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-APR-2013, entry version 69.
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 HSSP; P21859; 1J2L.
DR ProteinModelPortal; Q28483; -.
DR MEROPS; M12.953; -.
DR HOVERGEN; HBG103628; -.
DR GO; GO:0016021; C:integral to 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; Disintegrin; 1.
DR PROSITE; PS50215; ADAM_MEPRO; 1.
DR PROSITE; PS00427; DISINTEGRIN_1; 1.
DR PROSITE; PS50214; DISINTEGRIN_2; 1.
DR PROSITE; PS00022; EGF_1; FALSE_NEG.
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
//
