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Conserved domains on  [gi|57527403|ref|NP_001009690|]
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rod outer segment membrane protein 1 [Rattus norvegicus]

Protein Classification

peripherin_like_LEL domain-containing protein( domain architecture ID 10123579)

peripherin_like_LEL domain-containing protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
peripherin_like_LEL cd03162
Tetraspanin, extracellular domain or large extracellular loop (LEL), peripherin_like family. ...
 128-264 4.07e-79

Tetraspanin, extracellular domain or large extracellular loop (LEL), peripherin_like family. Tetraspanins are trans-membrane proteins with 4 trans-membrane segments. Both the N- and C-termini lie on the intracellular side of the membrane. This alignment model spans the extracellular domain between the 3rd and 4th trans-membrane segment. Tetraspanins are involved in diverse processes and their various functions may relate to their ability to act as molecular facilitators. Tetraspanins associate laterally with one another and cluster dynamically with numerous parnter domains in membrane microdomains, forming a network of multimolecular complexes, the "tetraspanin web". Peripherin, or RDS (retinal degradation slow) is a glycoprotein expressed in vertebrate photoreceptors, located at the rim of the disc membranes of the photoreceptor outer segments. RDS is thought to play a major role in folding and stacking of the discs. Mutations in RDS have been linked to hereditary retinal dystrophies, which typically exhibit a wide phenotypic spectrum.


:

Pssm-ID: 239415  Cd Length: 143  Bit Score: 238.49  E-value: 4.07e-79
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57527403 128 SLHQGLEEGLQAALAHYKDTEVPGHCQAKRLMDELQLRYHCCGRHGYKDWFGVQWVSSRYLDPNDQDVVDRIQSNVEGLY 207
Cdd:cd03162   6 SLEESLKTGLKNAMKFYKDTDTPGRCFLKKTIDMLQIEFQCCGNNGYRDWFEIQWISNRYLDFSSKEVKDRIKSNVDGRY 85

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 57527403 208 LIDGVPFSCCNPHSPRPCLQSQLSDPYAHPLFDPRQPNLNLWAQGCHEVLVGHLQGL 264
Cdd:cd03162  86 LTDGVPFSCCNPSSPRPCIQHQITDNSAHYNYDYQTEELNLWTRGCREALLEYYTSK 142
 
Name Accession Description Interval E-value
peripherin_like_LEL cd03162
Tetraspanin, extracellular domain or large extracellular loop (LEL), peripherin_like family. ...
 128-264 4.07e-79

Tetraspanin, extracellular domain or large extracellular loop (LEL), peripherin_like family. Tetraspanins are trans-membrane proteins with 4 trans-membrane segments. Both the N- and C-termini lie on the intracellular side of the membrane. This alignment model spans the extracellular domain between the 3rd and 4th trans-membrane segment. Tetraspanins are involved in diverse processes and their various functions may relate to their ability to act as molecular facilitators. Tetraspanins associate laterally with one another and cluster dynamically with numerous parnter domains in membrane microdomains, forming a network of multimolecular complexes, the "tetraspanin web". Peripherin, or RDS (retinal degradation slow) is a glycoprotein expressed in vertebrate photoreceptors, located at the rim of the disc membranes of the photoreceptor outer segments. RDS is thought to play a major role in folding and stacking of the discs. Mutations in RDS have been linked to hereditary retinal dystrophies, which typically exhibit a wide phenotypic spectrum.


Pssm-ID: 239415  Cd Length: 143  Bit Score: 238.49  E-value: 4.07e-79
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57527403 128 SLHQGLEEGLQAALAHYKDTEVPGHCQAKRLMDELQLRYHCCGRHGYKDWFGVQWVSSRYLDPNDQDVVDRIQSNVEGLY 207
Cdd:cd03162   6 SLEESLKTGLKNAMKFYKDTDTPGRCFLKKTIDMLQIEFQCCGNNGYRDWFEIQWISNRYLDFSSKEVKDRIKSNVDGRY 85

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 57527403 208 LIDGVPFSCCNPHSPRPCLQSQLSDPYAHPLFDPRQPNLNLWAQGCHEVLVGHLQGL 264
Cdd:cd03162  86 LTDGVPFSCCNPSSPRPCIQHQITDNSAHYNYDYQTEELNLWTRGCREALLEYYTSK 142
 
Name Accession Description Interval E-value
peripherin_like_LEL cd03162
Tetraspanin, extracellular domain or large extracellular loop (LEL), peripherin_like family. ...
 128-264 4.07e-79

Tetraspanin, extracellular domain or large extracellular loop (LEL), peripherin_like family. Tetraspanins are trans-membrane proteins with 4 trans-membrane segments. Both the N- and C-termini lie on the intracellular side of the membrane. This alignment model spans the extracellular domain between the 3rd and 4th trans-membrane segment. Tetraspanins are involved in diverse processes and their various functions may relate to their ability to act as molecular facilitators. Tetraspanins associate laterally with one another and cluster dynamically with numerous parnter domains in membrane microdomains, forming a network of multimolecular complexes, the "tetraspanin web". Peripherin, or RDS (retinal degradation slow) is a glycoprotein expressed in vertebrate photoreceptors, located at the rim of the disc membranes of the photoreceptor outer segments. RDS is thought to play a major role in folding and stacking of the discs. Mutations in RDS have been linked to hereditary retinal dystrophies, which typically exhibit a wide phenotypic spectrum.


Pssm-ID: 239415  Cd Length: 143  Bit Score: 238.49  E-value: 4.07e-79
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57527403 128 SLHQGLEEGLQAALAHYKDTEVPGHCQAKRLMDELQLRYHCCGRHGYKDWFGVQWVSSRYLDPNDQDVVDRIQSNVEGLY 207
Cdd:cd03162   6 SLEESLKTGLKNAMKFYKDTDTPGRCFLKKTIDMLQIEFQCCGNNGYRDWFEIQWISNRYLDFSSKEVKDRIKSNVDGRY 85

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 57527403 208 LIDGVPFSCCNPHSPRPCLQSQLSDPYAHPLFDPRQPNLNLWAQGCHEVLVGHLQGL 264
Cdd:cd03162  86 LTDGVPFSCCNPSSPRPCIQHQITDNSAHYNYDYQTEELNLWTRGCREALLEYYTSK 142
tetraspanin_LEL cd03127
Tetraspanin, extracellular domain or large extracellular loop (LEL). Tetraspanins are ...
 129-262 7.57e-12

Tetraspanin, extracellular domain or large extracellular loop (LEL). Tetraspanins are trans-membrane proteins with 4 trans-membrane segments. Both the N- and C-termini lie on the intracellular side of the membrane. This alignment model spans the extracellular domain between the 3rd and 4th trans-membrane segment. The tetraspanin family contains CD9, CD63, CD37, CD53, CD82, CD151, and CD81, amongst others. Tetraspanins are involved in diverse processes such as cell activation and proliferation, adhesion and motility, differentiation, cancer, and others. Their various functions may relate to their ability to act as molecular facilitators, grouping specific cell-surface proteins and affecting formation and stability of signaling complexes. Tetraspanins associate laterally with one another and cluster dynamically with numerous parnter domains in membrane microdomains, forming a network of multimolecular complexes, the "tetraspanin web", which may also include integrins.


Pssm-ID: 239401 [Multi-domain]  Cd Length: 90  Bit Score: 60.98  E-value: 7.57e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57527403 129 LHQGLEEGLQAALAHYKDTEvpghcQAKRLMDELQLRYHCCGRHGYKDWfgvqwvssryldpndqdvvdriqsnvegLYL 208
Cdd:cd03127   7 LESLVSDTLNDAWDEYYVDD-----DFQEAMDALQSTFECCGVNGPTDY----------------------------LDL 53

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....
gi 57527403 209 IDGVPFSCCNPHSPRPClqsqlsdpyahplfdprqpnLNLWAQGCHEVLVGHLQ 262
Cdd:cd03127  54 RLLVPSSCCKGTDGNCG--------------------LNLYTEGCLEKLVDFLR 87
CD151_like_LEL cd03155
Tetraspanin, extracellular domain or large extracellular loop (LEL), CD151_Like family. ...
 130-258 8.57e-08

Tetraspanin, extracellular domain or large extracellular loop (LEL), CD151_Like family. Tetraspanins are trans-membrane proteins with 4 trans-membrane segments. Both the N- and C-termini lie on the intracellular side of the membrane. This alignment model spans the extracellular domain between the 3rd and 4th trans-membrane segment. Tetraspanins are involved in diverse processes and their various functions may relate to their ability to act as molecular facilitators. Tetraspanins associate laterally with one another and cluster dynamically with numerous parnter domains in membrane microdomains, forming a network of multimolecular complexes, the "tetraspanin web". CD151strongly associates with integrins, especially alpha3beta1, alpha6beta1, alpha7beta1, and alpha6beta4; it may play roles in cell-cell adhesion, cell migration, platelet aggregation, and angiogenesis. For example, CD151 is is involved in regulation of migration of neutrophils, endothelial cells, and various tumor cell lines; it associates specifically with laminin-binding integrins and strengthens alpha6beta1 integrin-mediated adhesion to laminin-1; CD151 also specifically attenuates adhesion-dependent activation of Ras and correspdonding downstream effects, and is involved in epithelial cell-cell adhesion as a modulator of PKC- and Cdc42-dependent actin cytoskeletal reorganization.


Pssm-ID: 239408 [Multi-domain]  Cd Length: 110  Bit Score: 50.04  E-value: 8.57e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57527403 130 HQGLEEGLQAAL-----AHYKDTEVPGHCQAkrlMDELQLRYHCCGRHGYKDwfgvqWVSSRYldpndqdvvdrIQSNVE 204
Cdd:cd03155   4 YQQLEDELKESLkrtmqENYGQSGEEALTLT---VDELQQEFKCCGSNNYTD-----WQDSEW-----------INSNEA 64

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....
gi 57527403 205 GLYLidgVPFSCCNPHSPRPCLQSqlsdpyAHPlfdprqPNLNLWAQGCHEVLV 258
Cdd:cd03155  65 NGRL---VPDSCCKTVVDRCGCLR------DHP------SNIYKVEGGCIPKLE 103
penumbra_like_LEL cd03158
Tetraspanin, extracellular domain or large extracellular loop (LEL), penumbra_like family. ...
 133-217 1.52e-05

Tetraspanin, extracellular domain or large extracellular loop (LEL), penumbra_like family. Tetraspanins are trans-membrane proteins with 4 trans-membrane segments. Both the N- and C-termini lie on the intracellular side of the membrane. This alignment model spans the extracellular domain between the 3rd and 4th trans-membrane segment. Tetraspanins are involved in diverse processes and their various functions may relate to their ability to act as molecular facilitators. Tetraspanins associate laterally with one another and cluster dynamically with numerous parnter domains in membrane microdomains, forming a network of multimolecular complexes, the "tetraspanin web". Human Penumbra exhibits growth-suppressive activity in vitro and has been associated with myeloid malignancies.


Pssm-ID: 239411  Cd Length: 119  Bit Score: 43.83  E-value: 1.52e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57527403 133 LEEGLQAALAHYKDTEvpghcQAKRLMDELQLRYHCCGRHGYKDWfgvQWvsSRYLDPNDqdvvdriqSNVEGLylidGV 212
Cdd:cd03158  11 LEENIRKAIVHYYDDL-----DLQNIIDFVQKEFKCCGGDDYRDW---SK--NMYFNCSS--------PNPEAC----GV 68


                ....*
gi 57527403 213 PFSCC 217
Cdd:cd03158  69 PYSCC 73
TM4SF8_like_LEL cd03163
Tetraspanin, extracellular domain or large extracellular loop (LEL), TM4SF8_like subfamily. ...
 155-263 3.19e-05

Tetraspanin, extracellular domain or large extracellular loop (LEL), TM4SF8_like subfamily. Tetraspanins are trans-membrane proteins with 4 trans-membrane segments. Both the N- and C-termini lie on the intracellular side of the membrane. This alignment model spans the extracellular domain between the 3rd and 4th trans-membrane segment. Tetraspanins are involved in diverse processes and their various functions may relate to their ability to act as molecular facilitators. Tetraspanins associate laterally with one another and cluster dynamically with numerous parnter domains in membrane microdomains, forming a network of multimolecular complexes, the "tetraspanin web". This subfamily contaions transmembrane 4 superfamily 8 (TM4SF8) or Tspan-3 and related proteins. Tspan-3 has been reported to form a complex with integrin beta1 and OSP/claudin-11, which may be involved in oligodendrocyte proliferation and migration.


Pssm-ID: 239416  Cd Length: 105  Bit Score: 42.41  E-value: 3.19e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57527403 155 AKRLMDELQLRYHCCGRHGYKDWFGVQWVSSryldpndqdvvdriQSNveglyliDGVPFSCCNPhSPRPClQSQLSdpy 234
Cdd:cd03163  29 ESRAVDYLQRQLQCCGIHNYTDWENTPWFKE--------------SKN-------NSVPLSCCKE-TFTSC-TGSLT--- 82

                        90       100
                ....*....|....*....|....*....
gi 57527403 235 ahplfdprQPNLnLWAQGCHEVLVGHLQG 263
Cdd:cd03163  83 --------QPKD-LYQEGCEAKLVKKLQE 102
NET-5_like_LEL cd03165
Tetraspanin, extracellular domain or large extracellular loop (LEL), NET-5_like family. ...
 128-257 3.79e-05

Tetraspanin, extracellular domain or large extracellular loop (LEL), NET-5_like family. Tetraspanins are trans-membrane proteins with 4 trans-membrane segments. Both the N- and C-termini lie on the intracellular side of the membrane. This alignment model spans the extracellular domain between the 3rd and 4th trans-membrane segment. Tetraspanins are involved in diverse processes and their various functions may relate to their ability to act as molecular facilitators. Tetraspanins associate laterally with one another and cluster dynamically with numerous parnter domains in membrane microdomains, forming a network of multimolecular complexes, the "tetraspanin web". This sub-family contains proteins similar to human tetraspan NET-5.


Pssm-ID: 239418 [Multi-domain]  Cd Length: 98  Bit Score: 41.97  E-value: 3.79e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57527403 128 SLHQGLEEGLQAALAHYKDTEVPGHCQAkrlMDELQLRYHCCGRHGYKDWFGVQWVSSryldpndqdvvdriqsnvegly 207
Cdd:cd03165   6 KVDLTAKDDLKEGLELYGTRNNRGLTNA---WDITQTEFRCCGVTNYTDWYEVLGENR---------------------- 60

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|
gi 57527403 208 lidgVPFSCCNPHSPrPClqsqlsdpyahplfdPRQPNLNLWAQGCHEVL 257
Cdd:cd03165  61 ----VPDSCCQEDSQ-DC---------------GRNPTELWWKTGCYEKV 90
TM4SF2_6_like_LEL cd03161
Tetraspanin, extracellular domain or large extracellular loop (LEL), TM4SF2_6_like subfamily. ...
 132-261 8.80e-05

Tetraspanin, extracellular domain or large extracellular loop (LEL), TM4SF2_6_like subfamily. Tetraspanins are trans-membrane proteins with 4 trans-membrane segments. Both the N- and C-termini lie on the intracellular side of the membrane. This alignment model spans the extracellular domain between the 3rd and 4th trans-membrane segment. Tetraspanins are involved in diverse processes and their various functions may relate to their ability to act as molecular facilitators. Tetraspanins associate laterally with one another and cluster dynamically with numerous parnter domains in membrane microdomains, forming a network of multimolecular complexes, the "tetraspanin web". This subfamily contaions transmembrane 4 superfamily 2 (TM4SF2) or Tspan-7, transmembrane 4 superfamily 6 (TM4SF6) or Tspan-6, and related proteins. TM4SF2 has been identified as involved in some forms of X-linked mental retardation.


Pssm-ID: 239414  Cd Length: 104  Bit Score: 41.19  E-value: 8.80e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57527403 132 GLEEGLQAALAHYKDTEvpGHCQAkrlMDELQLRYHCCGRHGYKDWFGVQWvssryldpndqdvvdriqsnveglYLIDG 211
Cdd:cd03161  10 TFLRTYNEAVSNYNGDD--ERSDA---VDTVQRTLHCCGVENYTDWLNSPY------------------------FLEKG 60

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|
gi 57527403 212 VPFSCCNphSPRPCLQSQLSDPYAHPlfdprqpnLNLWAQGCHEvLVGHL 261
Cdd:cd03161  61 IPLSCCK--NRSDCSPQDLKNLTKAA--------TKVYQQGCFT-LVTSF 99
uroplakin_I_like_LEL cd03156
Tetraspanin, extracellular domain or large extracellular loop (LEL), uroplakin_I_like family. ...
 157-262 1.27e-04

Tetraspanin, extracellular domain or large extracellular loop (LEL), uroplakin_I_like family. Tetraspanins are trans-membrane proteins with 4 trans-membrane segments. Both the N- and C-termini lie on the intracellular side of the membrane. This alignment model spans the extracellular domain between the 3rd and 4th trans-membrane segment. Tetraspanins are involved in diverse processes and their various functions may relate to their ability to act as molecular facilitators. Tetraspanins associate laterally with one another and cluster dynamically with numerous parnter domains in membrane microdomains, forming a network of multimolecular complexes, the "tetraspanin web". Uroplakin Ia and Ib are components of the 16nm protein particles, which are packed hexagonally to form 2D crystals of asymmetric unit membranes, and cover the apical surface of mammalian urothelium, contributing to the urinay bladder's permeability barrier function. Uroplakins Ia and Ib are maturation facilitators. They trigger conformational changes in their single-transmembrane-domain binding partner proteins uroplakin II and IIIa, which in turn may lead to ER-exit, stabilization, and cell-surface expression.


Pssm-ID: 239409  Cd Length: 114  Bit Score: 40.98  E-value: 1.27e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 57527403 157 RLMDELQLRYHCCGRHGYKDWFGVQWVSSRYLDPNDQdvvdriqsnveglylidgVPFSCCnphspRPCLQSQLSDPYAH 236
Cdd:cd03156  33 STWNRVMIELKCCGVNGPTDFVDSTSFFRQKNEPNSP------------------YPESCC-----KRNSNSQIVDLDCP 89

                        90       100
                ....*....|....*....|....*.
gi 57527403 237 PLFDPRQPNLnlwaQGCHEVLVGHLQ 262
Cdd:cd03156  90 KLGSPNSYNK----KGCYEKLSNPIE 111
oculospanin_like_LEL cd03167
Tetraspanin, extracellular domain or large extracellular loop (LEL), oculospanin_like family. ...
 129-177 3.21e-03

Tetraspanin, extracellular domain or large extracellular loop (LEL), oculospanin_like family. Tetraspanins are trans-membrane proteins with 4 trans-membrane segments. Both the N- and C-termini lie on the intracellular side of the membrane. This alignment model spans the extracellular domain between the 3rd and 4th trans-membrane segment. Tetraspanins are involved in diverse processes and their various functions may relate to their ability to act as molecular facilitators. Tetraspanins associate laterally with one another and cluster dynamically with numerous parnter domains in membrane microdomains, forming a network of multimolecular complexes, the "tetraspanin web". This subfamily contains sequences similar to oculospanin, which is found to be expressed in retinal pigment epithelium, iris, ciliary body, and retinal ganglion cells.


Pssm-ID: 239420  Cd Length: 120  Bit Score: 37.06  E-value: 3.21e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*....
gi 57527403 129 LHQGLEEGLQAALAHYKDTEvpghcQAKRLMDELQLRYHCCGRHGYKDW 177
Cdd:cd03167   7 LQDGLEHTLRLAIAHYQDDP-----DLRFLIDQVQLGLQCCGASSYQDW 50
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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