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Database: UniProt
Entry: Q28483
LinkDB: Q28483
Original site: Q28483 
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   19-MAR-2014, entry version 74.
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;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; 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-
RT   like, disintegrin-like, cysteine-rich (MDC) family of mammalian
RT   proteins and its 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
RT   distribution and processing in the male reproductive tract.";
RL   Mol. Hum. Reprod. 4:429-437(1998).
CC   -!- FUNCTION: This is a non catalytic metalloprotease-like protein.
CC       May play a role in sperm-egg fusion (By similarity).
CC   -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane
CC       protein (Potential).
CC   -!- TISSUE SPECIFICITY: Detected in testis (at protein level).
CC       Detected in adult and prepubertal testis. Detected at very low
CC       levels in heart, kidney, brain, muscle ovary and uterus.
CC   -!- DEVELOPMENTAL STAGE: Detected in elongate spermatids, and in caput
CC       and cauda epididymal spermatozoa (at protein level).
CC   -!- PTM: Subject to proteolytic processing during epididymal transit
CC       of spermatozoa.
CC   -!- SIMILARITY: Contains 1 disintegrin domain.
CC   -!- SIMILARITY: Contains 1 EGF-like domain.
CC   -!- SIMILARITY: Contains 1 peptidase M12B domain.
CC   -!- CAUTION: Not expected to have protease activity.
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DR   EMBL; X77619; CAA54713.1; -; mRNA.
DR   PIR; S47656; S47656.
DR   RefSeq; NP_001270657.1; NM_001283728.1.
DR   UniGene; Mfa.8590; -.
DR   ProteinModelPortal; Q28483; -.
DR   MEROPS; M12.953; -.
DR   GeneID; 101865559; -.
DR   HOVERGEN; HBG103628; -.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR   Gene3D; 3.40.390.10; -; 1.
DR   Gene3D; 4.10.70.10; -; 1.
DR   InterPro; IPR006586; ADAM_Cys-rich.
DR   InterPro; IPR001762; Blood-coag_inhib_Disintegrin.
DR   InterPro; IPR018358; Disintegrin_CS.
DR   InterPro; IPR000742; EG-like_dom.
DR   InterPro; IPR013032; EGF-like_CS.
DR   InterPro; IPR024079; MetalloPept_cat_dom.
DR   InterPro; IPR001590; Peptidase_M12B.
DR   InterPro; IPR002870; Peptidase_M12B_N.
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; Signal;
KW   Transmembrane; Transmembrane helix.
FT   SIGNAL        1     16       Potential.
FT   PROPEP       17    142       Potential.
FT                                /FTId=PRO_0000349299.
FT   CHAIN       143    756       Disintegrin and metalloproteinase domain-
FT                                containing protein 5.
FT                                /FTId=PRO_5000146218.
FT   TOPO_DOM     17    698       Extracellular (Potential).
FT   TRANSMEM    699    719       Helical; (Potential).
FT   TOPO_DOM    720    756       Cytoplasmic (Potential).
FT   DOMAIN      183    380       Peptidase M12B.
FT   DOMAIN      389    478       Disintegrin.
FT   DOMAIN      630    664       EGF-like.
FT   COMPBIAS    734    755       Ser-rich.
FT   CARBOHYD    559    559       N-linked (GlcNAc...) (Potential).
FT   DISULFID    292    375       By similarity.
FT   DISULFID    334    359       By similarity.
FT   DISULFID    336    341       By similarity.
FT   DISULFID    449    470       By similarity.
FT   DISULFID    634    646       By similarity.
FT   DISULFID    640    652       By similarity.
FT   DISULFID    654    663       By similarity.
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
//
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