DR GO; GO:0034332; P:adherens junction organization; TAS:Reactome.
DR GO; GO:0034329; P:cell junction assembly; TAS:Reactome.
DR GO; GO:0016337; P:cell-cell adhesion; IDA:MGI.
DR GO; GO:0007156; P:homophilic cell adhesion; IEA:InterPro.
DR Gene3D; 2.60.40.60; -; 6.
DR Gene3D; 4.10.900.10; -; 1.
DR InterPro; IPR002126; Cadherin.
DR InterPro; IPR015919; Cadherin-like.
DR InterPro; IPR020894; Cadherin_CS.
DR InterPro; IPR000233; Cadherin_cytoplasmic-dom.
DR InterPro; IPR027397; Catenin_binding_dom.
DR Pfam; PF00028; Cadherin; 4.
DR Pfam; PF01049; Cadherin_C; 1.
DR PRINTS; PR00205; CADHERIN.
DR SMART; SM00112; CA; 4.
DR SUPFAM; SSF49313; SSF49313; 5.
DR PROSITE; PS00232; CADHERIN_1; 2.
DR PROSITE; PS50268; CADHERIN_2; 5.
PE 1: Evidence at protein level;
KW Alternative splicing; Calcium; Cell adhesion; Cell membrane;
KW Cleavage on pair of basic residues; Complete proteome; Glycoprotein;
KW Membrane; Metal-binding; Reference proteome; Repeat; Signal;
KW Transmembrane; Transmembrane helix.
FT SIGNAL 1 19 Potential.
FT PROPEP 21 44 Potential.
FT /FTId=PRO_0000003827.
FT CHAIN 45 819 Cadherin-24.
FT /FTId=PRO_0000003828.
FT TOPO_DOM 45 641 Extracellular (Potential).
FT TRANSMEM 642 662 Helical; (Potential).
FT TOPO_DOM 663 819 Cytoplasmic (Potential).
FT DOMAIN 46 150 Cadherin 1.
FT DOMAIN 151 259 Cadherin 2.
FT DOMAIN 260 374 Cadherin 3.
FT DOMAIN 375 517 Cadherin 4.
FT DOMAIN 517 630 Cadherin 5.
FT CARBOHYD 446 446 N-linked (GlcNAc...) (Potential).
FT CARBOHYD 548 548 N-linked (GlcNAc...) (Potential).
FT CARBOHYD 563 563 N-linked (GlcNAc...) (Potential).
FT VAR_SEQ 1 427 Missing (in isoform 3).
FT /FTId=VSP_008718.
FT VAR_SEQ 428 492 EGTIHTAAPLDREARAWHNLTVLATELGWSWGPERGWVPLL
FT VAEWSAPAAPPQRSPVGSAVGIPQ -> MNIVCTWYCSIHS
FT ATLFSTCTLHAYFMCFLCMLYASCGIHAHAPHMLRVNCVVC
FT VWRVCFGVLPS (in isoform 3).
FT /FTId=VSP_008719.
FT VAR_SEQ 455 492 Missing (in isoform 2).
FT /FTId=VSP_008717.
SQ SEQUENCE 819 AA; 87752 MW; 9083034F18BA7E4A CRC64;
MWGLVRLLLA WLGGWGCMGR LAAPARAWAG SREHPGPALL RTRRSWVWNQ FFVIEEYAGP
EPVLIGKLHS DVDRGEGRTK YLLTGEGAGT VFVIDEATGN IHVTKSLDRE EKAQYVLLAQ
AVDRASNRPL EPPSEFIIKV QDINDNPPIF PLGPYHATVP EMSNVGTSVI QVTAHDADDP
SYGNSAKLVY TVLDGLPFFS VDPQTGVVRT AIPNMDRETQ EEFLVVIQAK DMGGHMGGLS
GSTTVTVTLS DVNDNPPKFP QSLYQFSVVE TAGPGTLVGR LRAQDPDLGD NALMAYSILD
GEGSEAFSIS TDLQGRDGLL TVRKPLDFES QRSYSFRVEA TNTLIDPAYL RRGPFKDVAS
VRVAVQDAPE PPAFTQAAYH LTVPENKAPG TLVGQISAAD LDSPASPIRY SILPHSDPER
CFSIQPEEGT IHTAAPLDRE ARAWHNLTVL ATELGWSWGP ERGWVPLLVA EWSAPAAPPQ
RSPVGSAVGI PQDSSAQASR VQVAIQTLDE NDNAPQLAEP YDTFVCDSAA PGQLIQVIRA
LDRDEVGNSS HVSFQGPLGP DANFTVQDNR DGSASLLLPS RPAPPRHAPY LVPIELWDWG
QPALSSTATV TVSVCRCQPD GSVASCWPEA HLSAAGLSTG ALLAIITCVG ALLALVVLFV
ALRRQKQEAL MVLEEEDVRE NIITYDDEGG GEEDTEAFDI TALQNPDGAA PPAPGPPARR
DVLPRARVSR QPRPPGPADV AQLLALRLRE ADEDPGVPPY DSVQVYGYEG RGSSCGSLSS
LGSGSEAGGA PGPAEPLDDW GPLFRTLAEL YGAKEPPAP
//