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Disintegrin and metalloproteinase domain-containing protein 21 (ADAM 21) (EC 3.4.24.-) (Disintegrin and metalloproteinase domain-containing protein 31) (ADAM 31)

 ADA21_MOUSE             Reviewed;         729 AA.
Q9JI76; A2RSL1;
01-JUN-2001, integrated into UniProtKB/Swiss-Prot.
01-OCT-2000, sequence version 1.
28-FEB-2018, entry version 143.
RecName: Full=Disintegrin and metalloproteinase domain-containing protein 21;
Short=ADAM 21;
EC=3.4.24.-;
AltName: Full=Disintegrin and metalloproteinase domain-containing protein 31;
Short=ADAM 31;
Flags: Precursor;
Name=Adam21; Synonyms=Adam31;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=BALB/cJ; TISSUE=Bone marrow;
PubMed=10830287; DOI=10.1210/endo.141.6.7497;
Liu L., Smith J.W.;
"Identification of ADAM 31: a protein expressed in Leydig cells and
specialized epithelia.";
Endocrinology 141:2033-2042(2000).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J; TISSUE=Testis;
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Brain;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
-!- FUNCTION: May be involved in sperm maturation and/or
fertilization. May also be involved in epithelia functions
associated with establishing and maintaining gradients of ions or
nutrients.
-!- COFACTOR:
Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000305};
Note=Binds 1 zinc ion per subunit. {ECO:0000305};
-!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane
protein.
-!- TISSUE SPECIFICITY: Highly expressed in Leydig cells. Expressed
also in cauda epididymidis, vas deferens, convoluted tubules,
kidney and the parietal cells of stomach. Not detected on
developing spermatocytes or mature sperm.
-!- DOMAIN: A tripeptide motif (VGE) within disintegrin-like domain
could be involved in the binding to egg integrin receptor and thus
could mediate sperm/egg binding.
-!- DOMAIN: The cysteine-rich domain encodes putative cell-fusion
peptides, which could be involved in sperm-egg fusion.
-!- DOMAIN: The conserved cysteine present in the cysteine-switch
motif binds the catalytic zinc ion, thus inhibiting the enzyme.
The dissociation of the cysteine from the zinc ion upon the
activation-peptide release activates the enzyme.
-!- PTM: Has no obvious cleavage site for furin endopeptidase,
suggesting that the proteolytic processing is regulated.
{ECO:0000250}.
-----------------------------------------------------------------------
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EMBL; AF251559; AAF74731.1; -; mRNA.
EMBL; AK014827; BAB29569.1; -; mRNA.
EMBL; BC132152; AAI32153.1; -; mRNA.
EMBL; BC132344; AAI32345.1; -; mRNA.
CCDS; CCDS26022.1; -.
RefSeq; NP_065063.1; NM_020330.5.
UniGene; Mm.117130; -.
ProteinModelPortal; Q9JI76; -.
STRING; 10090.ENSMUSP00000008582; -.
MEROPS; M12.233; -.
iPTMnet; Q9JI76; -.
PhosphoSitePlus; Q9JI76; -.
PaxDb; Q9JI76; -.
PRIDE; Q9JI76; -.
Ensembl; ENSMUST00000008582; ENSMUSP00000008582; ENSMUSG00000008438.
GeneID; 56622; -.
KEGG; mmu:56622; -.
UCSC; uc007ock.1; mouse.
CTD; 8747; -.
MGI; MGI:1861229; Adam21.
eggNOG; KOG3607; Eukaryota.
eggNOG; ENOG410XX2M; LUCA.
GeneTree; ENSGT00910000144019; -.
HOGENOM; HOG000230883; -.
HOVERGEN; HBG006978; -.
InParanoid; Q9JI76; -.
KO; K08610; -.
OMA; FSQWKQI; -.
OrthoDB; EOG091G03BZ; -.
PhylomeDB; Q9JI76; -.
TreeFam; TF314733; -.
Reactome; R-MMU-1300644; Interaction With The Zona Pellucida.
PRO; PR:Q9JI76; -.
Proteomes; UP000000589; Chromosome 12.
Bgee; ENSMUSG00000008438; -.
CleanEx; MM_ADAM21; -.
Genevisible; Q9JI76; MM.
GO; GO:0030424; C:axon; IDA:MGI.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0043005; C:neuron projection; IDA:MGI.
GO; GO:0043025; C:neuronal cell body; IDA:MGI.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
CDD; cd04269; ZnMc_adamalysin_II_like; 1.
Gene3D; 3.40.390.10; -; 1.
Gene3D; 4.10.70.10; -; 1.
InterPro; IPR006586; ADAM_Cys-rich.
InterPro; IPR018358; Disintegrin_CS.
InterPro; IPR001762; Disintegrin_dom.
InterPro; IPR036436; Disintegrin_dom_sf.
InterPro; IPR013032; EGF-like_CS.
InterPro; IPR000742; EGF-like_dom.
InterPro; IPR024079; MetalloPept_cat_dom_sf.
InterPro; IPR001590; Peptidase_M12B.
InterPro; IPR002870; Peptidase_M12B_N.
InterPro; IPR034027; Reprolysin_adamalysin.
Pfam; PF08516; ADAM_CR; 1.
Pfam; PF00200; Disintegrin; 1.
Pfam; PF01562; Pep_M12B_propep; 1.
Pfam; PF01421; Reprolysin; 1.
PRINTS; PR00289; DISINTEGRIN.
SMART; SM00608; ACR; 1.
SMART; SM00050; DISIN; 1.
SUPFAM; SSF57552; SSF57552; 1.
PROSITE; PS50215; ADAM_MEPRO; 1.
PROSITE; PS00427; DISINTEGRIN_1; 1.
PROSITE; PS50214; DISINTEGRIN_2; 1.
PROSITE; PS01186; EGF_2; 1.
PROSITE; PS50026; EGF_3; 1.
PROSITE; PS00142; ZINC_PROTEASE; 1.
2: Evidence at transcript level;
Complete proteome; Disulfide bond; EGF-like domain; Glycoprotein;
Hydrolase; Membrane; Metal-binding; Metalloprotease; Protease;
Reference proteome; Signal; Transmembrane; Transmembrane helix; Zinc;
Zymogen.
SIGNAL 1 39 {ECO:0000255}.
PROPEP 40 209 {ECO:0000255}.
/FTId=PRO_0000029110.
CHAIN 210 729 Disintegrin and metalloproteinase domain-
containing protein 21.
/FTId=PRO_0000029111.
TOPO_DOM 210 685 Extracellular. {ECO:0000255}.
TRANSMEM 686 706 Helical. {ECO:0000255}.
TOPO_DOM 707 729 Cytoplasmic. {ECO:0000255}.
DOMAIN 212 402 Peptidase M12B. {ECO:0000255|PROSITE-
ProRule:PRU00276}.
DOMAIN 410 496 Disintegrin. {ECO:0000255|PROSITE-
ProRule:PRU00068}.
DOMAIN 638 667 EGF-like. {ECO:0000255|PROSITE-
ProRule:PRU00076}.
MOTIF 176 183 Cysteine switch. {ECO:0000250}.
COMPBIAS 497 639 Cys-rich.
ACT_SITE 346 346 {ECO:0000255|PROSITE-ProRule:PRU00276,
ECO:0000255|PROSITE-ProRule:PRU10095}.
METAL 178 178 Zinc; in inhibited form. {ECO:0000250}.
METAL 345 345 Zinc; catalytic. {ECO:0000255}.
METAL 349 349 Zinc; catalytic. {ECO:0000255}.
METAL 355 355 Zinc; catalytic. {ECO:0000255}.
CARBOHYD 169 169 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 231 231 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 381 381 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 441 441 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 482 482 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 320 397 {ECO:0000250}.
DISULFID 360 382 {ECO:0000250}.
DISULFID 362 367 {ECO:0000250}.
DISULFID 468 488 {ECO:0000250}.
DISULFID 638 649 {ECO:0000250}.
DISULFID 643 655 {ECO:0000250}.
DISULFID 657 666 {ECO:0000250}.
SEQUENCE 729 AA; 80850 MW; E70B79BC46B64549 CRC64;
MECFIMLGAD ARTLMRVTLL LLWLKALPSL IDLSQTGSTQ YLSSPEVVIP LKVTSRARGA
KNSEWLSYSL VFGGRRHVVH MRVKKLLVST HIPVLTYTEE HTPLSDYPFV PSDCYYHGYV
EGALESLVAF SACNGGLQGV LQMNGFSYEI EPIKHSSTFE HLVYTLNNNK TQFPPMLCSL
TEKRLLYQPF GVEEAKKSAM KQNYGKLWPH MWFLELAVVV DYGFFTNAQQ NLSKVRGDVV
LVVNMVDSMY KPLDTYVTLV GIEIWNRGNV LPMENIHQVL EDFSHWKQIS LSQVHHDAAH
IFIRSSLISV LGIAYIAGIC RPPLDCGVEN FQGDAWSLFA NTVAHELGHT FGMKHDEESC
SCGKSGCVMS TFRVPAERFT NCSYSDFMKT TLNQGTCLYN HPRPGAGFLV KRCGNGMVES
EEECDCGSVQ ECEQDPCCFL NCTLRPAAAC SFGLCCKDCK FMLLGELCRP KINECDLPEW
CNGTSHQCPE DGYVQDGVPC GAGAYCYQKQ CNNHDQQCRE IFGKGARSAS HNCYKEINLQ
GNRFGHCGTD GTVFLKCRMS DVFCGKVHCE NVEDIHHPQA PYVLQNIYAN GITCWSTGHC
LGMGVPDVGE VKDGTTCGVG KICLHKKCVS LSVLSNACLP ETCNRKGVCN NKHHCHCDYG
WSPPFCLHRG YGGSIDSGPT SQKRRVIITV LSITVPVLSI LICLLIAGLY RIYCKIPSGP
KETKASSPG


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