ADAM5_MACFA
ID ADAM5_MACFA Reviewed; 756 AA.
AC Q28483;
DT 02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 101.
DE RecName: Full=Disintegrin and metalloproteinase domain-containing protein 5;
DE AltName: Full=Transmembrane metalloproteinase-like, disintegrin-like, and cysteine-rich protein II;
DE Short=tMDC II;
DE Flags: Precursor;
GN Name=ADAM5; Synonyms=TMDC2;
OS Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Macaca.
OX NCBI_TaxID=9541;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Testis;
RX PubMed=8043604; DOI=10.1016/0167-4838(94)90062-0;
RA Perry A.C.F., Barker H.L., Jones R., Hall L.;
RT "Genetic evidence for an additional member of the metalloproteinase-like,
RT disintegrin-like, cysteine-rich (MDC) family of mammalian proteins and its
RT abundant expression in the testis.";
RL Biochim. Biophys. Acta 1207:134-137(1994).
RN [2]
RP TISSUE SPECIFICITY, PROTEOLYTIC PROCESSING, AND DEVELOPMENTAL STAGE.
RX PubMed=9665629; DOI=10.1093/molehr/4.5.429;
RA Frayne J., Jury J.A., Barker H.L., Perry A.C.F., Jones R., Hall L.;
RT "Macaque MDC family of proteins: sequence analysis, tissue distribution and
RT processing in the male reproductive tract.";
RL Mol. Hum. Reprod. 4:429-437(1998).
CC -!- FUNCTION: This is a non catalytic metalloprotease-like protein. May
CC play a role in sperm-egg fusion (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Interacts with TEX101. {ECO:0000250|UniProtKB:Q3TTE0}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I
CC membrane protein {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Detected in testis (at protein level). Detected in
CC adult and prepubertal testis. Detected at very low levels in heart,
CC kidney, brain, muscle ovary and uterus. {ECO:0000269|PubMed:9665629}.
CC -!- DEVELOPMENTAL STAGE: Detected in elongate spermatids, and in caput and
CC cauda epididymal spermatozoa (at protein level).
CC {ECO:0000269|PubMed:9665629}.
CC -!- PTM: Subject to proteolytic processing during epididymal transit of
CC spermatozoa. {ECO:0000269|PubMed:9665629}.
CC -!- CAUTION: Not expected to have protease activity. {ECO:0000305}.
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DR EMBL; X77619; CAA54713.1; -; mRNA.
DR PIR; S47656; S47656.
DR RefSeq; NP_001270657.1; NM_001283728.1.
DR AlphaFoldDB; Q28483; -.
DR SMR; Q28483; -.
DR STRING; 9541.XP_005563193.1; -.
DR MEROPS; M12.957; -.
DR GeneID; 101865559; -.
DR KEGG; mcf:101865559; -.
DR CTD; 255926; -.
DR eggNOG; KOG3607; Eukaryota.
DR OrthoDB; 162519at2759; -.
DR Proteomes; UP000233100; Unplaced.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:InterPro.
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; IPR000742; EGF-like_dom.
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 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.
DR PROSITE; PS01186; EGF_2; 1.
DR PROSITE; PS50026; EGF_3; 1.
PE 1: Evidence at protein level;
KW Disulfide bond; EGF-like domain; Glycoprotein; Membrane;
KW Reference proteome; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..16
FT /evidence="ECO:0000255"
FT PROPEP 17..142
FT /evidence="ECO:0000255"
FT /id="PRO_0000349299"
FT CHAIN 143..756
FT /note="Disintegrin and metalloproteinase domain-containing
FT protein 5"
FT /id="PRO_5000146218"
FT TOPO_DOM 17..698
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 699..719
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 720..756
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 183..380
FT /note="Peptidase M12B"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00276"
FT DOMAIN 389..478
FT /note="Disintegrin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00068"
FT DOMAIN 630..664
FT /note="EGF-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT REGION 731..756
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 732..756
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 559
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 292..375
FT /evidence="ECO:0000250"
FT DISULFID 334..359
FT /evidence="ECO:0000250"
FT DISULFID 336..341
FT /evidence="ECO:0000250"
FT DISULFID 449..470
FT /evidence="ECO:0000250"
FT DISULFID 634..646
FT /evidence="ECO:0000250"
FT DISULFID 640..652
FT /evidence="ECO:0000250"
FT DISULFID 654..663
FT /evidence="ECO:0000250"
SQ SEQUENCE 756 AA; 85043 MW; 4C6F932F1F462C25 CRC64;
MFLLLVLLTG LGGMHADLNP HKTFLQTTIP EKISSSDAKT DPEHNVVYMI TIEGKPYFVH
LKKQSILSSA SFIHSYDKND IRHSKPLLVQ MDCNYNGYVA GIPNSLVTLS VCSGLRGTMQ
LKNISYGIEP MEAVSGFIHK IYEEKFADTN ILLEENDTYS WFNSEYQVRK SSEKTDFIKL
FPRYIEMHIV VDKNLFDYMG SDINAVTQKV IQIIGLVNTM LTQLQLTVII SSIEIWSNKN
KISTTGHAEY VLLEFFEWKK DHLNFKPHQI AYLFVYRKLP TLIGATFPGQ VCNKDFAAAV
ALYPEGLSLE SYTVIIVQLL GLNLGLTYDK TDTCHCSGDV CTMTPKAVYS GGVKDFSVCS
LDDFKYISSH NGLTCLQTNP LEMPTYTQRR ICGNGLLEGG EECDCGNKDN CTHKLCCDAL
TCRLKDNAQC GSGDCCSKDC KFKPANTICR KSVDVECDFT EFCNGSYPYC LLDTYVRDGE
YCDSGGAFCF QGRCRTFDKQ CDDLIGRGSR GAPIFCYDEI NTRGDKFGNC GTEYCLFQHI
LCGKLVCTWE HKDLISRPNL SVIYAHVRDQ TCVSTYLPSR KPPPVASTVS KTSYYSVDDR
DETFVQDGSV CGPDMYCFKM RCKHVRFLMD FETCEASIEC SGHGICNNFN HCHCEKGYNP
PHCKPKKEAF GSTDDGHLVP AEKSYMEEGR HAPFQKQRFQ LIFYISLPVL IITTAILIKR
KKLRELCYRG ETESESSVSQ ESSSNSKSSL SESTSL
