MAMC2_MOUSE
ID MAMC2_MOUSE Reviewed; 686 AA.
AC Q8CG85; Q8BM24;
DT 13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 25-MAY-2022, entry version 120.
DE RecName: Full=MAM domain-containing protein 2;
DE AltName: Full=MAM domain-containing proteoglycan;
DE Short=Mamcan;
DE Flags: Precursor;
GN Name=Mamdc2;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Urinary bladder;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Czech II;
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 project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP GLYCOSYLATION, SUBCELLULAR LOCATION, AND DEVELOPMENTAL STAGE.
RX PubMed=18757743; DOI=10.1073/pnas.0803640105;
RA Manabe R., Tsutsui K., Yamada T., Kimura M., Nakano I., Shimono C.,
RA Sanzen N., Furutani Y., Fukuda T., Oguri Y., Shimamoto K., Kiyozumi D.,
RA Sato Y., Sado Y., Senoo H., Yamashina S., Fukuda S., Kawai J., Sugiura N.,
RA Kimata K., Hayashizaki Y., Sekiguchi K.;
RT "Transcriptome-based systematic identification of extracellular matrix
RT proteins.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:12849-12854(2008).
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC matrix {ECO:0000269|PubMed:18757743}.
CC -!- DEVELOPMENTAL STAGE: At 16.5 dpc, present in rib cartilage (at protein
CC level). {ECO:0000269|PubMed:18757743}.
CC -!- PTM: O-glycosylated; contains chondroitin sulfate.
CC {ECO:0000269|PubMed:18757743}.
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DR EMBL; AK035566; BAC29108.1; -; mRNA.
DR EMBL; BC042773; AAH42773.1; -; mRNA.
DR CCDS; CCDS29707.1; -.
DR RefSeq; NP_777282.1; NM_174857.3.
DR AlphaFoldDB; Q8CG85; -.
DR SMR; Q8CG85; -.
DR STRING; 10090.ENSMUSP00000045432; -.
DR GlyGen; Q8CG85; 3 sites.
DR iPTMnet; Q8CG85; -.
DR PhosphoSitePlus; Q8CG85; -.
DR MaxQB; Q8CG85; -.
DR PaxDb; Q8CG85; -.
DR PRIDE; Q8CG85; -.
DR ProteomicsDB; 292013; -.
DR DNASU; 71738; -.
DR GeneID; 71738; -.
DR KEGG; mmu:71738; -.
DR CTD; 256691; -.
DR MGI; MGI:1918988; Mamdc2.
DR eggNOG; ENOG502QVDI; Eukaryota.
DR InParanoid; Q8CG85; -.
DR OrthoDB; 270113at2759; -.
DR PhylomeDB; Q8CG85; -.
DR TreeFam; TF330345; -.
DR BioGRID-ORCS; 71738; 1 hit in 72 CRISPR screens.
DR ChiTaRS; Mamdc2; mouse.
DR PRO; PR:Q8CG85; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; Q8CG85; protein.
DR GO; GO:0005783; C:endoplasmic reticulum; ISO:MGI.
DR GO; GO:0031012; C:extracellular matrix; IDA:MGI.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR GO; GO:0005614; C:interstitial matrix; IDA:MGI.
DR GO; GO:0016020; C:membrane; IEA:InterPro.
DR GO; GO:0005539; F:glycosaminoglycan binding; IDA:MGI.
DR GO; GO:0019800; P:peptide cross-linking via chondroitin 4-sulfate glycosaminoglycan; IDA:MGI.
DR CDD; cd06263; MAM; 4.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR000998; MAM_dom.
DR Pfam; PF00629; MAM; 4.
DR PRINTS; PR00020; MAMDOMAIN.
DR SMART; SM00137; MAM; 4.
DR SUPFAM; SSF49899; SSF49899; 4.
DR PROSITE; PS00740; MAM_1; 2.
DR PROSITE; PS50060; MAM_2; 4.
PE 1: Evidence at protein level;
KW Extracellular matrix; Glycoprotein; Reference proteome; Repeat; Secreted;
KW Signal.
FT SIGNAL 1..18
FT /evidence="ECO:0000255"
FT CHAIN 19..686
FT /note="MAM domain-containing protein 2"
FT /id="PRO_0000014863"
FT DOMAIN 24..169
FT /note="MAM 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00128"
FT DOMAIN 168..329
FT /note="MAM 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00128"
FT DOMAIN 340..498
FT /note="MAM 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00128"
FT DOMAIN 507..666
FT /note="MAM 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00128"
FT REGION 665..686
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 134
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 329
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 524
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 17
FT /note="S -> N (in Ref. 1; BAC29108)"
FT /evidence="ECO:0000305"
FT CONFLICT 135
FT /note="T -> S (in Ref. 1; BAC29108)"
FT /evidence="ECO:0000305"
FT CONFLICT 203
FT /note="V -> I (in Ref. 1; BAC29108)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 686 AA; 77324 MW; C276B12A90226EAC CRC64;
MLLEGVLLVV QALQLASALD LPAGSCAFEE DTCGFDSVFA FLPWILNEEG HYVYMDTSFA
RQGEKAVLLS SDLQAEEWNC LRLVYQITTP PGSVSDPSQL NLYVRFEDES FDRLLWSTKE
PSDSWLIASL DLQNTSKKFK ILIEGVLGQG NTASIALFEI KMTAGYCIEC DFEENHLCGF
VNRWNPNVNW FVGGGTAKNT HSVLPQDHTF RSEHGHYMYV DSVYVKHFQE VAQLISPVTT
ASMSGCLSFY YQLQQGNDNV FSVYTRDMAG LYEEIWKVDS PGNAAWNLAE VEFSAPYPME
VIFEVAFNGP KGGYVALDDI SFSPVHCQNQ TGLPFSAVET SCDFEIGLCN FYQDKEGPGW
TRVRVKANMY RAGDHTTGTG HYLLANTKFT SQPGYIGRLY GPSLPGNMQY CVRFHYAIFG
FLKMSDTLAV YIFEENHVVQ EKIWSVLESP RGVWMQAEIS FKKPMPTKVV FMSLCKSFWD
CGLVALDDIT IQLGNCRSPA RLPPPPGECT FDQDECAFTQ EKRNRSSWHR GRGETPTSYT
GPKGDHTTGV GYYMYIEASH MVYGQKAHLL SQPLRGVPGK HCLTFFYHMY GAGTGLLSVY
LKREEDSEES LLWRRRGEQS ISWLRALVEY SCRRRHQIIF EATRGVSIRS DIAIDDVKLQ
AGPCAGMEDT TEQSSGYSED LNEIEY