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Protein

Usherin

Gene

Ush2A

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Involved in hearing and vision.By similarity

GO - Molecular functioni

  • collagen binding Source: MGI
  • myosin binding Source: MGI
  • protein homodimerization activity Source: MGI

GO - Biological processi

  • establishment of protein localization Source: MGI
  • hair cell differentiation Source: BHF-UCL
  • inner ear receptor cell differentiation Source: MGI
  • maintenance of animal organ identity Source: MGI
  • photoreceptor cell maintenance Source: MGI
  • response to stimulus Source: UniProtKB-KW
  • sensory perception of light stimulus Source: MGI
  • sensory perception of sound Source: MGI
  • visual perception Source: UniProtKB-KW
Complete GO annotation...

Keywords - Biological processi

Hearing, Sensory transduction, Vision

Names & Taxonomyi

Protein namesi
Recommended name:
Usherin
Alternative name(s):
Usher syndrome type IIa protein homolog
Usher syndrome type-2A protein homolog
Gene namesi
Name:Ush2A
Synonyms:Gm676
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 1

Organism-specific databases

MGIiMGI:1341292. Ush2a.

Subcellular locationi

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini35 – 5033ExtracellularSequence analysisAdd BLAST4999
Transmembranei5034 – 5054HelicalSequence analysisAdd BLAST21
Topological domaini5055 – 5193CytoplasmicSequence analysisAdd BLAST139

GO - Cellular componenti

  • apical plasma membrane Source: MGI
  • basement membrane Source: MGI
  • ciliary basal body Source: MGI
  • cytoplasm Source: MGI
  • integral component of membrane Source: UniProtKB-KW
  • periciliary membrane compartment Source: MGI
  • photoreceptor connecting cilium Source: MGI
  • photoreceptor inner segment Source: MGI
  • stereocilia ankle link Source: BHF-UCL
  • stereocilia ankle link complex Source: MGI
  • stereocilium bundle Source: MGI
  • stereocilium membrane Source: BHF-UCL
  • USH2 complex Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cell projection, Membrane, Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 34Sequence analysisAdd BLAST34
ChainiPRO_000022980535 – 5193UsherinAdd BLAST5159

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi230N-linked (GlcNAc...)Sequence analysis1
Glycosylationi258N-linked (GlcNAc...)Sequence analysis1
Glycosylationi274N-linked (GlcNAc...)Sequence analysis1
Glycosylationi358N-linked (GlcNAc...)Sequence analysis1
Glycosylationi415N-linked (GlcNAc...)Sequence analysis1
Glycosylationi448N-linked (GlcNAc...)Sequence analysis1
Glycosylationi469N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi515 ↔ 524By similarity
Disulfide bondi517 ↔ 533By similarity
Disulfide bondi535 ↔ 546By similarity
Disulfide bondi549 ↔ 569By similarity
Disulfide bondi572 ↔ 581By similarity
Disulfide bondi574 ↔ 602By similarity
Disulfide bondi605 ↔ 614By similarity
Disulfide bondi617 ↔ 635By similarity
Disulfide bondi638 ↔ 652By similarity
Disulfide bondi640 ↔ 659By similarity
Glycosylationi647N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi661 ↔ 670By similarity
Disulfide bondi673 ↔ 688By similarity
Disulfide bondi691 ↔ 705By similarity
Disulfide bondi693 ↔ 712By similarity
Disulfide bondi714 ↔ 723By similarity
Disulfide bondi726 ↔ 741By similarity
Disulfide bondi744 ↔ 756By similarity
Disulfide bondi746 ↔ 763By similarity
Disulfide bondi765 ↔ 774By similarity
Disulfide bondi777 ↔ 789By similarity
Disulfide bondi792 ↔ 805By similarity
Disulfide bondi794 ↔ 812By similarity
Disulfide bondi814 ↔ 823By similarity
Disulfide bondi826 ↔ 846By similarity
Glycosylationi836N-linked (GlcNAc...)Sequence analysis1
Glycosylationi853N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi867 ↔ 876By similarity
Disulfide bondi879 ↔ 894By similarity
Glycosylationi885N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi897 ↔ 910By similarity
Disulfide bondi899 ↔ 917By similarity
Disulfide bondi919 ↔ 928By similarity
Disulfide bondi931 ↔ 945By similarity
Glycosylationi941N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi948 ↔ 960By similarity
Disulfide bondi950 ↔ 967By similarity
Disulfide bondi969 ↔ 979By similarity
Disulfide bondi982 ↔ 996By similarity
Disulfide bondi999 ↔ 1011By similarity
Disulfide bondi1001 ↔ 1018By similarity
Glycosylationi1008N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi1020 ↔ 1029By similarity
Disulfide bondi1032 ↔ 1047By similarity
Glycosylationi1068N-linked (GlcNAc...)Sequence analysis1
Glycosylationi1089N-linked (GlcNAc...)Sequence analysis1
Glycosylationi1150N-linked (GlcNAc...)Sequence analysis1
Glycosylationi1171N-linked (GlcNAc...)Sequence analysis1
Glycosylationi1222N-linked (GlcNAc...)Sequence analysis1
Glycosylationi1382N-linked (GlcNAc...)Sequence analysis1
Glycosylationi1473N-linked (GlcNAc...)Sequence analysis1
Glycosylationi1626N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi1663 ↔ 1700By similarity
Glycosylationi1770N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi1853 ↔ 1882By similarity
Glycosylationi1894N-linked (GlcNAc...)Sequence analysis1
Glycosylationi1958N-linked (GlcNAc...)Sequence analysis1
Glycosylationi2095N-linked (GlcNAc...)Sequence analysis1
Glycosylationi2121N-linked (GlcNAc...)Sequence analysis1
Glycosylationi2177N-linked (GlcNAc...)Sequence analysis1
Glycosylationi2186N-linked (GlcNAc...)Sequence analysis1
Glycosylationi2249N-linked (GlcNAc...)Sequence analysis1
Glycosylationi2276N-linked (GlcNAc...)Sequence analysis1
Glycosylationi2313N-linked (GlcNAc...)Sequence analysis1
Glycosylationi2368N-linked (GlcNAc...)Sequence analysis1
Glycosylationi2404N-linked (GlcNAc...)Sequence analysis1
Glycosylationi2575N-linked (GlcNAc...)Sequence analysis1
Glycosylationi2647N-linked (GlcNAc...)Sequence analysis1
Glycosylationi2701N-linked (GlcNAc...)Sequence analysis1
Glycosylationi2761N-linked (GlcNAc...)Sequence analysis1
Glycosylationi2779N-linked (GlcNAc...)Sequence analysis1
Glycosylationi2928N-linked (GlcNAc...)Sequence analysis1
Glycosylationi2998N-linked (GlcNAc...)Sequence analysis1
Glycosylationi3023N-linked (GlcNAc...)Sequence analysis1
Glycosylationi3090N-linked (GlcNAc...)Sequence analysis1
Glycosylationi3208N-linked (GlcNAc...)Sequence analysis1
Glycosylationi3322N-linked (GlcNAc...)Sequence analysis1
Glycosylationi3411N-linked (GlcNAc...)Sequence analysis1
Glycosylationi3589N-linked (GlcNAc...)Sequence analysis1
Glycosylationi3645N-linked (GlcNAc...)Sequence analysis1
Glycosylationi3686N-linked (GlcNAc...)Sequence analysis1
Glycosylationi3712N-linked (GlcNAc...)Sequence analysis1
Glycosylationi3723N-linked (GlcNAc...)Sequence analysis1
Glycosylationi3772N-linked (GlcNAc...)Sequence analysis1
Glycosylationi3976N-linked (GlcNAc...)Sequence analysis1
Glycosylationi4063N-linked (GlcNAc...)Sequence analysis1
Glycosylationi4194N-linked (GlcNAc...)Sequence analysis1
Glycosylationi4218N-linked (GlcNAc...)Sequence analysis1
Glycosylationi4304N-linked (GlcNAc...)Sequence analysis1
Glycosylationi4340N-linked (GlcNAc...)Sequence analysis1
Glycosylationi4365N-linked (GlcNAc...)Sequence analysis1
Glycosylationi4410N-linked (GlcNAc...)Sequence analysis1
Glycosylationi4556N-linked (GlcNAc...)Sequence analysis1
Glycosylationi4575N-linked (GlcNAc...)Sequence analysis1
Glycosylationi4683N-linked (GlcNAc...)Sequence analysis1
Glycosylationi4716N-linked (GlcNAc...)Sequence analysis1
Glycosylationi4746N-linked (GlcNAc...)Sequence analysis1
Glycosylationi4756N-linked (GlcNAc...)Sequence analysis1
Glycosylationi4765N-linked (GlcNAc...)Sequence analysis1
Glycosylationi4915N-linked (GlcNAc...)Sequence analysis1
Glycosylationi4934N-linked (GlcNAc...)Sequence analysis1

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

PaxDbiQ2QI47.
PRIDEiQ2QI47.

PTM databases

iPTMnetiQ2QI47.
PhosphoSitePlusiQ2QI47.

Expressioni

Tissue specificityi

Present in the testis, epididymis, oviduct, spleen, submaxillary gland, and small and large intestines. Not detected in the brain, skin, lung, skeletal muscle, cardiac muscle, liver or kidney. Expressed in smooth muscle of the colon and the epididymis. Also present in select vascular basement membranes. In the cochlea, it is present in virtually every basement membrane. It is particularly high in the strial capillary basement membranes (SCBMs). In the retina, it is again expressed in all of the basement membranes. It is also very prevalent in the lens capsule and the Bruch's layer between the retinal pigment epithelium and the choroid layer, which is very rich in basement membranes. At postnatal day 0 in it is widely expressed in the basement membranes of the cochlea. Present in the synaptic terminals of retinal photoreceptors (at protein level).2 Publications

Gene expression databases

BgeeiENSMUSG00000026609.
ExpressionAtlasiQ2QI47. baseline and differential.

Interactioni

Subunit structurei

Interacts with collagen IV and fibronectin via its laminin EGF-like domains. Interaction with collagen may be required for stable integration into the basement membrane. Interacts with NINL (By similarity). Interacts with USH1C and WHRN. Interacts with PDZD7 (By similarity).By similarity

GO - Molecular functioni

  • collagen binding Source: MGI
  • myosin binding Source: MGI
  • protein homodimerization activity Source: MGI

Protein-protein interaction databases

BioGridi204466. 2 interactors.
STRINGi10090.ENSMUSP00000050454.

Structurei

3D structure databases

ProteinModelPortaliQ2QI47.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini268 – 514Laminin N-terminalPROSITE-ProRule annotationAdd BLAST247
Domaini515 – 571Laminin EGF-like 1PROSITE-ProRule annotationAdd BLAST57
Domaini572 – 637Laminin EGF-like 2PROSITE-ProRule annotationAdd BLAST66
Domaini638 – 690Laminin EGF-like 3PROSITE-ProRule annotationAdd BLAST53
Domaini691 – 743Laminin EGF-like 4PROSITE-ProRule annotationAdd BLAST53
Domaini744 – 791Laminin EGF-like 5PROSITE-ProRule annotationAdd BLAST48
Domaini792 – 848Laminin EGF-like 6PROSITE-ProRule annotationAdd BLAST57
Domaini853 – 896Laminin EGF-like 7PROSITE-ProRule annotationAdd BLAST44
Domaini897 – 947Laminin EGF-like 8PROSITE-ProRule annotationAdd BLAST51
Domaini948 – 998Laminin EGF-like 9PROSITE-ProRule annotationAdd BLAST51
Domaini999 – 1049Laminin EGF-like 10PROSITE-ProRule annotationAdd BLAST51
Domaini1055 – 1143Fibronectin type-III 1PROSITE-ProRule annotationAdd BLAST89
Domaini1147 – 1241Fibronectin type-III 2PROSITE-ProRule annotationAdd BLAST95
Domaini1242 – 1357Fibronectin type-III 3PROSITE-ProRule annotationAdd BLAST116
Domaini1358 – 1462Fibronectin type-III 4PROSITE-ProRule annotationAdd BLAST105
Domaini1463 – 1566Fibronectin type-III 5PROSITE-ProRule annotationAdd BLAST104
Domaini1511 – 1700Laminin G-like 1PROSITE-ProRule annotationAdd BLAST190
Domaini1705 – 1882Laminin G-like 2PROSITE-ProRule annotationAdd BLAST178
Domaini1847 – 1946Fibronectin type-III 6PROSITE-ProRule annotationAdd BLAST100
Domaini1948 – 2045Fibronectin type-III 7PROSITE-ProRule annotationAdd BLAST98
Domaini2046 – 2132Fibronectin type-III 8PROSITE-ProRule annotationAdd BLAST87
Domaini2133 – 2234Fibronectin type-III 9PROSITE-ProRule annotationAdd BLAST102
Domaini2235 – 2321Fibronectin type-III 10PROSITE-ProRule annotationAdd BLAST87
Domaini2322 – 2421Fibronectin type-III 11PROSITE-ProRule annotationAdd BLAST100
Domaini2422 – 2525Fibronectin type-III 12PROSITE-ProRule annotationAdd BLAST104
Domaini2526 – 2613Fibronectin type-III 13PROSITE-ProRule annotationAdd BLAST88
Domaini2617 – 2713Fibronectin type-III 14PROSITE-ProRule annotationAdd BLAST97
Domaini2717 – 2810Fibronectin type-III 15PROSITE-ProRule annotationAdd BLAST94
Domaini2811 – 2914Fibronectin type-III 16PROSITE-ProRule annotationAdd BLAST104
Domaini2918 – 3009Fibronectin type-III 17PROSITE-ProRule annotationAdd BLAST92
Domaini3013 – 3103Fibronectin type-III 18PROSITE-ProRule annotationAdd BLAST91
Domaini3395 – 3489Fibronectin type-III 20PROSITE-ProRule annotationAdd BLAST95
Domaini3490 – 3580Fibronectin type-III 21PROSITE-ProRule annotationAdd BLAST91
Domaini3581 – 3671Fibronectin type-III 22PROSITE-ProRule annotationAdd BLAST91
Domaini3672 – 3766Fibronectin type-III 23PROSITE-ProRule annotationAdd BLAST95
Domaini3769 – 3857Fibronectin type-III 24PROSITE-ProRule annotationAdd BLAST89
Domaini3858 – 3955Fibronectin type-III 25PROSITE-ProRule annotationAdd BLAST98
Domaini3956 – 4059Fibronectin type-III 26PROSITE-ProRule annotationAdd BLAST104
Domaini4060 – 4148Fibronectin type-III 27PROSITE-ProRule annotationAdd BLAST89
Domaini4149 – 4256Fibronectin type-III 28PROSITE-ProRule annotationAdd BLAST108
Domaini4257 – 4346Fibronectin type-III 29PROSITE-ProRule annotationAdd BLAST90
Domaini4347 – 4437Fibronectin type-III 30PROSITE-ProRule annotationAdd BLAST91
Domaini4438 – 4522Fibronectin type-III 31PROSITE-ProRule annotationAdd BLAST85
Domaini4523 – 4625Fibronectin type-III 32PROSITE-ProRule annotationAdd BLAST103
Domaini4628 – 4725Fibronectin type-III 33PROSITE-ProRule annotationAdd BLAST98
Domaini4726 – 4818Fibronectin type-III 34PROSITE-ProRule annotationAdd BLAST93
Domaini4819 – 4921Fibronectin type-III 35PROSITE-ProRule annotationAdd BLAST103
Domaini4922 – 5005Fibronectin type-III 36PROSITE-ProRule annotationAdd BLAST84

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi5191 – 5193PDZ-binding3

Domaini

The PDZ-binding motif probably mediates the association with some of the PDZ domains of USH1C and WHRN.By similarity

Sequence similaritiesi

Contains 36 fibronectin type-III domains.PROSITE-ProRule annotation
Contains 10 laminin EGF-like domains.PROSITE-ProRule annotation
Contains 2 laminin G-like domains.PROSITE-ProRule annotation
Contains 1 laminin N-terminal domain.PROSITE-ProRule annotation

Keywords - Domaini

Laminin EGF-like domain, Repeat, Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG1836. Eukaryota.
ENOG410Y1E5. LUCA.
GeneTreeiENSGT00840000129717.
HOGENOMiHOG000124780.
HOVERGENiHBG094138.
InParanoidiQ2QI47.
KOiK19636.
OMAiEIRIQAC.
OrthoDBiEOG091G003E.
TreeFamiTF330287.

Family and domain databases

CDDicd00063. FN3. 28 hits.
Gene3Di2.60.120.200. 3 hits.
2.60.40.10. 35 hits.
InterProiIPR013320. ConA-like_dom.
IPR003961. FN3_dom.
IPR013783. Ig-like_fold.
IPR006558. LamG-like.
IPR002049. Laminin_EGF.
IPR001791. Laminin_G.
IPR008211. Laminin_N.
IPR026915. USH2A.
[Graphical view]
PANTHERiPTHR10574:SF274. PTHR10574:SF274. 3 hits.
PfamiPF00041. fn3. 13 hits.
PF00053. Laminin_EGF. 10 hits.
PF00054. Laminin_G_1. 1 hit.
PF02210. Laminin_G_2. 1 hit.
PF00055. Laminin_N. 1 hit.
[Graphical view]
SMARTiSM00180. EGF_Lam. 10 hits.
SM00060. FN3. 34 hits.
SM00282. LamG. 2 hits.
SM00560. LamGL. 1 hit.
SM00136. LamNT. 1 hit.
[Graphical view]
SUPFAMiSSF49265. SSF49265. 22 hits.
SSF49899. SSF49899. 4 hits.
PROSITEiPS00022. EGF_1. 7 hits.
PS01248. EGF_LAM_1. 7 hits.
PS50027. EGF_LAM_2. 10 hits.
PS50853. FN3. 34 hits.
PS50025. LAM_G_DOMAIN. 2 hits.
PS51117. LAMININ_NTER. 1 hit.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 3 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q2QI47-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

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        10         20         30         40         50
MHYLALSPGF LCYTIKTLIL AYLASVLVLA ASQGVFPRLE NVGAFRKVST
60 70 80 90 100
VPTHATCGFP GPSTFCRSPV AAEHVQLCTE RLCIQDCPYR SASPLYTALL
110 120 130 140 150
EGLRSCIPAD DGDLHPYSRS SSVSFMFGSH QNCPSLRAPR LAAELTLAVW
160 170 180 190 200
LKLEQGGTMC VIEKTVDGQI VFKVTISEKE TMFYYRTVNG LQPPIKVMTP
210 220 230 240 250
GRILMKKWIH LTVQVHQTAI SFFVDGLEEN STAFDTRTLH DSVTDSVSSV
260 270 280 290 300
IQVGQSLNGS EQFVGRMQDF RLYNVSLTNR EILEVFSGDF PHLHIQPHCR
310 320 330 340 350
CPGSHPRVHP SVQQYCIPNG AGDTPEHRMS RLNPEAHPLS FINDDDVATS
360 370 380 390 400
WISHVFTNIT QLYEGVAISI DLENGQYQVL KVITQFSSLQ PVAIRIQRKK
410 420 430 440 450
ADSSPWEDWQ YFARNCSVWG MKDNEDLENP NSVNCLQLPD FIPFSHGNVT
460 470 480 490 500
FDLLTSGQKH RPGYNDFYNS SVLQEFMRAT QIRLHFHGQY YPAGHTVDWR
510 520 530 540 550
HQYYAVDEII VSGRCQCHGH AETCDRTRRP YRCLCSPHSF TEGPQCDRCS
560 570 580 590 600
PLYNDKPFRS GDNVNAFNCK PCQCHGHASS CHYDASVDPF PLEHNRGGGG
610 620 630 640 650
VCDDCQHHTT GRHCESCQDY FYRPVGADPA APDACKLCDC NRAGTRNGSL
660 670 680 690 700
HCDPIGGQCD CKRRVSGRQC LQCQDGFYDL QALDPDGCRP CNCNPSGTVD
710 720 730 740 750
GDITCHQNSG QCSCKANVIG LRCNRCNFGF KFLQSFNGDG CEPCQCNLHG
760 770 780 790 800
SVNQLCDPLS GQCACKKEAK GLKCDSCREN FYGLPWSACE VCDCSKAGSQ
810 820 830 840 850
PGTVCDTETG QCVCKPNVGG RQCSQCKAGY FNLYQNDSHL CLTCNCEKMG
860 870 880 890 900
TVNGSLRCDK STGQCPCKLG VTGLRCHQCK PHRFNLTMDN PQGCQACDCD
910 920 930 940 950
SLGTLPGSMC DPISGQCLCL PHRQGRRCEQ CQPGFYSSPS NATGCLPCLC
960 970 980 990 1000
HTAGAVSHIC NSVTGQCSCH DPSTTGRSCH QCQESYFRFD PLTGRCRPCH
1010 1020 1030 1040 1050
CHVAGASNGT CDAVTGQCFC KEFVTGSKCD TCVPGASHLD VNNLLGCSKT
1060 1070 1080 1090 1100
PSQQPPPRGW VQSSSTINVS WSPPECPNAH WLTYTLFRNG SEIYTTEDEH
1110 1120 1130 1140 1150
PYYTQYFLDT SLSPHTAYSY YIETSNVHSS TRSIPVIYET KPEVSEGHLN
1160 1170 1180 1190 1200
LTHIIPVGSD SITLTWTGLS NSSDPVAKYV LSCTPVDSTE PCVSYEGPET
1210 1220 1230 1240 1250
SATIWNLVPF TQYCFSVQGC TNESCFYSLP IIVTTAQAPP QTQGPPTVWK
1260 1270 1280 1290 1300
ISPTELRIEW SPPVDSNGII ISYELYMRRW LSTEESLVFE SHGLVSSHSA
1310 1320 1330 1340 1350
LQSVNPSKNL LQQPQASTFI SGLEPHTEYA FRVLAVNMAG RVSSAWASER
1360 1370 1380 1390 1400
TGESVPVFMA PPSVSPLSPH SLSVSWEKPA ENFTRGEIIG YKISMVSEHF
1410 1420 1430 1440 1450
PLHDVPVMCS KMVHFAKSQD QSYIVRGLEP YRTYSFTVSL CDSVGCVTSA
1460 1470 1480 1490 1500
LGSGQTLAAA PAQLRPPMVT GVNSTTVHIR WLPPAGVNGP PPLYHLERKK
1510 1520 1530 1540 1550
SSLPAATAAV TKGTRFVGHG YCRFPRTAHA DFIGIKASFR TRVPEGLILL
1560 1570 1580 1590 1600
ALSPGDQEEY FTLQLKNGRP YFLYNSQGTL VEVTPTDDPS QGYRDGEWHE
1610 1620 1630 1640 1650
IIAVRHQAFG QITLDGQYTG SSSSLNGSSV TGGYTGLFVG GVPQGHSVLQ
1660 1670 1680 1690 1700
KRLEIIQRGF VGCLKDVFIM KGYSPSGTWL PLDWQSSEEQ VNVHPSWEGC
1710 1720 1730 1740 1750
PTNLEEGVQF LGAGFLELPS DTFHAAKDFE ISLKFQTDQL NGLLLFIHNT
1760 1770 1780 1790 1800
EGPDFLAVEL KRGLLSFKFN SSLVFTRVDL RLGLADCDGK WNTVSIKKEG
1810 1820 1830 1840 1850
SVVSVRVNAL KKSTSQAGGQ PLLVNSPVYL GGIPRELQDA YRHLTLEPGF
1860 1870 1880 1890 1900
RGCVKEVAFA RGVVVNLASV SSRAVRVNQD GCLSSDSTVN CGGNDSILVY
1910 1920 1930 1940 1950
RGSQQSVYES GLQPFTEYLY RVTASHEGGA VSSDWSRGRT LGTAPQSVPT
1960 1970 1980 1990 2000
PSRAQSINGS SVEVAWNEPA VVKGVLEKYV LKAYSEDSSQ PRVPSASTEL
2010 2020 2030 2040 2050
HDTSTHSGVL IGLHPFHSYT VTLTACSRAG CTESSQALSI STPQEAPQEV
2060 2070 2080 2090 2100
QAPVAVALPN SLSFFWSLPR QANGIITQYS LYVDGRLVYT GKGQNYTVTD
2110 2120 2130 2140 2150
LRVFAAYEII VGACTQAGCT NSSQVILHTA QLPPEQVDPP GLTVLDSRTI
2160 2170 2180 2190 2200
HVRWKQPRQL NGILERYILY ILNPIHNSTM WSVVYNSTEK LQAHVLHHLS
2210 2220 2230 2240 2250
PGGLYLIRLR VCTGGGCTTS EPSQALMEET IPEGVPAPRA HSYSPDSFNI
2260 2270 2280 2290 2300
SWTEPEYPNG VITTYELYLD DTLIHNSSGL SCHAYGFDPG SLHTFQVQAC
2310 2320 2330 2340 2350
TAKGCALGPL VGNRTLEAPP EGVVNVLVKP EGSREAHVRW DAPAHPNGRL
2360 2370 2380 2390 2400
TYSVHFTGSF YADQAGDNYT LLSGTKTIRG IEGSRLWVLV DGLVPCSHYM
2410 2420 2430 2440 2450
VQVNASNSRG SVLSDPVSVE MPPGAPDGLL SPRLAAAAPT SLQVVWSTPA
2460 2470 2480 2490 2500
RNNAPGSPRY QLQMRPGPST HGRLELFPIP SASLSYEVTG LQPFTVYEFR
2510 2520 2530 2540 2550
LVATNGFGTA YSAWTPLMTT EDKPGPIDAP ILINVKARML SVIWRQPAKC
2560 2570 2580 2590 2600
NGAITHYNIY LHGRLYLTVS GRVTNYTVVP LHPYKAYHFQ VEACTSQGCS
2610 2620 2630 2640 2650
KSPSSETVWT LPGNPEGIPS PQLFPYTPTS IIVTWQPSAH LDLLVENVTI
2660 2670 2680 2690 2700
ERRVKGKKEV RNLVTLARSQ AMKFIDNDPA LRPWTRYEYR VLGSTLDGGT
2710 2720 2730 2740 2750
NSSAWVEVTT RPCRPSGVQP PTVRVLAPDT VEVSWKAPLM QNGDILSYEI
2760 2770 2780 2790 2800
RMPEPLIKMT NMSSIMLSHL VKHLIPFTNY SVTIVACSGG NGYLAGCTES
2810 2820 2830 2840 2850
PPTLATTHPA PPQELAPLSV ILLSESDVGI SWQPPSKPNG PNLRYELLRC
2860 2870 2880 2890 2900
KIQQPLASNP PEDLNLWHNI YSGTRWFYKD KGLSRFTTYE YKLFVHNSVG
2910 2920 2930 2940 2950
FTPSREVTVT TLAGSPERGA TVTASILNHT AIDVRWKKPT FQDLQGDVEY
2960 2970 2980 2990 3000
YTLFWSSGTS EESLKIFPDV DFHVIGQLSP NVEYQVFLLV FNGVHAINST
3010 3020 3030 3040 3050
VVHVTMWEEE PQGMLPPEVV IINSTAVRVI WTSPSNPNAV VTESSVYVNN
3060 3070 3080 3090 3100
KLYKTGTDAP GSFVLEDLSP FTIYDIQVEV CTKDACVKSN GTQVSTAEDT
3110 3120 3130 3140 3150
PSDISIPVIR GITSRSLQID WTTPANPNGI ILGYDVLRKT WRPCSETQKL
3160 3170 3180 3190 3200
TDKPRDELCK AVKCQYPGKV CGHTCYSPGT KVCCDGLLYD PQPGYSCCED
3210 3220 3230 3240 3250
KYIALSPNAT GVCCGGRMWE AQPDHQCCSG HYARILPGEI CCPDERHNRV
3260 3270 3280 3290 3300
SVGFGDACCG TMPYATSGSQ VCCAGRLQDG YRQQCCGGEM VSQDFQCCGG
3310 3320 3330 3340 3350
GEEGMVYSYL PGMLCCGQDY VNMSETICCS ASSGESKAHV RKDDPTPVKC
3360 3370 3380 3390 3400
CGTELSPESQ RCCDGVGYNP LKYVCSDEIS AGMAMKETRV CATICPATMK
3410 3420 3430 3440 3450
ATAHCGRCDF NATTHICTVM RGPLNPTGKK AVEGLCSAAE EIVHSGDVNT
3460 3470 3480 3490 3500
HSFIDRDLKP STVYEYRISA WNSYGRGFSQ SVRASTREDV PEGVKAPRWA
3510 3520 3530 3540 3550
RTGKHEDVIF LQWEEPMQSN GPIIHYILFR DGRERFQGTA LSFTDTQGIQ
3560 3570 3580 3590 3600
PLQEYSYQLK ACTAAGCAVS CKVVAATTQR SPENVPPPNI TAQSSETLHL
3610 3620 3630 3640 3650
SWSVPEKMKD AIKAYQLWLD GKGLIYTDTS DRRQHTVTGL QPYTNYSFTL
3660 3670 3680 3690 3700
AVCTSVGCTS SEPCVGQTLQ AAPQGVWVTP RHIIINSTTV ELYWNPPERP
3710 3720 3730 3740 3750
NGLISQYQLR RNGSLLLVGG RDNQSFTDSN LEPGSRYIYK LEARTGGGSS
3760 3770 3780 3790 3800
WSEDYLVQMP LWTPEDIHPP CNVTVLGSDS IFVAWPTPGN LLPKIPVEYS
3810 3820 3830 3840 3850
ILLSGGSVTL LVFSVRHRQS AHLKNLSPFT QYEIRIQACQ NGGCGVSPGT
3860 3870 3880 3890 3900
YVRTLEAAPV GLMPPLLKAL GSSCIEVKWM PPTRPNGIIT SYVVHRRPAD
3910 3920 3930 3940 3950
TEEESLLFVW SEGALEFTDD TGTLRPFTLY EYRVRAWNSQ GAVDSPWSTI
3960 3970 3980 3990 4000
QTLEAPPRGL PAPRVQATSA HSAMLNWTEP EAPNGLISQY HVIYQERPDA
4010 4020 4030 4040 4050
AAPGSSTVHA FTVTGTSRQA HLFGLEPFTT YHIGVVAVNS AGKVSSPWTL
4060 4070 4080 4090 4100
IKTLESAPSG LMNFTVEQRE KGRALLLQWS EPVKTNGVIK AYNIFNDGVL
4110 4120 4130 4140 4150
EYSGLGRQFL FRRLAPFTLY TLILEACTTA GCAHSVPQPL WTEEAPPDTQ
4160 4170 4180 4190 4200
MAPTIQSVGP TNVRLHWSQP ASPNGKIIHY EVIRRRSEEE DWGNTTWQAD
4210 4220 4230 4240 4250
GNTVFTEYNT QGNAWVYNDT GLQPWRQYAY RICAWNSAGH TCSSWNVVRT
4260 4270 4280 4290 4300
LQAPPDGLSP PEISYVSMSP LQLLISWLPP RHSNGVIQGY RLQRDGVLPA
4310 4320 4330 4340 4350
LNFNASTFSY MDSQLLPFST YSYAILACTG GGCCTSEPTN ITTPEVPPSE
4360 4370 4380 4390 4400
VSPPVLWDIS AHQMNVSWSP PSIPNGKIVK YLLQCDGEEH LAGQGLSFLL
4410 4420 4430 4440 4450
SNLQPSTQYN ISLVACTSGG CTASRTTSAW TKEAPPENMD PPTLHITGPE
4460 4470 4480 4490 4500
SIEITWTPPR NPHGLIRSYE LRRDGAIVYV GLETRYHDFT LAPGVEYSYS
4510 4520 4530 4540 4550
VTATNSRGSV LSPLVKGQTS PSAPSGLQPP KLHSGDALEL LADWDPPVRT
4560 4570 4580 4590 4600
NGKIINYTLF VREMFEGKTR AMSINTTHSS FGTRSLTVKH LKPFHRYEVR
4610 4620 4630 4640 4650
VQACTALGCT SSEWTSTQTS EVPPLRQPAP HLEVQTATGG FQPIVAVWWA
4660 4670 4680 4690 4700
GPLQPNGKII CFELYRRQVA AWPGTSSSLL IYNGSFRSFM DSELLPFTEY
4710 4720 4730 4740 4750
EYQVWAVNSA GKAASNWTRC RTGPAPPEGL QAPTFHTVSS TRAVVNISVP
4760 4770 4780 4790 4800
SRPNGNISLF RVFSNSSGTH VTLSEGTATQ QTLHDLSPFT TYTIGVEACT
4810 4820 4830 4840 4850
CFNCCSRGPT AELRTHPAPP SGLSPPQVQT LGSRMASVHW TPPLLPNGVI
4860 4870 4880 4890 4900
HSYELQLQRA CPPDSAPRCP PSHTERKYWG PGHRASLAGL QPNTAYGVQV
4910 4920 4930 4940 4950
VAYNEAGSTA SGWTNFSTKK EMPQYQALFS VDSNASMVWV DWSGTFLLNG
4960 4970 4980 4990 5000
HLKEYVVTDG GRRVYSGLDT TLYIPRMVDK IFFFQVTCTT DIGSVKTPLV
5010 5020 5030 5040 5050
QYDAATGSGL VLTTPGEKKG AGTKSTEFYS ELWFIMVMAV VGLILLAIFL
5060 5070 5080 5090 5100
SLILQRKIHK EPCIRERPPL VPLQKRMTPL SVYPPGETHV GLADTRLPRS
5110 5120 5130 5140 5150
GTPMSIRSSQ SVSVLRIPSQ SQLSHAYSQS SLHRSVSQLM DMADKKVVTE
5160 5170 5180 5190
DSLWETIMGH SSGLYVDEEE LMNAIKGFSS VTKEHTAFTD THL
Length:5,193
Mass (Da):569,660
Last modified:July 27, 2011 - v2
Checksum:i5579C5D8665CA121
GO
Isoform 2 (identifier: Q2QI47-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1460-1461: AP → GK
     1462-5193: Missing.

Show »
Length:1,461
Mass (Da):160,933
Checksum:i996D755F0347D01B
GO
Isoform 3 (identifier: Q2QI47-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     5090-5090: V → VFDSVADISDVSSNVTLKSYTMHFE

Show »
Length:5,217
Mass (Da):572,335
Checksum:i1E539052DAC0D406
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti78C → R in AAF70550 (PubMed:12160733).Curated1
Sequence conflicti78C → R in AAZ23164 (Ref. 2) Curated1
Sequence conflicti178E → D in AAF70550 (PubMed:12160733).Curated1
Sequence conflicti178E → D in AAZ23164 (Ref. 2) Curated1
Sequence conflicti206K → R in AAF70550 (PubMed:12160733).Curated1
Sequence conflicti206K → R in AAZ23164 (Ref. 2) Curated1
Sequence conflicti624P → S in AAF70550 (PubMed:12160733).Curated1
Sequence conflicti624P → S in AAZ23164 (Ref. 2) Curated1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_0177741460 – 1461AP → GK in isoform 2. 1 Publication2
Alternative sequenceiVSP_0177751462 – 5193Missing in isoform 2. 1 PublicationAdd BLAST3732
Alternative sequenceiVSP_0177765090V → VFDSVADISDVSSNVTLKSY TMHFE in isoform 3. Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF151717 mRNA. Translation: AAF70550.1.
DQ073638 mRNA. Translation: AAZ23164.1.
AC121799 Genomic DNA. No translation available.
AC121892 Genomic DNA. No translation available.
AC122122 Genomic DNA. No translation available.
AC129312 Genomic DNA. No translation available.
AC135863 Genomic DNA. No translation available.
AC165230 Genomic DNA. No translation available.
CCDSiCCDS15607.1. [Q2QI47-1]
RefSeqiNP_067383.3. NM_021408.3. [Q2QI47-1]
UniGeneiMm.331238.

Genome annotation databases

EnsembliENSMUST00000060479; ENSMUSP00000050454; ENSMUSG00000026609. [Q2QI47-1]
GeneIDi22283.
KEGGimmu:22283.
UCSCiuc007eae.1. mouse. [Q2QI47-2]
uc007eaf.1. mouse. [Q2QI47-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF151717 mRNA. Translation: AAF70550.1.
DQ073638 mRNA. Translation: AAZ23164.1.
AC121799 Genomic DNA. No translation available.
AC121892 Genomic DNA. No translation available.
AC122122 Genomic DNA. No translation available.
AC129312 Genomic DNA. No translation available.
AC135863 Genomic DNA. No translation available.
AC165230 Genomic DNA. No translation available.
CCDSiCCDS15607.1. [Q2QI47-1]
RefSeqiNP_067383.3. NM_021408.3. [Q2QI47-1]
UniGeneiMm.331238.

3D structure databases

ProteinModelPortaliQ2QI47.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi204466. 2 interactors.
STRINGi10090.ENSMUSP00000050454.

PTM databases

iPTMnetiQ2QI47.
PhosphoSitePlusiQ2QI47.

Proteomic databases

PaxDbiQ2QI47.
PRIDEiQ2QI47.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000060479; ENSMUSP00000050454; ENSMUSG00000026609. [Q2QI47-1]
GeneIDi22283.
KEGGimmu:22283.
UCSCiuc007eae.1. mouse. [Q2QI47-2]
uc007eaf.1. mouse. [Q2QI47-1]

Organism-specific databases

CTDi7399.
MGIiMGI:1341292. Ush2a.

Phylogenomic databases

eggNOGiKOG1836. Eukaryota.
ENOG410Y1E5. LUCA.
GeneTreeiENSGT00840000129717.
HOGENOMiHOG000124780.
HOVERGENiHBG094138.
InParanoidiQ2QI47.
KOiK19636.
OMAiEIRIQAC.
OrthoDBiEOG091G003E.
TreeFamiTF330287.

Miscellaneous databases

ChiTaRSiUsh2a. mouse.
PROiQ2QI47.
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000026609.
ExpressionAtlasiQ2QI47. baseline and differential.

Family and domain databases

CDDicd00063. FN3. 28 hits.
Gene3Di2.60.120.200. 3 hits.
2.60.40.10. 35 hits.
InterProiIPR013320. ConA-like_dom.
IPR003961. FN3_dom.
IPR013783. Ig-like_fold.
IPR006558. LamG-like.
IPR002049. Laminin_EGF.
IPR001791. Laminin_G.
IPR008211. Laminin_N.
IPR026915. USH2A.
[Graphical view]
PANTHERiPTHR10574:SF274. PTHR10574:SF274. 3 hits.
PfamiPF00041. fn3. 13 hits.
PF00053. Laminin_EGF. 10 hits.
PF00054. Laminin_G_1. 1 hit.
PF02210. Laminin_G_2. 1 hit.
PF00055. Laminin_N. 1 hit.
[Graphical view]
SMARTiSM00180. EGF_Lam. 10 hits.
SM00060. FN3. 34 hits.
SM00282. LamG. 2 hits.
SM00560. LamGL. 1 hit.
SM00136. LamNT. 1 hit.
[Graphical view]
SUPFAMiSSF49265. SSF49265. 22 hits.
SSF49899. SSF49899. 4 hits.
PROSITEiPS00022. EGF_1. 7 hits.
PS01248. EGF_LAM_1. 7 hits.
PS50027. EGF_LAM_2. 10 hits.
PS50853. FN3. 34 hits.
PS50025. LAM_G_DOMAIN. 2 hits.
PS51117. LAMININ_NTER. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiUSH2A_MOUSE
AccessioniPrimary (citable) accession number: Q2QI47
Secondary accession number(s): E9QLJ9, Q9JLP3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 4, 2006
Last sequence update: July 27, 2011
Last modified: November 30, 2016
This is version 97 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.