IMPG2_HUMAN » Interphotoreceptor matrix proteoglycan 2

IMPG2_HUMAN » Interphotoreceptor matrix proteoglycan 2
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Topology in Plasma membrane
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IMPG2_HUMAN » Interphotoreceptor matrix proteoglycan 2 » Interphotoreceptor matrix proteoglycan of 200 kDa;IPM 200; Sialoprotein associated with cones and rods proteoglycan;Spacrcan;
Hydrophobic Thickness 34.8 ± 1.4 Å
Tilt Angle 0 ± 0°
ΔGtransfer -50.2 kcal/mol
ΔGfold -20.3 kcal/mol
Links UniProtKB, Pfam, Interpro, iHOP, STRING, HGNC, HMDB
Topology Out
TM Segments 1098-1127 (1098-1130)
Pathways none
PDB none
OPM none
Complexes none
Interactions none
Domains

AA: 241-335, PDBID: 2ACM, Subunit A, Seq Identity:29%, SEA domain

AA: 900-999, PDBID: 2ACM, Subunit A, Seq Identity:22%, SEA domain

UniProt annotation for IMPG2_HUMAN » Interphotoreceptor matrix proteoglycan 2
FUNCTION: Chondroitin sulfate- and hyaluronan-binding proteoglycan involved in the organization of interphotoreceptor matrix; may participate in the maturation and maintenance of the light- sensitive photoreceptor outer segment. Binds heparin.

TISSUE SPECIFICITY: Expressed in the retina. Expressed by photoreceptors of the interphotoreceptor matrix (IPM) surrounding both rods and cones. IPM occupies the subretinal space between the apices of the retinal pigment epithelium and the neural retina. Detected in the pineal gland.

DISEASE: Retinitis pigmentosa 56 (RP56) OMIM: A retinal dystrophy belonging to the group of pigmentary retinopathies. Retinitis pigmentosa is characterized by retinal pigment deposits visible on fundus examination and primary loss of rod photoreceptor cells followed by secondary loss of cone photoreceptors. Patients typically have night vision blindness and loss of midperipheral visual field. As their condition progresses, they lose their far peripheral visual field and eventually central vision as well. caused by mutations affecting the gene represented in this entry.

DISEASE: Macular dystrophy, vitelliform, 5 (VMD5) OMIM: A form of macular dystrophy, a retinal disease in which various forms of deposits, pigmentary changes, and atrophic lesions are observed in the macula lutea. Vitelliform macular dystrophies are characterized by yellow, lipofuscin-containing deposits, usually localized at the center of the macula. VMD5 features include late- onset moderate visual impairment and preservation of retinal pigment epithelium reflectivity. mutations affecting the gene represented in this entry.

UniProt features for IMPG2_HUMAN » Interphotoreceptor matrix proteoglycan 2
SIGNAL 1 22 Potential.
CHAIN 23 1241 Interphotoreceptor matrix proteoglycan 2.
DOMAIN 234 356 SEA 1.
DOMAIN 892 1011 SEA 2.
DOMAIN 1010 1051 EGF-like 1.
DOMAIN 1052 1093 EGF-like 2.
REGION 259 267 Hyaluronan-binding motif involved in chondroitin sulfate A-binding (By similarity).
REGION 1080 1088 Hyaluronan-binding motif involved in chondroitin sulfate C-binding (By similarity).
REGION 1125 1133 Hyaluronan-binding motif involved in chondroitin sulfate A- and C-binding (By similarity).
REGION 1136 1145 Hyaluronan-binding motif involved in chondroitin sulfate C-binding (By similarity).
REGION 1210 1218 Hyaluronan-binding motif involved in chondroitin sulfate A- and C-binding motif (By similarity).
DISULFID 1014 1025 By similarity.
DISULFID 1019 1036 By similarity.
DISULFID 1038 1050 By similarity.
DISULFID 1054 1067 By similarity.
DISULFID 1061 1077 By similarity.
DISULFID 1079 1092 By similarity.
Amino Acid Sequence for IMPG2_HUMAN » Interphotoreceptor matrix proteoglycan 2
MIMFPLFGKI SLGILIFVLI EGDFPSLTAQ TYLSIEEIQE PKSAVSFLLP EESTDLSLAT KKKQPLDRRE TERQWLIRRR RSILFPNGVK ICPDESVAEA VANHVKYFKV RVCQEAVWEA FRTFWDRLPG REEYHYWMNL CEDGVTSIFE MGTNFSESVE HRSLIMKKLT YAKETVSSSE LSSPVPVGDT STLGDTTLSV PHPEVDAYEG ASESSLERPE ESISNEIENV IEEATKPAGE QIAEFSIHLL GKQYREELQD SSSFHHQHLE EEFISEVENA FTGLPGYKEI RVLEFRSPKE NDSGVDVYYA VTFNGEAISN TTWDLISLHS NKVENHGLVE LDDKPTVVYT ISNFRDYIAE TLQQNFLLGN SSLNPDPDSL QLINVRGVLR HQTEDLVWNT QSSSLQATPS SILDNTFQAA WPSADESITS SIPPLDFSSG PPSATGRELW SESPLGDLVS THKLAFPSKM GLSSSPEVLE VSSLTLHSVT PAVLQTGLPV ASEERTSGSH LVEDGLANVE ESEDFLSIDS LPSSSFTQPV PKETIPSMED SDVSLTSSPY LTSSIPFGLD SLTSKVKDQL KVSPFLPDAS MEKELIFDGG LGSGSGQKVD LITWPWSETS SEKSAEPLSK PWLEDDDSLL PAEIEDKKLV LVDKMDSTDQ ISKHSKYEHD DRSTHFPEEE PLSGPAVPIF ADTAAESASL TLPKHISEVP GVDDYSVTKA PLILTSVAIS ASTDKSDQAD AILREDMEQI TESSNYEWFD SEVSMVKPDM QTLWTILPES ERVWTRTSSL EKLSRDILAS TPQSADRLWL SVTQSTKLPP TTISTLLEDE VIMGVQDISL ELDRIGTDYY QPEQVQEQNG KVGSYVEMST SVHSTEMVSV AWPTEGGDDL SYTQTSGALV VFFSLRVTNM MFSEDLFNKN SLEYKALEQR FLELLVPYLQ SNLTGFQNLE ILNFRNGSIV VNSRMKFANS VPPNVNNAVY MILEDFCTTA YNTMNLAIDK YSLDVESGDE ANPCKFQACN EFSECLVNPW SGEAKCRCFP GYLSVEERPC QSLCDLQPDF CLNDGKCDIM PGHGAICRCR VGENWWYRGK HCEEFVSEPV IIGITIASVV GLLVIFSAII YFFIRTLQAH HDRSERESPF SGSSRQPDSL SSIENAVKYN PVYESHRAGC EKYEGPYPQH PFYSSASGDV IGGLSREEIR QMYESSELSR EEIQERMRVL ELYANDPEFA AFVREQQVTE V