Full text data of AMIGO2
AMIGO2
(ALI1)
[Confidence: low (only semi-automatic identification from reviews)]
Amphoterin-induced protein 2 (AMIGO-2; Alivin-1; Differentially expressed in gastric adenocarcinomas; DEGA; Flags: Precursor)
Amphoterin-induced protein 2 (AMIGO-2; Alivin-1; Differentially expressed in gastric adenocarcinomas; DEGA; Flags: Precursor)
UniProt
Q86SJ2
ID AMGO2_HUMAN Reviewed; 522 AA.
AC Q86SJ2; Q4VBP6; Q7Z4A0; Q96CN8;
DT 21-JUN-2005, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-JUN-2003, sequence version 1.
DT 22-JAN-2014, entry version 109.
DE RecName: Full=Amphoterin-induced protein 2;
DE AltName: Full=AMIGO-2;
DE AltName: Full=Alivin-1;
DE AltName: Full=Differentially expressed in gastric adenocarcinomas;
DE Short=DEGA;
DE Flags: Precursor;
GN Name=AMIGO2; Synonyms=ALI1;
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].
RC TISSUE=Fibrosarcoma;
RX PubMed=12629050; DOI=10.1083/jcb.200209074;
RA Kuja-Panula J., Kiiltomaeki M., Yamashiro T., Rouhiainen A.,
RA Rauvala H.;
RT "AMIGO, a transmembrane protein implicated in axon tract development,
RT defines a novel protein family with leucine-rich repeats.";
RL J. Cell Biol. 160:963-973(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Brain;
RX PubMed=12843293;
RA Ono T., Sekino-Suzuki N., Kikkawa Y., Yonekawa H., Kawashima S.;
RT "Alivin 1, a novel neuronal activity-dependent gene, inhibits
RT apoptosis and promotes survival of cerebellar granule neurons.";
RL J. Neurosci. 23:5887-5896(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RX PubMed=15107827; DOI=10.1038/sj.onc.1207681;
RA Rabenau K.E., O'Toole J.M., Bassi R., Kotanides H., Witte L.,
RA Ludwig D.L., Pereira D.S.;
RT "DEGA/AMIGO-2, a leucine-rich repeat family member, differentially
RT expressed in human gastric adenocarcinoma: effects on ploidy,
RT chromosomal stability, cell adhesion/migration and tumorigenicity.";
RL Oncogene 23:5056-5067(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Stomach;
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis, and Uterus;
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
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,
RA Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in
RT signaling networks.";
RL Cell 127:635-648(2006).
CC -!- FUNCTION: Required for depolarization-dependent survival of
CC cultured cerebellar granule neurons. May mediate homophilic as
CC well as heterophilic cell-cell interaction with AMIGO1 or AMIGO3.
CC May contribute to signal transduction through its intracellular
CC domain. May be required for tumorigenesis of a subset of gastric
CC adenocarcinomas.
CC -!- SUBUNIT: Binds itself as well as AMIGO1 and AMIGO3 (By
CC similarity).
CC -!- INTERACTION:
CC O00555:CACNA1A; NbExp=2; IntAct=EBI-3866830, EBI-766279;
CC -!- SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane
CC protein (By similarity). Nucleus (By similarity). Note=Associated
CC with nucleus as well as plasma membrane. Restricted to somata of
CC cerebellar as well as hippocampal neurons (By similarity).
CC -!- TISSUE SPECIFICITY: Highest levels in breast, ovary, cervix, and
CC uterus. Lower levels in lung, colon, and rectum. Differentially
CC expressed in 56% of thyroid, 57% of pancreatic and 45% of stomach
CC cancers.
CC -!- SIMILARITY: Belongs to the immunoglobulin superfamily. AMIGO
CC family.
CC -!- SIMILARITY: Contains 1 Ig-like C2-type (immunoglobulin-like)
CC domain.
CC -!- SIMILARITY: Contains 6 LRR (leucine-rich) repeats.
CC -!- SIMILARITY: Contains 1 LRRCT domain.
CC -!- SIMILARITY: Contains 1 LRRNT domain.
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; AY237005; AAO48946.1; -; mRNA.
DR EMBL; AB079074; BAC81188.1; -; mRNA.
DR EMBL; AB080610; BAC81189.1; -; mRNA.
DR EMBL; AY454159; AAR83271.1; -; mRNA.
DR EMBL; AL833007; CAH56293.1; -; mRNA.
DR EMBL; BC014103; AAH14103.2; -; mRNA.
DR EMBL; BC047595; AAH47595.1; -; mRNA.
DR EMBL; BC095477; AAH95477.1; -; mRNA.
DR RefSeq; NP_001137140.1; NM_001143668.1.
DR RefSeq; NP_862830.1; NM_181847.4.
DR RefSeq; XP_005268894.1; XM_005268837.1.
DR UniGene; Hs.121520; -.
DR ProteinModelPortal; Q86SJ2; -.
DR SMR; Q86SJ2; 41-387.
DR IntAct; Q86SJ2; 1.
DR STRING; 9606.ENSP00000266581; -.
DR DMDM; 68052338; -.
DR PaxDb; Q86SJ2; -.
DR PeptideAtlas; Q86SJ2; -.
DR PRIDE; Q86SJ2; -.
DR Ensembl; ENST00000266581; ENSP00000266581; ENSG00000139211.
DR Ensembl; ENST00000321382; ENSP00000320848; ENSG00000139211.
DR Ensembl; ENST00000429635; ENSP00000406020; ENSG00000139211.
DR Ensembl; ENST00000550413; ENSP00000449034; ENSG00000139211.
DR GeneID; 347902; -.
DR KEGG; hsa:347902; -.
DR UCSC; uc001rpk.3; human.
DR CTD; 347902; -.
DR GeneCards; GC12M047469; -.
DR HGNC; HGNC:24073; AMIGO2.
DR HPA; HPA054004; -.
DR neXtProt; NX_Q86SJ2; -.
DR PharmGKB; PA142672626; -.
DR eggNOG; NOG146733; -.
DR HOGENOM; HOG000231327; -.
DR HOVERGEN; HBG080231; -.
DR InParanoid; Q86SJ2; -.
DR OMA; SCIAMNR; -.
DR OrthoDB; EOG71CFKP; -.
DR PhylomeDB; Q86SJ2; -.
DR GenomeRNAi; 347902; -.
DR NextBio; 99311; -.
DR PRO; PR:Q86SJ2; -.
DR ArrayExpress; Q86SJ2; -.
DR Bgee; Q86SJ2; -.
DR CleanEx; HS_AMIGO2; -.
DR Genevestigator; Q86SJ2; -.
DR GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0007157; P:heterophilic cell-cell adhesion; ISS:UniProtKB.
DR GO; GO:0007156; P:homophilic cell adhesion; ISS:UniProtKB.
DR GO; GO:0043066; P:negative regulation of apoptotic process; IEA:Ensembl.
DR GO; GO:0043069; P:negative regulation of programmed cell death; ISS:UniProtKB.
DR Gene3D; 2.60.40.10; -; 1.
DR InterPro; IPR000483; Cys-rich_flank_reg_C.
DR InterPro; IPR007110; Ig-like_dom.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR003599; Ig_sub.
DR InterPro; IPR001611; Leu-rich_rpt.
DR InterPro; IPR003591; Leu-rich_rpt_typical-subtyp.
DR InterPro; IPR000372; LRR-contain_N.
DR Pfam; PF00560; LRR_1; 1.
DR SMART; SM00409; IG; 1.
DR SMART; SM00369; LRR_TYP; 1.
DR SMART; SM00082; LRRCT; 1.
DR SMART; SM00013; LRRNT; 1.
DR PROSITE; PS50835; IG_LIKE; 1.
DR PROSITE; PS51450; LRR; 7.
PE 1: Evidence at protein level;
KW Cell adhesion; Cell membrane; Complete proteome; Disulfide bond;
KW Glycoprotein; Immunoglobulin domain; Leucine-rich repeat; Membrane;
KW Nucleus; Reference proteome; Repeat; Signal; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1 39 Potential.
FT CHAIN 40 522 Amphoterin-induced protein 2.
FT /FTId=PRO_0000014509.
FT TOPO_DOM 40 398 Extracellular (Potential).
FT TRANSMEM 399 419 Helical; (Potential).
FT TOPO_DOM 420 522 Cytoplasmic (Potential).
FT DOMAIN 40 68 LRRNT.
FT REPEAT 69 90 LRR 1.
FT REPEAT 94 115 LRR 2.
FT REPEAT 118 139 LRR 3.
FT REPEAT 142 163 LRR 4.
FT REPEAT 166 187 LRR 5.
FT REPEAT 193 214 LRR 6.
FT DOMAIN 228 284 LRRCT.
FT DOMAIN 289 379 Ig-like C2-type.
FT CARBOHYD 58 58 N-linked (GlcNAc...) (Potential).
FT CARBOHYD 104 104 N-linked (GlcNAc...) (Potential).
FT CARBOHYD 281 281 N-linked (GlcNAc...) (Potential).
FT CARBOHYD 288 288 N-linked (GlcNAc...) (Potential).
FT CARBOHYD 345 345 N-linked (GlcNAc...) (Potential).
FT CARBOHYD 373 373 N-linked (GlcNAc...) (Potential).
FT CARBOHYD 381 381 N-linked (GlcNAc...) (Potential).
FT CARBOHYD 384 384 N-linked (GlcNAc...) (Potential).
FT DISULFID 41 47 By similarity.
FT DISULFID 45 54 By similarity.
FT DISULFID 232 260 By similarity.
FT DISULFID 234 282 By similarity.
FT DISULFID 310 363 By similarity.
SQ SEQUENCE 522 AA; 57934 MW; 20A86E3D82C05B9B CRC64;
MSLRVHTLPT LLGAVVRPGC RELLCLLMIT VTVGPGASGV CPTACICATD IVSCTNKNLS
KVPGNLFRLI KRLDLSYNRI GLLDSEWIPV SFAKLNTLIL RHNNITSIST GSFSTTPNLK
CLDLSSNKLK TVKNAVFQEL KVLEVLLLYN NHISYLDPSA FGGLSQLQKL YLSGNFLTQF
PMDLYVGRFK LAELMFLDVS YNRIPSMPMH HINLVPGKQL RGIYLHGNPF VCDCSLYSLL
VFWYRRHFSS VMDFKNDYTC RLWSDSRHSR QVLLLQDSFM NCSDSIINGS FRALGFIHEA
QVGERLMVHC DSKTGNANTD FIWVGPDNRL LEPDKEMENF YVFHNGSLVI ESPRFEDAGV
YSCIAMNKQR LLNETVDVTI NVSNFTVSRS HAHEAFNTAF TTLAACVASI VLVLLYLYLT
PCPCKCKTKR QKNMLHQSNA HSSILSPGPA SDASADERKA GAGKRVVFLE PLKDTAAGQN
GKVRLFPSEA VIAEGILKST RGKSDSDSVN SVFSDTPFVA ST
//
ID AMGO2_HUMAN Reviewed; 522 AA.
AC Q86SJ2; Q4VBP6; Q7Z4A0; Q96CN8;
DT 21-JUN-2005, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-JUN-2003, sequence version 1.
DT 22-JAN-2014, entry version 109.
DE RecName: Full=Amphoterin-induced protein 2;
DE AltName: Full=AMIGO-2;
DE AltName: Full=Alivin-1;
DE AltName: Full=Differentially expressed in gastric adenocarcinomas;
DE Short=DEGA;
DE Flags: Precursor;
GN Name=AMIGO2; Synonyms=ALI1;
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].
RC TISSUE=Fibrosarcoma;
RX PubMed=12629050; DOI=10.1083/jcb.200209074;
RA Kuja-Panula J., Kiiltomaeki M., Yamashiro T., Rouhiainen A.,
RA Rauvala H.;
RT "AMIGO, a transmembrane protein implicated in axon tract development,
RT defines a novel protein family with leucine-rich repeats.";
RL J. Cell Biol. 160:963-973(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Brain;
RX PubMed=12843293;
RA Ono T., Sekino-Suzuki N., Kikkawa Y., Yonekawa H., Kawashima S.;
RT "Alivin 1, a novel neuronal activity-dependent gene, inhibits
RT apoptosis and promotes survival of cerebellar granule neurons.";
RL J. Neurosci. 23:5887-5896(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RX PubMed=15107827; DOI=10.1038/sj.onc.1207681;
RA Rabenau K.E., O'Toole J.M., Bassi R., Kotanides H., Witte L.,
RA Ludwig D.L., Pereira D.S.;
RT "DEGA/AMIGO-2, a leucine-rich repeat family member, differentially
RT expressed in human gastric adenocarcinoma: effects on ploidy,
RT chromosomal stability, cell adhesion/migration and tumorigenicity.";
RL Oncogene 23:5056-5067(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Stomach;
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis, and Uterus;
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
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,
RA Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in
RT signaling networks.";
RL Cell 127:635-648(2006).
CC -!- FUNCTION: Required for depolarization-dependent survival of
CC cultured cerebellar granule neurons. May mediate homophilic as
CC well as heterophilic cell-cell interaction with AMIGO1 or AMIGO3.
CC May contribute to signal transduction through its intracellular
CC domain. May be required for tumorigenesis of a subset of gastric
CC adenocarcinomas.
CC -!- SUBUNIT: Binds itself as well as AMIGO1 and AMIGO3 (By
CC similarity).
CC -!- INTERACTION:
CC O00555:CACNA1A; NbExp=2; IntAct=EBI-3866830, EBI-766279;
CC -!- SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane
CC protein (By similarity). Nucleus (By similarity). Note=Associated
CC with nucleus as well as plasma membrane. Restricted to somata of
CC cerebellar as well as hippocampal neurons (By similarity).
CC -!- TISSUE SPECIFICITY: Highest levels in breast, ovary, cervix, and
CC uterus. Lower levels in lung, colon, and rectum. Differentially
CC expressed in 56% of thyroid, 57% of pancreatic and 45% of stomach
CC cancers.
CC -!- SIMILARITY: Belongs to the immunoglobulin superfamily. AMIGO
CC family.
CC -!- SIMILARITY: Contains 1 Ig-like C2-type (immunoglobulin-like)
CC domain.
CC -!- SIMILARITY: Contains 6 LRR (leucine-rich) repeats.
CC -!- SIMILARITY: Contains 1 LRRCT domain.
CC -!- SIMILARITY: Contains 1 LRRNT domain.
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; AY237005; AAO48946.1; -; mRNA.
DR EMBL; AB079074; BAC81188.1; -; mRNA.
DR EMBL; AB080610; BAC81189.1; -; mRNA.
DR EMBL; AY454159; AAR83271.1; -; mRNA.
DR EMBL; AL833007; CAH56293.1; -; mRNA.
DR EMBL; BC014103; AAH14103.2; -; mRNA.
DR EMBL; BC047595; AAH47595.1; -; mRNA.
DR EMBL; BC095477; AAH95477.1; -; mRNA.
DR RefSeq; NP_001137140.1; NM_001143668.1.
DR RefSeq; NP_862830.1; NM_181847.4.
DR RefSeq; XP_005268894.1; XM_005268837.1.
DR UniGene; Hs.121520; -.
DR ProteinModelPortal; Q86SJ2; -.
DR SMR; Q86SJ2; 41-387.
DR IntAct; Q86SJ2; 1.
DR STRING; 9606.ENSP00000266581; -.
DR DMDM; 68052338; -.
DR PaxDb; Q86SJ2; -.
DR PeptideAtlas; Q86SJ2; -.
DR PRIDE; Q86SJ2; -.
DR Ensembl; ENST00000266581; ENSP00000266581; ENSG00000139211.
DR Ensembl; ENST00000321382; ENSP00000320848; ENSG00000139211.
DR Ensembl; ENST00000429635; ENSP00000406020; ENSG00000139211.
DR Ensembl; ENST00000550413; ENSP00000449034; ENSG00000139211.
DR GeneID; 347902; -.
DR KEGG; hsa:347902; -.
DR UCSC; uc001rpk.3; human.
DR CTD; 347902; -.
DR GeneCards; GC12M047469; -.
DR HGNC; HGNC:24073; AMIGO2.
DR HPA; HPA054004; -.
DR neXtProt; NX_Q86SJ2; -.
DR PharmGKB; PA142672626; -.
DR eggNOG; NOG146733; -.
DR HOGENOM; HOG000231327; -.
DR HOVERGEN; HBG080231; -.
DR InParanoid; Q86SJ2; -.
DR OMA; SCIAMNR; -.
DR OrthoDB; EOG71CFKP; -.
DR PhylomeDB; Q86SJ2; -.
DR GenomeRNAi; 347902; -.
DR NextBio; 99311; -.
DR PRO; PR:Q86SJ2; -.
DR ArrayExpress; Q86SJ2; -.
DR Bgee; Q86SJ2; -.
DR CleanEx; HS_AMIGO2; -.
DR Genevestigator; Q86SJ2; -.
DR GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0007157; P:heterophilic cell-cell adhesion; ISS:UniProtKB.
DR GO; GO:0007156; P:homophilic cell adhesion; ISS:UniProtKB.
DR GO; GO:0043066; P:negative regulation of apoptotic process; IEA:Ensembl.
DR GO; GO:0043069; P:negative regulation of programmed cell death; ISS:UniProtKB.
DR Gene3D; 2.60.40.10; -; 1.
DR InterPro; IPR000483; Cys-rich_flank_reg_C.
DR InterPro; IPR007110; Ig-like_dom.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR003599; Ig_sub.
DR InterPro; IPR001611; Leu-rich_rpt.
DR InterPro; IPR003591; Leu-rich_rpt_typical-subtyp.
DR InterPro; IPR000372; LRR-contain_N.
DR Pfam; PF00560; LRR_1; 1.
DR SMART; SM00409; IG; 1.
DR SMART; SM00369; LRR_TYP; 1.
DR SMART; SM00082; LRRCT; 1.
DR SMART; SM00013; LRRNT; 1.
DR PROSITE; PS50835; IG_LIKE; 1.
DR PROSITE; PS51450; LRR; 7.
PE 1: Evidence at protein level;
KW Cell adhesion; Cell membrane; Complete proteome; Disulfide bond;
KW Glycoprotein; Immunoglobulin domain; Leucine-rich repeat; Membrane;
KW Nucleus; Reference proteome; Repeat; Signal; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1 39 Potential.
FT CHAIN 40 522 Amphoterin-induced protein 2.
FT /FTId=PRO_0000014509.
FT TOPO_DOM 40 398 Extracellular (Potential).
FT TRANSMEM 399 419 Helical; (Potential).
FT TOPO_DOM 420 522 Cytoplasmic (Potential).
FT DOMAIN 40 68 LRRNT.
FT REPEAT 69 90 LRR 1.
FT REPEAT 94 115 LRR 2.
FT REPEAT 118 139 LRR 3.
FT REPEAT 142 163 LRR 4.
FT REPEAT 166 187 LRR 5.
FT REPEAT 193 214 LRR 6.
FT DOMAIN 228 284 LRRCT.
FT DOMAIN 289 379 Ig-like C2-type.
FT CARBOHYD 58 58 N-linked (GlcNAc...) (Potential).
FT CARBOHYD 104 104 N-linked (GlcNAc...) (Potential).
FT CARBOHYD 281 281 N-linked (GlcNAc...) (Potential).
FT CARBOHYD 288 288 N-linked (GlcNAc...) (Potential).
FT CARBOHYD 345 345 N-linked (GlcNAc...) (Potential).
FT CARBOHYD 373 373 N-linked (GlcNAc...) (Potential).
FT CARBOHYD 381 381 N-linked (GlcNAc...) (Potential).
FT CARBOHYD 384 384 N-linked (GlcNAc...) (Potential).
FT DISULFID 41 47 By similarity.
FT DISULFID 45 54 By similarity.
FT DISULFID 232 260 By similarity.
FT DISULFID 234 282 By similarity.
FT DISULFID 310 363 By similarity.
SQ SEQUENCE 522 AA; 57934 MW; 20A86E3D82C05B9B CRC64;
MSLRVHTLPT LLGAVVRPGC RELLCLLMIT VTVGPGASGV CPTACICATD IVSCTNKNLS
KVPGNLFRLI KRLDLSYNRI GLLDSEWIPV SFAKLNTLIL RHNNITSIST GSFSTTPNLK
CLDLSSNKLK TVKNAVFQEL KVLEVLLLYN NHISYLDPSA FGGLSQLQKL YLSGNFLTQF
PMDLYVGRFK LAELMFLDVS YNRIPSMPMH HINLVPGKQL RGIYLHGNPF VCDCSLYSLL
VFWYRRHFSS VMDFKNDYTC RLWSDSRHSR QVLLLQDSFM NCSDSIINGS FRALGFIHEA
QVGERLMVHC DSKTGNANTD FIWVGPDNRL LEPDKEMENF YVFHNGSLVI ESPRFEDAGV
YSCIAMNKQR LLNETVDVTI NVSNFTVSRS HAHEAFNTAF TTLAACVASI VLVLLYLYLT
PCPCKCKTKR QKNMLHQSNA HSSILSPGPA SDASADERKA GAGKRVVFLE PLKDTAAGQN
GKVRLFPSEA VIAEGILKST RGKSDSDSVN SVFSDTPFVA ST
//