ADA29_HUMAN
ID ADA29_HUMAN Reviewed; 820 AA.
AC Q9UKF5; Q4W5F3; Q9UHP1; Q9UKF3; Q9UKF4;
DT 20-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT 17-APR-2007, sequence version 3.
DT 03-AUG-2022, entry version 187.
DE RecName: Full=Disintegrin and metalloproteinase domain-containing protein 29;
DE Short=ADAM 29;
DE AltName: Full=Cancer/testis antigen 73;
DE Short=CT73;
DE Flags: Precursor;
GN Name=ADAM29;
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] (ISOFORMS ALPHA; BETA AND GAMMA).
RC TISSUE=Testis;
RX PubMed=10512762; DOI=10.1006/bbrc.1999.1322;
RA Cerretti D.P., DuBose R.F., Black R.A., Nelson N.;
RT "Isolation of two novel metalloproteinase-disintegrin (ADAM) cDNAs that
RT show testis-specific gene expression.";
RL Biochem. Biophys. Res. Commun. 263:810-815(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM ALPHA).
RC TISSUE=Testis;
RX PubMed=10644455; DOI=10.1006/geno.1999.6029;
RA Xu R., Cai J., Xu T., Zhou W., Ying B., Deng K., Zhao S., Li C.;
RT "Molecular cloning and mapping of a novel ADAM gene (ADAM29) to human
RT chromosome 4.";
RL Genomics 62:537-539(1999).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM ALPHA).
RC TISSUE=Testis;
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
RA Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT 4.";
RL Nature 434:724-731(2005).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton 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 [6]
RP INVOLVEMENT IN CUTANEOUS MELANOMA, VARIANTS PHE-72; MET-89; LYS-111;
RP PHE-112; PHE-115; ASN-131; LYS-176; PHE-234; PHE-257; GLU-305; ASN-345;
RP ASP-403; ASP-434; LYS-503 AND TYR-533, AND CHARACTERIZATION OF VARIANTS
RP LYS-111; PHE-112; PHE-115; PHE-257; ASP-434 AND LYS-503.
RX PubMed=21618342; DOI=10.1002/humu.21477;
RA Wei X., Moncada-Pazos A., Cal S., Soria-Valles C., Gartner J., Rudloff U.,
RA Lin J.C., Rosenberg S.A., Lopez-Otin C., Samuels Y.;
RT "Analysis of the disintegrin-metalloproteinases family reveals ADAM29 and
RT ADAM7 are often mutated in melanoma.";
RL Hum. Mutat. 32:E2148-E2175(2011).
RN [7]
RP VARIANTS [LARGE SCALE ANALYSIS] LEU-31 AND ILE-205.
RX PubMed=16959974; DOI=10.1126/science.1133427;
RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P.,
RA Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V.,
RA Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H.,
RA Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W.,
RA Velculescu V.E.;
RT "The consensus coding sequences of human breast and colorectal cancers.";
RL Science 314:268-274(2006).
CC -!- FUNCTION: May be involved in spermatogenesis and fertilization. Seems
CC to be a non catalytic metalloprotease-like protein.
CC -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=Alpha;
CC IsoId=Q9UKF5-1; Sequence=Displayed;
CC Name=Beta;
CC IsoId=Q9UKF5-2; Sequence=VSP_005491;
CC Name=Gamma;
CC IsoId=Q9UKF5-3; Sequence=VSP_005492, VSP_005493;
CC -!- TISSUE SPECIFICITY: Expressed specifically in testes.
CC -!- DISEASE: Note=Has been found to be frequently mutated in melanoma.
CC ADAM7 mutations may play a role in melanoma progression and metastasis.
CC {ECO:0000269|PubMed:21618342}.
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; AF171929; AAF03777.1; -; mRNA.
DR EMBL; AF171930; AAF03778.1; -; mRNA.
DR EMBL; AF171931; AAF03779.1; -; mRNA.
DR EMBL; AF134708; AAF22163.1; -; mRNA.
DR EMBL; AK292410; BAF85099.1; -; mRNA.
DR EMBL; AC105914; AAY41055.1; -; Genomic_DNA.
DR EMBL; CH471056; EAX04727.1; -; Genomic_DNA.
DR EMBL; CH471056; EAX04728.1; -; Genomic_DNA.
DR CCDS; CCDS3823.1; -. [Q9UKF5-1]
DR RefSeq; NP_001124175.1; NM_001130703.1. [Q9UKF5-1]
DR RefSeq; NP_001124176.1; NM_001130704.1. [Q9UKF5-1]
DR RefSeq; NP_001124177.1; NM_001130705.1. [Q9UKF5-1]
DR RefSeq; NP_001265054.1; NM_001278125.1. [Q9UKF5-1]
DR RefSeq; NP_001265055.1; NM_001278126.1. [Q9UKF5-1]
DR RefSeq; NP_001265056.1; NM_001278127.1. [Q9UKF5-1]
DR RefSeq; NP_055084.3; NM_014269.4. [Q9UKF5-1]
DR RefSeq; XP_011529858.1; XM_011531556.1. [Q9UKF5-1]
DR RefSeq; XP_011529859.1; XM_011531557.1. [Q9UKF5-1]
DR RefSeq; XP_011529861.1; XM_011531559.1. [Q9UKF5-1]
DR RefSeq; XP_011529862.1; XM_011531560.1. [Q9UKF5-1]
DR RefSeq; XP_011529863.1; XM_011531561.1. [Q9UKF5-1]
DR AlphaFoldDB; Q9UKF5; -.
DR SMR; Q9UKF5; -.
DR BioGRID; 116268; 1.
DR IntAct; Q9UKF5; 1.
DR STRING; 9606.ENSP00000484862; -.
DR MEROPS; M12.981; -.
DR GlyGen; Q9UKF5; 9 sites.
DR iPTMnet; Q9UKF5; -.
DR PhosphoSitePlus; Q9UKF5; -.
DR BioMuta; ADAM29; -.
DR DMDM; 145559438; -.
DR MassIVE; Q9UKF5; -.
DR MaxQB; Q9UKF5; -.
DR PaxDb; Q9UKF5; -.
DR PeptideAtlas; Q9UKF5; -.
DR PRIDE; Q9UKF5; -.
DR ProteomicsDB; 84779; -. [Q9UKF5-1]
DR ProteomicsDB; 84780; -. [Q9UKF5-2]
DR ProteomicsDB; 84781; -. [Q9UKF5-3]
DR Antibodypedia; 2608; 93 antibodies from 27 providers.
DR DNASU; 11086; -.
DR Ensembl; ENST00000359240.7; ENSP00000352177.3; ENSG00000168594.15. [Q9UKF5-1]
DR Ensembl; ENST00000404450.8; ENSP00000384229.3; ENSG00000168594.15. [Q9UKF5-1]
DR Ensembl; ENST00000445694.5; ENSP00000414544.1; ENSG00000168594.15. [Q9UKF5-1]
DR Ensembl; ENST00000514159.1; ENSP00000423517.1; ENSG00000168594.15. [Q9UKF5-1]
DR Ensembl; ENST00000615367.4; ENSP00000484862.1; ENSG00000168594.15. [Q9UKF5-1]
DR Ensembl; ENST00000618444.1; ENSP00000478469.1; ENSG00000168594.15. [Q9UKF5-1]
DR GeneID; 11086; -.
DR KEGG; hsa:11086; -.
DR MANE-Select; ENST00000359240.7; ENSP00000352177.3; NM_014269.4; NP_055084.3.
DR UCSC; uc003iuc.3; human. [Q9UKF5-1]
DR CTD; 11086; -.
DR DisGeNET; 11086; -.
DR GeneCards; ADAM29; -.
DR HGNC; HGNC:207; ADAM29.
DR HPA; ENSG00000168594; Tissue enriched (testis).
DR MIM; 604778; gene.
DR neXtProt; NX_Q9UKF5; -.
DR OpenTargets; ENSG00000168594; -.
DR PharmGKB; PA24524; -.
DR VEuPathDB; HostDB:ENSG00000168594; -.
DR eggNOG; KOG3607; Eukaryota.
DR GeneTree; ENSGT00940000163394; -.
DR HOGENOM; CLU_012714_4_0_1; -.
DR InParanoid; Q9UKF5; -.
DR OMA; TSHMCPD; -.
DR PhylomeDB; Q9UKF5; -.
DR TreeFam; TF314733; -.
DR PathwayCommons; Q9UKF5; -.
DR BioGRID-ORCS; 11086; 9 hits in 1070 CRISPR screens.
DR ChiTaRS; ADAM29; human.
DR GenomeRNAi; 11086; -.
DR Pharos; Q9UKF5; Tbio.
DR PRO; PR:Q9UKF5; -.
DR Proteomes; UP000005640; Chromosome 4.
DR RNAct; Q9UKF5; protein.
DR Bgee; ENSG00000168594; Expressed in sperm and 79 other tissues.
DR ExpressionAtlas; Q9UKF5; baseline and differential.
DR Genevisible; Q9UKF5; HS.
DR GO; GO:0009897; C:external side of plasma membrane; IBA:GO_Central.
DR GO; GO:0005887; C:integral component of plasma membrane; TAS:ProtInc.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:1990913; C:sperm head plasma membrane; IBA:GO_Central.
DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR GO; GO:0008237; F:metallopeptidase activity; TAS:ProtInc.
DR GO; GO:0008584; P:male gonad development; IBA:GO_Central.
DR GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR GO; GO:0007283; P:spermatogenesis; TAS:ProtInc.
DR CDD; cd04269; ZnMc_adamalysin_II_like; 1.
DR Gene3D; 3.40.390.10; -; 1.
DR Gene3D; 4.10.70.10; -; 1.
DR InterPro; IPR006586; ADAM_Cys-rich.
DR InterPro; IPR018358; Disintegrin_CS.
DR InterPro; IPR001762; Disintegrin_dom.
DR InterPro; IPR036436; Disintegrin_dom_sf.
DR InterPro; IPR024079; MetalloPept_cat_dom_sf.
DR InterPro; IPR001590; Peptidase_M12B.
DR InterPro; IPR002870; Peptidase_M12B_N.
DR InterPro; IPR034027; Reprolysin_adamalysin.
DR Pfam; PF08516; ADAM_CR; 1.
DR Pfam; PF00200; Disintegrin; 1.
DR Pfam; PF01562; Pep_M12B_propep; 1.
DR Pfam; PF01421; Reprolysin; 1.
DR PRINTS; PR00289; DISINTEGRIN.
DR SMART; SM00608; ACR; 1.
DR SMART; SM00050; DISIN; 1.
DR SUPFAM; SSF57552; SSF57552; 1.
DR PROSITE; PS50215; ADAM_MEPRO; 1.
DR PROSITE; PS00427; DISINTEGRIN_1; 1.
DR PROSITE; PS50214; DISINTEGRIN_2; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Disulfide bond; EGF-like domain; Glycoprotein;
KW Membrane; Reference proteome; Repeat; Signal; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..18
FT /evidence="ECO:0000255"
FT PROPEP 19..193
FT /evidence="ECO:0000250"
FT /id="PRO_0000029134"
FT CHAIN 194..820
FT /note="Disintegrin and metalloproteinase domain-containing
FT protein 29"
FT /id="PRO_0000029135"
FT TOPO_DOM 194..674
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 675..695
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 696..820
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 198..390
FT /note="Peptidase M12B"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00276"
FT DOMAIN 397..483
FT /note="Disintegrin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00068"
FT DOMAIN 625..654
FT /note="EGF-like"
FT REPEAT 739..747
FT /note="1"
FT REPEAT 748..756
FT /note="2"
FT REPEAT 757..765
FT /note="3"
FT REPEAT 766..774
FT /note="4"
FT REPEAT 775..783
FT /note="5"
FT REPEAT 784..792
FT /note="6"
FT REPEAT 793..801
FT /note="7"
FT REPEAT 802..810
FT /note="8"
FT REPEAT 811..819
FT /note="9"
FT REGION 706..820
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 739..819
FT /note="9 X 9 AA approximate repeats"
FT COMPBIAS 706..726
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 742..811
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 217
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 320
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 368
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 428
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 469
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 538
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 545
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 558
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 564
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 307..384
FT /evidence="ECO:0000250"
FT DISULFID 347..369
FT /evidence="ECO:0000250"
FT DISULFID 349..354
FT /evidence="ECO:0000250"
FT DISULFID 455..475
FT /evidence="ECO:0000250"
FT DISULFID 625..636
FT /evidence="ECO:0000250"
FT DISULFID 630..642
FT /evidence="ECO:0000250"
FT DISULFID 644..653
FT /evidence="ECO:0000250"
FT VAR_SEQ 750..803
FT /note="Missing (in isoform Beta)"
FT /evidence="ECO:0000303|PubMed:10512762"
FT /id="VSP_005491"
FT VAR_SEQ 763..787
FT /note="VTPSQSQPRVMPSQSQPPVMPSQSH -> QNLFLFSFSISDCVLNFRLLYLQ
FT AT (in isoform Gamma)"
FT /evidence="ECO:0000303|PubMed:10512762"
FT /id="VSP_005492"
FT VAR_SEQ 788..820
FT /note="Missing (in isoform Gamma)"
FT /evidence="ECO:0000303|PubMed:10512762"
FT /id="VSP_005493"
FT VARIANT 31
FT /note="P -> L (in a colorectal cancer sample; somatic
FT mutation; dbSNP:rs544557652)"
FT /evidence="ECO:0000269|PubMed:16959974"
FT /id="VAR_036148"
FT VARIANT 72
FT /note="L -> F (in a melanoma cell line)"
FT /evidence="ECO:0000269|PubMed:21618342"
FT /id="VAR_066322"
FT VARIANT 89
FT /note="I -> M (in a cutaneous metastatic melanoma sample;
FT somatic mutation)"
FT /evidence="ECO:0000269|PubMed:21618342"
FT /id="VAR_066323"
FT VARIANT 111
FT /note="E -> K (in a cutaneous metastatic melanoma sample;
FT somatic mutation; increases the adhesion of melanoma cells
FT to collagens I and IV; dbSNP:rs267600087)"
FT /evidence="ECO:0000269|PubMed:21618342"
FT /id="VAR_066324"
FT VARIANT 112
FT /note="S -> F (in a cutaneous metastatic melanoma sample;
FT somatic mutation; increases the adhesion of melanoma cells
FT to collagens I and IV)"
FT /evidence="ECO:0000269|PubMed:21618342"
FT /id="VAR_066325"
FT VARIANT 115
FT /note="S -> F (in a cutaneous metastatic melanoma sample;
FT somatic mutation; increases the adhesion of melanoma cells
FT to collagens I and IV)"
FT /evidence="ECO:0000269|PubMed:21618342"
FT /id="VAR_066326"
FT VARIANT 131
FT /note="D -> N (in a cutaneous metastatic melanoma sample;
FT somatic mutation)"
FT /evidence="ECO:0000269|PubMed:21618342"
FT /id="VAR_066327"
FT VARIANT 176
FT /note="E -> K (in a cutaneous metastatic melanoma sample;
FT somatic mutation; dbSNP:rs899870236)"
FT /evidence="ECO:0000269|PubMed:21618342"
FT /id="VAR_066328"
FT VARIANT 205
FT /note="V -> I (in a colorectal cancer sample; somatic
FT mutation; dbSNP:rs772388824)"
FT /evidence="ECO:0000269|PubMed:16959974"
FT /id="VAR_036149"
FT VARIANT 234
FT /note="S -> F (in a cutaneous metastatic melanoma sample;
FT somatic mutation; dbSNP:rs866380131)"
FT /evidence="ECO:0000269|PubMed:21618342"
FT /id="VAR_066329"
FT VARIANT 257
FT /note="I -> F (in a cutaneous metastatic melanoma sample;
FT somatic mutation; increases the adhesion of melanoma cells
FT to collagens I and IV; dbSNP:rs140083180)"
FT /evidence="ECO:0000269|PubMed:21618342"
FT /id="VAR_066330"
FT VARIANT 305
FT /note="G -> E (in a cutaneous metastatic melanoma sample;
FT somatic mutation; dbSNP:rs267600089)"
FT /evidence="ECO:0000269|PubMed:21618342"
FT /id="VAR_066331"
FT VARIANT 345
FT /note="D -> N (in a cutaneous metastatic melanoma sample;
FT somatic mutation; dbSNP:rs267600090)"
FT /evidence="ECO:0000269|PubMed:21618342"
FT /id="VAR_066332"
FT VARIANT 403
FT /note="G -> D (in a cutaneous metastatic melanoma sample;
FT somatic mutation; dbSNP:rs150047888)"
FT /evidence="ECO:0000269|PubMed:21618342"
FT /id="VAR_066333"
FT VARIANT 434
FT /note="G -> D (in a cutaneous metastatic melanoma sample;
FT somatic mutation; increases the adhesion of melanoma cells
FT to collagens I and IV; dbSNP:rs267600091)"
FT /evidence="ECO:0000269|PubMed:21618342"
FT /id="VAR_066334"
FT VARIANT 503
FT /note="E -> K (in a cutaneous metastatic melanoma sample;
FT somatic mutation; increases the adhesion of melanoma cells
FT to collagens I and IV)"
FT /evidence="ECO:0000269|PubMed:21618342"
FT /id="VAR_066335"
FT VARIANT 533
FT /note="H -> Y (in a cutaneous metastatic melanoma sample;
FT somatic mutation; dbSNP:rs267600093)"
FT /evidence="ECO:0000269|PubMed:21618342"
FT /id="VAR_066336"
FT CONFLICT 196
FT /note="H -> Y (in Ref. 2; AAF22163)"
FT /evidence="ECO:0000305"
FT CONFLICT 744
FT /note="P -> H (in Ref. 2; AAF22163)"
FT /evidence="ECO:0000305"
FT CONFLICT 748
FT /note="S -> Y (in Ref. 2; AAF22163)"
FT /evidence="ECO:0000305"
FT CONFLICT 753
FT /note="Q -> R (in Ref. 1; AAF03777)"
FT /evidence="ECO:0000305"
FT CONFLICT 764
FT /note="T -> M (in Ref. 1; AAF03777)"
FT /evidence="ECO:0000305"
FT CONFLICT 769..773
FT /note="QPRVM -> HPQLT (in Ref. 1; AAF03777)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 820 AA; 92759 MW; AA2FB11342A884C9 CRC64;
MKMLLLLHCL GVFLSCSGHI QDEHPQYHSP PDVVIPVRIT GTTRGMTPPG WLSYILPFGG
QKHIIHIKVK KLLFSKHLPV FTYTDQGAIL EDQPFVQNNC YYHGYVEGDP ESLVSLSTCF
GGFQGILQIN DFAYEIKPLA FSTTFEHLVY KMDSEEKQFS TMRSGFMQNE ITCRMEFEEI
DNSTQKQSSY VGWWIHFRIV EIVVVIDNYL YIRYERNDSK LLEDLYVIVN IVDSILDVIG
VKVLLFGLEI WTNKNLIVVD DVRKSVHLYC KWKSENITPR MQHDTSHLFT TLGLRGLSGI
GAFRGMCTPH RSCAIVTFMN KTLGTFSIAV AHHLGHNLGM NHDEDTCRCS QPRCIMHEGN
PPITKFSNCS YGDFWEYTVE RTKCLLETVH TKDIFNVKRC GNGVVEEGEE CDCGPLKHCA
KDPCCLSNCT LTDGSTCAFG LCCKDCKFLP SGKVCRKEVN ECDLPEWCNG TSHKCPDDFY
VEDGIPCKER GYCYEKSCHD RNEQCRRIFG AGANTASETC YKELNTLGDR VGHCGIKNAT
YIKCNISDVQ CGRIQCENVT EIPNMSDHTT VHWARFNDIM CWSTDYHLGM KGPDIGEVKD
GTECGIDHIC IHRHCVHITI LNSNCSPAFC NKRGICNNKH HCHCNYLWDP PNCLIKGYGG
SVDSGPPPKR KKKKKFCYLC ILLLIVLFIL LCCLYRLCKK SKPIKKQQDV QTPSAKEEEK
IQRRPHELPP QSQPWVMPSQ SQPPVTPSQS HPQVMPSQSQ PPVTPSQSQP RVMPSQSQPP
VMPSQSHPQL TPSQSQPPVT PSQRQPQLMP SQSQPPVTPS