Full text data of A2ML1
A2ML1
(CPAMD9)
[Confidence: low (only semi-automatic identification from reviews)]
Alpha-2-macroglobulin-like protein 1 (C3 and PZP-like alpha-2-macroglobulin domain-containing protein 9; Flags: Precursor)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
Alpha-2-macroglobulin-like protein 1 (C3 and PZP-like alpha-2-macroglobulin domain-containing protein 9; Flags: Precursor)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
A8K2U0
ID A2ML1_HUMAN Reviewed; 1454 AA.
AC A8K2U0; B5MDD1; Q2M224; Q6ZW52; Q6ZW53; Q8N1M4; Q96LQ8;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
read moreDT 05-OCT-2010, sequence version 3.
DT 22-JAN-2014, entry version 50.
DE RecName: Full=Alpha-2-macroglobulin-like protein 1;
DE AltName: Full=C3 and PZP-like alpha-2-macroglobulin domain-containing protein 9;
DE Flags: Precursor;
GN Name=A2ML1; Synonyms=CPAMD9;
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 [LARGE SCALE MRNA], AND VARIANTS GLU-850 AND
RP ARG-1229.
RC TISSUE=Brain, and Tongue;
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.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA 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.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., 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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANTS GLU-850 AND
RP ARG-1229.
RC TISSUE=Cervix;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16541075; DOI=10.1038/nature04569;
RA Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y.,
RA Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C.,
RA Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M.,
RA Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L.,
RA Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B.,
RA Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D.,
RA Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z.,
RA Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z.,
RA Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H.,
RA Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H.,
RA Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V.,
RA Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J.,
RA Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A.,
RA Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M.,
RA Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E.,
RA Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K.,
RA Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D.,
RA Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M.,
RA Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R.,
RA Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J.,
RA Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C.,
RA Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M.,
RA Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M.,
RA Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P.,
RA Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L.,
RA Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E.,
RA Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C.,
RA Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F.,
RA Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M.,
RA Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S.,
RA Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J.,
RA Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A.,
RA Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M.,
RA Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I.,
RA Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A.,
RA Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D.,
RA Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I.,
RA Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T.,
RA Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S.,
RA Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D.,
RA Kucherlapati R., Weinstock G., Gibbs R.A.;
RT "The finished DNA sequence of human chromosome 12.";
RL Nature 440:346-351(2006).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1290-1454.
RC TISSUE=Brain;
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 [5]
RP FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND
RP DEVELOPMENTAL STAGE.
RX PubMed=16298998; DOI=10.1074/jbc.M508017200;
RA Galliano M.-F., Toulza E., Gallinaro H., Jonca N., Ishida-Yamamoto A.,
RA Serre G., Guerrin M.;
RT "A novel protease inhibitor of the alpha2-macroglobulin family
RT expressed in the human epidermis.";
RL J. Biol. Chem. 281:5780-5789(2006).
CC -!- FUNCTION: Is able to inhibit all four classes of proteinases by a
CC unique 'trapping' mechanism. This protein has a peptide stretch,
CC called the 'bait region' which contains specific cleavage sites
CC for different proteinases. When a proteinase cleaves the bait
CC region, a conformational change is induced in the protein which
CC traps the proteinase. The entrapped enzyme remains active against
CC low molecular weight substrates (activity against high molecular
CC weight substrates is greatly reduced). Following cleavage in the
CC bait region a thioester bond is hydrolyzed and mediates the
CC covalent binding of the protein to the proteinase (By similarity).
CC Displays inhibitory activity against chymotrypsin, papain,
CC thermolysin, subtilisin A and, to a lesser extent, elastase but
CC not trypsin. May play an important role during desquamation by
CC inhibiting extracellular proteases.
CC -!- SUBUNIT: Monomer.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- TISSUE SPECIFICITY: In the epidermis, expressed predominantly in
CC the granular layer at the apical edge of keratinocytes (at protein
CC level). Also detected in placenta, testis and thymus but not in
CC epithelia of kidney, lung, small intestine or colon.
CC -!- DEVELOPMENTAL STAGE: Up-regulated during keratinocyte
CC differentiation.
CC -!- SIMILARITY: Belongs to the protease inhibitor I39 (alpha-2-
CC macroglobulin) family.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB71612.1; Type=Erroneous initiation;
CC Sequence=BAC04793.1; Type=Erroneous initiation;
CC Sequence=BAC85653.1; Type=Erroneous initiation;
CC Sequence=BAC85654.1; Type=Erroneous initiation;
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; AK057908; BAB71612.1; ALT_INIT; mRNA.
DR EMBL; AK096448; BAC04793.1; ALT_INIT; mRNA.
DR EMBL; AK123591; BAC85653.1; ALT_INIT; mRNA.
DR EMBL; AK123592; BAC85654.1; ALT_INIT; mRNA.
DR EMBL; AK290355; BAF83044.1; -; mRNA.
DR EMBL; AL832139; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AC006513; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC006581; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC093840; AAH93840.2; -; mRNA.
DR EMBL; BC112131; AAI12132.1; -; mRNA.
DR UniGene; Hs.620532; -.
DR ProteinModelPortal; A8K2U0; -.
DR STRING; 9606.ENSP00000299698; -.
DR MEROPS; I39.007; -.
DR PhosphoSite; A8K2U0; -.
DR PaxDb; A8K2U0; -.
DR PRIDE; A8K2U0; -.
DR Ensembl; ENST00000299698; ENSP00000299698; ENSG00000166535.
DR UCSC; uc001quz.5; human.
DR GeneCards; GC12P008975; -.
DR HGNC; HGNC:23336; A2ML1.
DR HPA; HPA038848; -.
DR MIM; 610627; gene.
DR neXtProt; NX_A8K2U0; -.
DR eggNOG; COG2373; -.
DR HOVERGEN; HBG000039; -.
DR OMA; ATGIVAW; -.
DR OrthoDB; EOG7DJSKB; -.
DR ChiTaRS; A2ML1; human.
DR PRO; PR:A8K2U0; -.
DR ArrayExpress; A8K2U0; -.
DR Bgee; A8K2U0; -.
DR CleanEx; HS_A2ML1; -.
DR Genevestigator; A8K2U0; -.
DR GO; GO:0005615; C:extracellular space; IDA:UniProtKB.
DR GO; GO:0030414; F:peptidase inhibitor activity; IDA:UniProtKB.
DR GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; IEA:UniProtKB-KW.
DR GO; GO:0010951; P:negative regulation of endopeptidase activity; IEA:GOC.
DR Gene3D; 2.60.40.690; -; 1.
DR InterPro; IPR009048; A-macroglobulin_rcpt-bd.
DR InterPro; IPR011626; A2M_comp.
DR InterPro; IPR002890; A2M_N.
DR InterPro; IPR011625; A2M_N_2.
DR InterPro; IPR014756; Ig_E-set.
DR InterPro; IPR001599; Macroglobln_a2.
DR InterPro; IPR019742; MacrogloblnA2_CS.
DR InterPro; IPR019565; MacrogloblnA2_thiol-ester-bond.
DR InterPro; IPR008930; Terpenoid_cyclase/PrenylTrfase.
DR Pfam; PF00207; A2M; 1.
DR Pfam; PF07678; A2M_comp; 1.
DR Pfam; PF01835; A2M_N; 1.
DR Pfam; PF07703; A2M_N_2; 1.
DR Pfam; PF07677; A2M_recep; 1.
DR Pfam; PF10569; Thiol-ester_cl; 1.
DR SUPFAM; SSF48239; SSF48239; 1.
DR SUPFAM; SSF49410; SSF49410; 1.
DR SUPFAM; SSF81296; SSF81296; 1.
DR PROSITE; PS00477; ALPHA_2_MACROGLOBULIN; 1.
PE 1: Evidence at protein level;
KW Bait region; Complete proteome; Disulfide bond; Glycoprotein;
KW Polymorphism; Protease inhibitor; Reference proteome; Secreted;
KW Serine protease inhibitor; Signal; Thioester bond.
FT SIGNAL 1 17 Potential.
FT CHAIN 18 1454 Alpha-2-macroglobulin-like protein 1.
FT /FTId=PRO_0000318074.
FT REGION 695 726 Bait region.
FT CARBOHYD 120 120 N-linked (GlcNAc...) (Potential).
FT CARBOHYD 281 281 N-linked (GlcNAc...) (Potential).
FT CARBOHYD 409 409 N-linked (GlcNAc...) (Potential).
FT CARBOHYD 857 857 N-linked (GlcNAc...) (Potential).
FT CARBOHYD 1020 1020 N-linked (GlcNAc...) (Potential).
FT DISULFID 40 78 By similarity.
FT DISULFID 241 291 By similarity.
FT DISULFID 259 279 By similarity.
FT DISULFID 464 557 By similarity.
FT DISULFID 589 769 By similarity.
FT DISULFID 819 847 By similarity.
FT DISULFID 845 881 By similarity.
FT DISULFID 919 1307 By similarity.
FT DISULFID 1075 1123 By similarity.
FT DISULFID 1338 1453 By similarity.
FT CROSSLNK 970 973 Isoglutamyl cysteine thioester (Cys-Gln)
FT (By similarity).
FT VARIANT 207 207 G -> R (in dbSNP:rs11047499).
FT /FTId=VAR_055463.
FT VARIANT 850 850 D -> E (in dbSNP:rs1860926).
FT /FTId=VAR_059083.
FT VARIANT 970 970 C -> Y (in dbSNP:rs1558526).
FT /FTId=VAR_055464.
FT VARIANT 1131 1131 T -> M (in dbSNP:rs7959680).
FT /FTId=VAR_055465.
FT VARIANT 1229 1229 H -> R (in dbSNP:rs10219561).
FT /FTId=VAR_059084.
FT VARIANT 1412 1412 T -> A (in dbSNP:rs7315591).
FT /FTId=VAR_055466.
FT CONFLICT 733 733 F -> L (in Ref. 1; BAC85654/BAF83044).
FT CONFLICT 748 748 G -> E (in Ref. 2; AL832139).
FT CONFLICT 1122 1122 R -> W (in Ref. 1; BAC04793/BAC85653/
FT BAC85654/BAF83044 and 2; AL832139).
FT CONFLICT 1150 1150 M -> I (in Ref. 1; BAF83044).
FT CONFLICT 1248 1248 L -> P (in Ref. 1; BAC85654).
FT CONFLICT 1257 1257 M -> V (in Ref. 1; BAC04793/BAC85653/
FT BAC85654/BAF83044 and 2; AL832139).
FT CONFLICT 1452 1452 P -> L (in Ref. 2; AL832139).
SQ SEQUENCE 1454 AA; 161107 MW; 15ED65D000834E33 CRC64;
MWAQLLLGML ALSPAIAEEL PNYLVTLPAR LNFPSVQKVC LDLSPGYSDV KFTVTLETKD
KTQKLLEYSG LKKRHLHCIS FLVPPPAGGT EEVATIRVSG VGNNISFEEK KKVLIQRQGN
GTFVQTDKPL YTPGQQVYFR IVTMDSNFVP VNDKYSMVEL QDPNSNRIAQ WLEVVPEQGI
VDLSFQLAPE AMLGTYTVAV AEGKTFGTFS VEEYVLPKFK VEVVEPKELS TVQESFLVKI
CCRYTYGKPM LGAVQVSVCQ KANTYWYREV EREQLPDKCR NLSGQTDKTG CFSAPVDMAT
FDLIGYAYSH QINIVATVVE EGTGVEANAT QNIYISPQMG SMTFEDTSNF YHPNFPFSGK
IRVRGHDDSF LKNHLVFLVI YGTNGTFNQT LVTDNNGLAP FTLETSGWNG TDVSLEGKFQ
MEDLVYNPEQ VPRYYQNAYL HLRPFYSTTR SFLGIHRLNG PLKCGQPQEV LVDYYIDPAD
ASPDQEISFS YYLIGKGSLV MEGQKHLNSK KKGLKASFSL SLTFTSRLAP DPSLVIYAIF
PSGGVVADKI QFSVEMCFDN QVSLGFSPSQ QLPGAEVELQ LQAAPGSLCA LRAVDESVLL
LRPDRELSNR SVYGMFPFWY GHYPYQVAEY DQCPVSGPWD FPQPLIDPMP QGHSSQRSII
WRPSFSEGTD LFSFFRDVGL KILSNAKIKK PVDCSHRSPE YSTAMGAGGG HPEAFESSTP
LHQAEDSQVR QYFPETWLWD LFPIGNSGKE AVHVTVPDAI TEWKAMSFCT SQSRGFGLSP
TVGLTAFKPF FVDLTLPYSV VRGESFRLTA TIFNYLKDCI RVQTDLAKSH EYQLESWADS
QTSSCLCADD AKTHHWNITA VKLGHINFTI STKILDSNEP CGGQKGFVPQ KGRSDTLIKP
VLVKPEGVLV EKTHSSLLCP KGKVASESVS LELPVDIVPD STKAYVTVLG DIMGTALQNL
DGLVQMPSGC GEQNMVLFAP IIYVLQYLEK AGLLTEEIRS RAVGFLEIGY QKELMYKHSN
GSYSAFGERD GNGNTWLTAF VTKCFGQAQK FIFIDPKNIQ DALKWMAGNQ LPSGCYANVG
NLLHTAMKGG VDDEVSLTAY VTAALLEMGK DVDDPMVSQG LRCLKNSATS TTNLYTQALL
AYIFSLAGEM DIRNILLKQL DQQAIISGES IYWSQKPTPS SNASPWSEPA AVDVELTAYA
LLAQLTKPSL TQKEIAKATS IVAWLAKQHN AYGGFSSTQD TVVALQALAK YATTAYMPSE
EINLVVKSTE NFQRTFNIQS VNRLVFQQDT LPNVPGMYTL EASGQGCVYV QTVLRYNILP
PTNMKTFSLS VEIGKARCEQ PTSPRSLTLT IHTSYVGSRS SSNMAIVEVK MLSGFSPMEG
TNQLLLQQPL VKKVEFGTDT LNIYLDELIK NTQTYTFTIS QSVLVTNLKP ATIKVYDYYL
PDEQATIQYS DPCE
//
ID A2ML1_HUMAN Reviewed; 1454 AA.
AC A8K2U0; B5MDD1; Q2M224; Q6ZW52; Q6ZW53; Q8N1M4; Q96LQ8;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
read moreDT 05-OCT-2010, sequence version 3.
DT 22-JAN-2014, entry version 50.
DE RecName: Full=Alpha-2-macroglobulin-like protein 1;
DE AltName: Full=C3 and PZP-like alpha-2-macroglobulin domain-containing protein 9;
DE Flags: Precursor;
GN Name=A2ML1; Synonyms=CPAMD9;
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 [LARGE SCALE MRNA], AND VARIANTS GLU-850 AND
RP ARG-1229.
RC TISSUE=Brain, and Tongue;
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.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA 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.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., 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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANTS GLU-850 AND
RP ARG-1229.
RC TISSUE=Cervix;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16541075; DOI=10.1038/nature04569;
RA Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y.,
RA Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C.,
RA Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M.,
RA Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L.,
RA Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B.,
RA Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D.,
RA Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z.,
RA Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z.,
RA Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H.,
RA Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H.,
RA Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V.,
RA Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J.,
RA Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A.,
RA Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M.,
RA Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E.,
RA Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K.,
RA Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D.,
RA Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M.,
RA Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R.,
RA Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J.,
RA Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C.,
RA Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M.,
RA Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M.,
RA Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P.,
RA Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L.,
RA Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E.,
RA Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C.,
RA Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F.,
RA Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M.,
RA Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S.,
RA Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J.,
RA Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A.,
RA Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M.,
RA Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I.,
RA Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A.,
RA Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D.,
RA Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I.,
RA Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T.,
RA Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S.,
RA Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D.,
RA Kucherlapati R., Weinstock G., Gibbs R.A.;
RT "The finished DNA sequence of human chromosome 12.";
RL Nature 440:346-351(2006).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1290-1454.
RC TISSUE=Brain;
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 [5]
RP FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND
RP DEVELOPMENTAL STAGE.
RX PubMed=16298998; DOI=10.1074/jbc.M508017200;
RA Galliano M.-F., Toulza E., Gallinaro H., Jonca N., Ishida-Yamamoto A.,
RA Serre G., Guerrin M.;
RT "A novel protease inhibitor of the alpha2-macroglobulin family
RT expressed in the human epidermis.";
RL J. Biol. Chem. 281:5780-5789(2006).
CC -!- FUNCTION: Is able to inhibit all four classes of proteinases by a
CC unique 'trapping' mechanism. This protein has a peptide stretch,
CC called the 'bait region' which contains specific cleavage sites
CC for different proteinases. When a proteinase cleaves the bait
CC region, a conformational change is induced in the protein which
CC traps the proteinase. The entrapped enzyme remains active against
CC low molecular weight substrates (activity against high molecular
CC weight substrates is greatly reduced). Following cleavage in the
CC bait region a thioester bond is hydrolyzed and mediates the
CC covalent binding of the protein to the proteinase (By similarity).
CC Displays inhibitory activity against chymotrypsin, papain,
CC thermolysin, subtilisin A and, to a lesser extent, elastase but
CC not trypsin. May play an important role during desquamation by
CC inhibiting extracellular proteases.
CC -!- SUBUNIT: Monomer.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- TISSUE SPECIFICITY: In the epidermis, expressed predominantly in
CC the granular layer at the apical edge of keratinocytes (at protein
CC level). Also detected in placenta, testis and thymus but not in
CC epithelia of kidney, lung, small intestine or colon.
CC -!- DEVELOPMENTAL STAGE: Up-regulated during keratinocyte
CC differentiation.
CC -!- SIMILARITY: Belongs to the protease inhibitor I39 (alpha-2-
CC macroglobulin) family.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB71612.1; Type=Erroneous initiation;
CC Sequence=BAC04793.1; Type=Erroneous initiation;
CC Sequence=BAC85653.1; Type=Erroneous initiation;
CC Sequence=BAC85654.1; Type=Erroneous initiation;
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; AK057908; BAB71612.1; ALT_INIT; mRNA.
DR EMBL; AK096448; BAC04793.1; ALT_INIT; mRNA.
DR EMBL; AK123591; BAC85653.1; ALT_INIT; mRNA.
DR EMBL; AK123592; BAC85654.1; ALT_INIT; mRNA.
DR EMBL; AK290355; BAF83044.1; -; mRNA.
DR EMBL; AL832139; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AC006513; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC006581; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC093840; AAH93840.2; -; mRNA.
DR EMBL; BC112131; AAI12132.1; -; mRNA.
DR UniGene; Hs.620532; -.
DR ProteinModelPortal; A8K2U0; -.
DR STRING; 9606.ENSP00000299698; -.
DR MEROPS; I39.007; -.
DR PhosphoSite; A8K2U0; -.
DR PaxDb; A8K2U0; -.
DR PRIDE; A8K2U0; -.
DR Ensembl; ENST00000299698; ENSP00000299698; ENSG00000166535.
DR UCSC; uc001quz.5; human.
DR GeneCards; GC12P008975; -.
DR HGNC; HGNC:23336; A2ML1.
DR HPA; HPA038848; -.
DR MIM; 610627; gene.
DR neXtProt; NX_A8K2U0; -.
DR eggNOG; COG2373; -.
DR HOVERGEN; HBG000039; -.
DR OMA; ATGIVAW; -.
DR OrthoDB; EOG7DJSKB; -.
DR ChiTaRS; A2ML1; human.
DR PRO; PR:A8K2U0; -.
DR ArrayExpress; A8K2U0; -.
DR Bgee; A8K2U0; -.
DR CleanEx; HS_A2ML1; -.
DR Genevestigator; A8K2U0; -.
DR GO; GO:0005615; C:extracellular space; IDA:UniProtKB.
DR GO; GO:0030414; F:peptidase inhibitor activity; IDA:UniProtKB.
DR GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; IEA:UniProtKB-KW.
DR GO; GO:0010951; P:negative regulation of endopeptidase activity; IEA:GOC.
DR Gene3D; 2.60.40.690; -; 1.
DR InterPro; IPR009048; A-macroglobulin_rcpt-bd.
DR InterPro; IPR011626; A2M_comp.
DR InterPro; IPR002890; A2M_N.
DR InterPro; IPR011625; A2M_N_2.
DR InterPro; IPR014756; Ig_E-set.
DR InterPro; IPR001599; Macroglobln_a2.
DR InterPro; IPR019742; MacrogloblnA2_CS.
DR InterPro; IPR019565; MacrogloblnA2_thiol-ester-bond.
DR InterPro; IPR008930; Terpenoid_cyclase/PrenylTrfase.
DR Pfam; PF00207; A2M; 1.
DR Pfam; PF07678; A2M_comp; 1.
DR Pfam; PF01835; A2M_N; 1.
DR Pfam; PF07703; A2M_N_2; 1.
DR Pfam; PF07677; A2M_recep; 1.
DR Pfam; PF10569; Thiol-ester_cl; 1.
DR SUPFAM; SSF48239; SSF48239; 1.
DR SUPFAM; SSF49410; SSF49410; 1.
DR SUPFAM; SSF81296; SSF81296; 1.
DR PROSITE; PS00477; ALPHA_2_MACROGLOBULIN; 1.
PE 1: Evidence at protein level;
KW Bait region; Complete proteome; Disulfide bond; Glycoprotein;
KW Polymorphism; Protease inhibitor; Reference proteome; Secreted;
KW Serine protease inhibitor; Signal; Thioester bond.
FT SIGNAL 1 17 Potential.
FT CHAIN 18 1454 Alpha-2-macroglobulin-like protein 1.
FT /FTId=PRO_0000318074.
FT REGION 695 726 Bait region.
FT CARBOHYD 120 120 N-linked (GlcNAc...) (Potential).
FT CARBOHYD 281 281 N-linked (GlcNAc...) (Potential).
FT CARBOHYD 409 409 N-linked (GlcNAc...) (Potential).
FT CARBOHYD 857 857 N-linked (GlcNAc...) (Potential).
FT CARBOHYD 1020 1020 N-linked (GlcNAc...) (Potential).
FT DISULFID 40 78 By similarity.
FT DISULFID 241 291 By similarity.
FT DISULFID 259 279 By similarity.
FT DISULFID 464 557 By similarity.
FT DISULFID 589 769 By similarity.
FT DISULFID 819 847 By similarity.
FT DISULFID 845 881 By similarity.
FT DISULFID 919 1307 By similarity.
FT DISULFID 1075 1123 By similarity.
FT DISULFID 1338 1453 By similarity.
FT CROSSLNK 970 973 Isoglutamyl cysteine thioester (Cys-Gln)
FT (By similarity).
FT VARIANT 207 207 G -> R (in dbSNP:rs11047499).
FT /FTId=VAR_055463.
FT VARIANT 850 850 D -> E (in dbSNP:rs1860926).
FT /FTId=VAR_059083.
FT VARIANT 970 970 C -> Y (in dbSNP:rs1558526).
FT /FTId=VAR_055464.
FT VARIANT 1131 1131 T -> M (in dbSNP:rs7959680).
FT /FTId=VAR_055465.
FT VARIANT 1229 1229 H -> R (in dbSNP:rs10219561).
FT /FTId=VAR_059084.
FT VARIANT 1412 1412 T -> A (in dbSNP:rs7315591).
FT /FTId=VAR_055466.
FT CONFLICT 733 733 F -> L (in Ref. 1; BAC85654/BAF83044).
FT CONFLICT 748 748 G -> E (in Ref. 2; AL832139).
FT CONFLICT 1122 1122 R -> W (in Ref. 1; BAC04793/BAC85653/
FT BAC85654/BAF83044 and 2; AL832139).
FT CONFLICT 1150 1150 M -> I (in Ref. 1; BAF83044).
FT CONFLICT 1248 1248 L -> P (in Ref. 1; BAC85654).
FT CONFLICT 1257 1257 M -> V (in Ref. 1; BAC04793/BAC85653/
FT BAC85654/BAF83044 and 2; AL832139).
FT CONFLICT 1452 1452 P -> L (in Ref. 2; AL832139).
SQ SEQUENCE 1454 AA; 161107 MW; 15ED65D000834E33 CRC64;
MWAQLLLGML ALSPAIAEEL PNYLVTLPAR LNFPSVQKVC LDLSPGYSDV KFTVTLETKD
KTQKLLEYSG LKKRHLHCIS FLVPPPAGGT EEVATIRVSG VGNNISFEEK KKVLIQRQGN
GTFVQTDKPL YTPGQQVYFR IVTMDSNFVP VNDKYSMVEL QDPNSNRIAQ WLEVVPEQGI
VDLSFQLAPE AMLGTYTVAV AEGKTFGTFS VEEYVLPKFK VEVVEPKELS TVQESFLVKI
CCRYTYGKPM LGAVQVSVCQ KANTYWYREV EREQLPDKCR NLSGQTDKTG CFSAPVDMAT
FDLIGYAYSH QINIVATVVE EGTGVEANAT QNIYISPQMG SMTFEDTSNF YHPNFPFSGK
IRVRGHDDSF LKNHLVFLVI YGTNGTFNQT LVTDNNGLAP FTLETSGWNG TDVSLEGKFQ
MEDLVYNPEQ VPRYYQNAYL HLRPFYSTTR SFLGIHRLNG PLKCGQPQEV LVDYYIDPAD
ASPDQEISFS YYLIGKGSLV MEGQKHLNSK KKGLKASFSL SLTFTSRLAP DPSLVIYAIF
PSGGVVADKI QFSVEMCFDN QVSLGFSPSQ QLPGAEVELQ LQAAPGSLCA LRAVDESVLL
LRPDRELSNR SVYGMFPFWY GHYPYQVAEY DQCPVSGPWD FPQPLIDPMP QGHSSQRSII
WRPSFSEGTD LFSFFRDVGL KILSNAKIKK PVDCSHRSPE YSTAMGAGGG HPEAFESSTP
LHQAEDSQVR QYFPETWLWD LFPIGNSGKE AVHVTVPDAI TEWKAMSFCT SQSRGFGLSP
TVGLTAFKPF FVDLTLPYSV VRGESFRLTA TIFNYLKDCI RVQTDLAKSH EYQLESWADS
QTSSCLCADD AKTHHWNITA VKLGHINFTI STKILDSNEP CGGQKGFVPQ KGRSDTLIKP
VLVKPEGVLV EKTHSSLLCP KGKVASESVS LELPVDIVPD STKAYVTVLG DIMGTALQNL
DGLVQMPSGC GEQNMVLFAP IIYVLQYLEK AGLLTEEIRS RAVGFLEIGY QKELMYKHSN
GSYSAFGERD GNGNTWLTAF VTKCFGQAQK FIFIDPKNIQ DALKWMAGNQ LPSGCYANVG
NLLHTAMKGG VDDEVSLTAY VTAALLEMGK DVDDPMVSQG LRCLKNSATS TTNLYTQALL
AYIFSLAGEM DIRNILLKQL DQQAIISGES IYWSQKPTPS SNASPWSEPA AVDVELTAYA
LLAQLTKPSL TQKEIAKATS IVAWLAKQHN AYGGFSSTQD TVVALQALAK YATTAYMPSE
EINLVVKSTE NFQRTFNIQS VNRLVFQQDT LPNVPGMYTL EASGQGCVYV QTVLRYNILP
PTNMKTFSLS VEIGKARCEQ PTSPRSLTLT IHTSYVGSRS SSNMAIVEVK MLSGFSPMEG
TNQLLLQQPL VKKVEFGTDT LNIYLDELIK NTQTYTFTIS QSVLVTNLKP ATIKVYDYYL
PDEQATIQYS DPCE
//
MIM
610627
*RECORD*
*FIELD* NO
610627
*FIELD* TI
*610627 ALPHA-2-MACROGLOBULIN-LIKE 1; A2ML1
*FIELD* TX
DESCRIPTION
The alpha-macroglobulin (AM) superfamily of proteins contains both
read morecomplement components and protease inhibitors, including A2M (103950)
and A2ML1. AM proteins display a unique trap mechanism of inhibition, by
which the AM inhibitor undergoes a major conformational change upon its
cleavage by a protease, thus trapping the protease and blocking it from
subsequent substrate binding (Galliano et al., 2006).
CLONING
By database analysis of an EST library generated from a large-scale
analysis of late-expressed genes in human epidermis, followed by RT-PCR
of an epidermis cDNA library, Galliano et al. (2006) cloned A2ML1. The
deduced 1454-amino acid protein contains an N-terminal 17-amino acid
signal sequence, a central bait domain, and a thiol ester sequence, and
maintains conservation of most of the Cys residues and glycosylation
sites seen in A2M. Northern blot analysis showed strong expression of a
5-kb transcript in epidermal granular keratinocytes, and RT-PCR analysis
showed expression in epidermis, placenta, thymus, and testis. Western
blot analysis detected A2ML1 as a monomeric 180-kD protein in human
epidermis. In vitro keratinocyte differentiation was associated with
increased A2ML1 expression levels. Immunohistochemistry on human skin
sections detected A2ML1 predominantly in the granular layer at the
apical edge of keratinocytes and also secreted into the extracellular
space between the upper granular and cornified layers. By database
analysis, Galliano et al. (2006) identified putative A2ML1 orthologs in
chimpanzee, dog, and pig but not mouse or rat.
GENE FUNCTION
Using a variety of enzymatic assays, Galliano et al. (2006) showed that
recombinant A2ML1 has inhibitory activity toward chymotrypsin, papain,
thermolysin, subtilisin A, and elastase. Incubation with chymotrypsin
and kallikrien-7 (KLK7; 604438) indicated that A2ML1 binds covalently to
these proteases.
GENE STRUCTURE
Galliano et al. (2006) determined that the A2ML1 gene contains 36 exons
spanning 54 kb.
MAPPING
Using genomic sequence analysis, Galliano et al. (2006) mapped the A2ML1
gene to chromosome 12p13.31, telomeric to AM family members A2M and PZP
(176420) but with the opposite orientation.
*FIELD* RF
1. Galliano, M.-F.; Toulza, E.; Gallinaro, H.; Jonca, N.; Ishida-Yamamoto,
A.; Serre, G.; Guerrin, M.: A novel protease inhibitor of the alpha-2-macroglobulin
family expressed in the human epidermis. J. Biol. Chem. 281: 5780-5789,
2006.
*FIELD* CD
Laura L. Baxter: 12/1/2006
*FIELD* ED
wwang: 12/01/2006
*RECORD*
*FIELD* NO
610627
*FIELD* TI
*610627 ALPHA-2-MACROGLOBULIN-LIKE 1; A2ML1
*FIELD* TX
DESCRIPTION
The alpha-macroglobulin (AM) superfamily of proteins contains both
read morecomplement components and protease inhibitors, including A2M (103950)
and A2ML1. AM proteins display a unique trap mechanism of inhibition, by
which the AM inhibitor undergoes a major conformational change upon its
cleavage by a protease, thus trapping the protease and blocking it from
subsequent substrate binding (Galliano et al., 2006).
CLONING
By database analysis of an EST library generated from a large-scale
analysis of late-expressed genes in human epidermis, followed by RT-PCR
of an epidermis cDNA library, Galliano et al. (2006) cloned A2ML1. The
deduced 1454-amino acid protein contains an N-terminal 17-amino acid
signal sequence, a central bait domain, and a thiol ester sequence, and
maintains conservation of most of the Cys residues and glycosylation
sites seen in A2M. Northern blot analysis showed strong expression of a
5-kb transcript in epidermal granular keratinocytes, and RT-PCR analysis
showed expression in epidermis, placenta, thymus, and testis. Western
blot analysis detected A2ML1 as a monomeric 180-kD protein in human
epidermis. In vitro keratinocyte differentiation was associated with
increased A2ML1 expression levels. Immunohistochemistry on human skin
sections detected A2ML1 predominantly in the granular layer at the
apical edge of keratinocytes and also secreted into the extracellular
space between the upper granular and cornified layers. By database
analysis, Galliano et al. (2006) identified putative A2ML1 orthologs in
chimpanzee, dog, and pig but not mouse or rat.
GENE FUNCTION
Using a variety of enzymatic assays, Galliano et al. (2006) showed that
recombinant A2ML1 has inhibitory activity toward chymotrypsin, papain,
thermolysin, subtilisin A, and elastase. Incubation with chymotrypsin
and kallikrien-7 (KLK7; 604438) indicated that A2ML1 binds covalently to
these proteases.
GENE STRUCTURE
Galliano et al. (2006) determined that the A2ML1 gene contains 36 exons
spanning 54 kb.
MAPPING
Using genomic sequence analysis, Galliano et al. (2006) mapped the A2ML1
gene to chromosome 12p13.31, telomeric to AM family members A2M and PZP
(176420) but with the opposite orientation.
*FIELD* RF
1. Galliano, M.-F.; Toulza, E.; Gallinaro, H.; Jonca, N.; Ishida-Yamamoto,
A.; Serre, G.; Guerrin, M.: A novel protease inhibitor of the alpha-2-macroglobulin
family expressed in the human epidermis. J. Biol. Chem. 281: 5780-5789,
2006.
*FIELD* CD
Laura L. Baxter: 12/1/2006
*FIELD* ED
wwang: 12/01/2006